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Huang, P., Gao, W., Fu, C., Wang, M., Li, Y., Chu, B., He, A., Li, Y., Deng, X., Zhang, Y., Kong, Q., Yuan, J., Wang, H., Shi, Y., Gao, D., Qin, R., Hunter, T., Tian, R. Clinical functional proteomics of intercellular signalling in pancreatic cancer. (2024) Nature. DOI: 10.1038/s41586-024-08225-y

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Ning, J., Sala, M., Reina, J., Kalagiri, R., Hunter, T., McCullough, B.S. Histidine Phosphorylation: Protein Kinases and Phosphatases. (2024) Int J Mol Sci. 25(14). DOI: 10.3390/ijms25147975

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Rivier, C., Hunter, T., Evans, R.M. Roger Guillemin (1924 to 2024): Discoverer of brain hormones that control physiology. (2024) Proceedings of the National Academy of Sciences of the United States of America. 121(20):e2407309121. DOI: 10.1073/pnas.2407309121

Reina, J., Vallmajo-Martin, Q., Ning, J., Michi, A.N., Yeung, K., Wahl, G.M., Hunter, T. LHPP expression in triple-negative breast cancer promotes tumor growth and metastasis by modulating the tumor microenvironment. (2024) bioRxiv. DOI: 10.1101/2024.04.19.590151

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Chen, C.W., Su, C., Huang, C.Y., Huang, X.R., Cuili, X., Chao, T., Fan, C.H., Ting, C.W., Tsai, Y.W., Yang, K.C., Yeh, T.Y., Hsieh, S.T., Chen, Y.J., Feng, Y., Hunter, T., Chang, Z.F. NME3 is a gatekeeper for DRP1-dependent mitophagy in hypoxia. (2024) Nature Communications. 15(1):2264. DOI: 10.1038/s41467-024-46385-7

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Liang, G., Oh, T.G., Hah, N., Tiriac, H., Shi, Y., Truitt, M.L., Antal, C.E., Atkins, A.R., Li, Y., Fraser, C., Ng, S., Pinto, A.F.M., Nelson, D.C., Estepa, G., Bashi, S., Banayo, E., Dai, Y., Liddle, C., Yu, R.T., Hunter, T., Engle, D.D., Han, H., Von Hoff, D.D., Downes, M., Evans, R.M. Inhibiting stromal Class I HDACs curbs pancreatic cancer progression. (2023) Nature Communications. 14(1):7791. DOI: 10.1038/s41467-023-42178-6

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Lewis, B.M., Cho, C.Y., Her, H.L., Mizrahi, O., Hunter, T., Yeo, G.W. LARP4 Is an RNA-Binding Protein That Binds Nuclear-Encoded Mitochondrial mRNAs To Promote Mitochondrial Function. (2023) RNA. DOI: 10.1261/rna.079799.123

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Branch, M.R., Hsu, C.L., Ohnishi, K., Shen, W.C., Lee, E., Meisenhelder, J., Winborn, B., Sopher, B.L., Taylor, J.P., Hunter, T., La Spada, A.R. MAP4K3 inhibits Sirtuin-1 to repress the LKB1-AMPK pathway to promote amino acid-dependent activation of the mTORC1 complex. (2023) Life Sci Alliance. 6(8). DOI: 10.26508/lsa.202201525

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Chen, D., Varanasi, S.K., Hara, T., Traina, K., Sun, M., McDonald, B., Farsakoglu, Y., Clanton, J., Xu, S., Garcia-Rivera, L., Mann, T.H., Du, V., Chung, H.K., Xu, Z., Tripple, V., Casillas, E., Ma, S., O’Connor, C., Yang, Q., Zheng, Y., Hunter, T., Lemke, G., Kaech, S.M. CTLA-4 blockade induces CD4 T cell IFNγ-driven microglial phagocytosis and anti-tumor function in glioblastoma. (2023) Immunity. DOI: 10.1016/j.immuni.2023.07.015

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Gubbala, V.B., Jytosana, N., Trinh, V.Q., Maurer, H.C., Naeem, R.F., Lytle, N.K., Ma, Z., Zhao, S., Lin, W., Han, H., Shi, Y., Hunter, T., Singh, P.K., Olive, K.P., Tan, M.C.B., Kaech, S.M., Wahl, G.M., DelGiorno, K.E. Eicosanoids in the pancreatic tumor microenvironment – a multicellular, multifaceted progression. (2022) Gastro Hep Adv. 1(4):682-697. DOI: 10.1016/j.gastha.2022.02.007

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Hunter, T. A journey from phosphotyrosine to phosphohistidine and beyond. (2022) Molecular Cell. DOI: 10.1016/j.molcel.2022.05.007

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Taylor, S.S., Hunter, T., Changeux, J.P. A tribute to Eddy Fischer (April 6, 1920-August 27, 2021): Passionate biochemist and mentor. (2022) Proceedings of the National Academy of Sciences of the United States of America. 119(3). DOI: 10.1073/pnas.2121815119

Kalagiri, R., Hunter, T. The many ways that nature has exploited the unusual structural and chemical properties of phosphohistidine for use in proteins. (2021) Biochemical Journal. 478(19):3575-3596. DOI: 10.1042/BCJ20210533

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Hara, T., Chanoch-Myers, R., Mathewson, N.D., Myskiw, C., Atta, L., Bussema, L., Eichhorn, S.W., Greenwald, A.C., Kinker, G.S., Rodman, C., Gonzalez Castro, L.N., Wakimoto, H., Rozenblatt-Rosen, O., Zhuang, X., Fan, J., Hunter, T., Verma, I.M., Wucherpfennig, K.W., Regev, A., Suvà, M.L., Tirosh, I. Interactions between cancer cells and immune cells drive transitions to mesenchymal-like states in glioblastoma. (2021) Cancer Cell. DOI: 10.1016/j.ccell.2021.05.002

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Hunter, S.A., McIntosh, B.J., Shi, Y., Sperberg, R.A.P., Funatogawa, C., Labanieh, L., Soon, E., Wastyk, H.C., Mehta, N., Carter, C., Hunter, T., Cochran, J.R. An engineered ligand trap inhibits leukemia inhibitory factor as pancreatic cancer treatment strategy. (2021) Communications Biology. 4(1):452. DOI: 10.1038/s42003-021-01928-2

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Kalagiri, R., Stanfield, R.L., Meisenhelder, J., La Clair, J.J., Fuhs, S.R., Wilson, I.A., Hunter, T. Structural basis for differential recognition of phosphohistidine-containing peptides by 1-pHis and 3-pHis monoclonal antibodies. (2021) Proceedings of the National Academy of Sciences of the United States of America. 118(6). DOI: 10.1073/pnas.2010644118

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Ke, M., Yuan, X., He, A., Yu, P., Chen, W., Shi, Y., Hunter, T., Zou, P., Tian, R. Spatiotemporal profiling of cytosolic signaling complexes in living cells by selective proximity proteomics. (2021) Nature Communications. 12(1):71. DOI: 10.1038/s41467-020-20367-x

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French, M.E., Koehler, C.F., Hunter, T. Emerging functions of branched ubiquitin chains. (2021) Cell Discov. 7(1):6. DOI: 10.1038/s41421-020-00237-y

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Adam, K., Ning, J., Reina, J., Hunter, T. NME/NM23/NDPK and Histidine Phosphorylation. (2020) International Journal of Molecular Sciences. 21(16). DOI: 10.3390/ijms21165848

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Ogawa, J., Zhu, W., Tonnu, N., Singer, O., Hunter, T., Ryan, A.L., Pao, G.M. The D614G mutation in the SARS-CoV2 Spike protein increases infectivity in an ACE2 receptor dependent manner. (2020) bioRxiv. DOI: 10.1101/2020.07.21.214932

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Adam, K., Lesperance, J., Hunter, T., Zage, P.E. The Potential Functional Roles of NME1 Histidine Kinase Activity in Neuroblastoma Pathogenesis. (2020) International Journal of Molecular Sciences. 21(9). DOI: 10.3390/ijms21093319

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DelGiorno, K.E., Naeem, R.F., Fang, L., Chung, C.Y., Ramos, C., Luhtala, N., O’Connor, C., Hunter, T., Manor, U., Wahl, G.M. Tuft Cell Formation Reflects Epithelial Plasticity in Pancreatic Injury: Implications for Modeling Human Pancreatitis. (2020) Frontiers in Physiology. 11:88. DOI: 10.3389/fphys.2020.00088

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Adam, K., Hunter, T. Subcellular Localization of Histidine Phosphorylated Proteins Through Indirect Immunofluorescence. (2020) Methods in Molecular Biology. 2077:209-224. DOI: 10.1007/978-1-4939-9884-5_14

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Luhtala, N., Hunter, T. Immunohistochemistry (IHC): Chromogenic Detection of 3-Phosphohistidine Proteins in Formaldehyde-Fixed, Frozen Mouse Liver Tissue Sections. (2020) Methods in Molecular Biology. 2077:193-208. DOI: 10.1007/978-1-4939-9884-5_13

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Kalagiri, R., Adam, K., Hunter, T. Empirical Evidence of Cellular Histidine Phosphorylation by Immunoblotting Using pHis mAbs. (2020) Methods in Molecular Biology. 2077:Methods in Molecular Biology. DOI: 10.1007/978-1-4939-9884-5_12

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Sahai, E., Astsaturov, I., Cukierman, E., DeNardo, D.G., Egeblad, M., Evans, R.M., Fearon, D., Greten, F.R., Hingorani, S.R., Hunter, T., Hynes, R.O., Jain, R.K., Janowitz, T., Jorgensen, C., Kimmelman, A.C., Kolonin, M.G., Maki, R.G., Powers, R.S., Puré, E., Ramirez, D.C., Scherz-Shouval, R., Sherman, M.H., Stewart, S., Tlsty, T.D., Tuveson, D.A., Watt, F.M., Weaver, V., Weeraratna, A.T., Werb, Z. A framework for advancing our understanding of cancer-associated fibroblasts. (2020) Nature Reviews Cancer. DOI: 10.1038/s41568-019-0238-1

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Shi, Y., Hunter, S., Hunter, T. Stem Cell Factor LIFted as a Promising Clinical Target for Cancer Therapy. (2019) Molecular Cancer Therapeutics. 18(8):1337-1340. DOI: 10.1158/1535-7163.MCT-19-0605

Neftel, C., Laffy, J., Filbin, M.G., Hara, T., Shore, M.E., Rahme, G.J., Richman, A.R., Silverbush, D., Shaw, M.L., Hebert, C.M., Dewitt, J., Gritsch, S., Perez, E.M., Gonzalez Castro, L.N., Lan, X., Druck, N., Rodman, C., Dionne, D., Kaplan, A., Bertalan, M.S., Small, J., Pelton, K., Becker, S., Bonal, D., Nguyen, Q.D., Servis, R.L., Fung, J.M., Mylvaganam, R., Mayr, L., Gojo, J., Haberler, C., Geyeregger, R., Czech, T., Slavc, I., Nahed, B.V., Curry, W.T., Carter, B.S., Wakimoto, H., Brastianos, P.K., Batchelor, T.T., Stemmer-Rachamimov, A., Martinez-Lage, M., Frosch, M.P., Stamenkovic, I., Riggi, N., Rheinbay, E., Monje, M., Rozenblatt-Rosen, O., Cahill, D.P., Patel, A.P., Hunter, T., Verma, I.M., Ligon, K.L., Louis, D.N., Regev, A., Bernstein, B.E., Tirosh, I., Suvà, M.L. An Integrative Model of Cellular States, Plasticity, and Genetics for Glioblastoma. (2019) Cell. 178(4):835-849. DOI: 10.1016/j.cell.2019.06.024

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Shi, Y., Gao, W., Lytle, N.K., Huang, P., Yuan, X., Dann, A.M., Ridinger-Saison, M., DelGiorno, K.E., Antal, C.E., Liang, G., Atkins, A.R., Erikson, G., Sun, H., Meisenhelder, J., Terenziani, E., Woo, G., Fang, L., Santisakultarm, T.P., Manor, U., Xu, R., Becerra, C.R., Borazanci, E., Von Hoff, D.D., Grandgenett, P.M., Hollingsworth, M.A., Leblanc, M., Umetsu, S.E., Collisson, E.A., Scadeng, M., Lowy, A.M., Donahue, T.R., Reya, T., Downes, M., Evans, R.M., Wahl, G.M., Pawson, T., Tian, R., Hunter, T. Targeting LIF-mediated paracrine interaction for pancreatic cancer therapy and monitoring. (2019) Nature. 569(7754):131-135. DOI: 10.1038/s41586-019-1130-6

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Pancreatic ductal adenocarcinoma (PDAC) has a dismal prognosis largely owing to inefficient diagnosis and tenacious drug resistance. Activation of pancreatic stellate cells (PSCs) and consequent development of dense stroma are prominent features accounting for this aggressive biology. The reciprocal interplay between PSCs and pancreatic cancer cells (PCCs) not only enhances tumour progression and metastasis but also sustains their own activation, facilitating a vicious cycle to exacerbate tumorigenesis and drug resistance. Furthermore, PSC activation occurs very early during PDAC tumorigenesis, and activated PSCs comprise a substantial fraction of the tumour mass, providing a rich source of readily detectable factors. Therefore, we hypothesized that the communication between PSCs and PCCs could be an exploitable target to develop effective strategies for PDAC therapy and diagnosis. Here, starting with a systematic proteomic investigation of secreted disease mediators and underlying molecular mechanisms, we reveal that leukaemia inhibitory factor (LIF) is a key paracrine factor from activated PSCs acting on cancer cells. Both pharmacologic LIF blockade and genetic Lifr deletion markedly slow tumour progression and augment the efficacy of chemotherapy to prolong survival of PDAC mouse models, mainly by modulating cancer cell differentiation and epithelial-mesenchymal transition status. Moreover, in both mouse models and human PDAC, aberrant production of LIF in the pancreas is restricted to pathological conditions and correlates with PDAC pathogenesis, and changes in the levels of circulating LIF correlate well with tumour response to therapy. Collectively, these findings reveal a function of LIF in PDAC tumorigenesis, and suggest its translational potential as an attractive therapeutic target and circulating marker. Our studies underscore how a better understanding of cell-cell communication within the tumour microenvironment can suggest novel strategies for cancer therapy.

Bonanomi, D., Valenza, F., Chivatakarn, O., Sternfeld, M.J., Driscoll, S.P., Aslanian, A., Lettieri, K., Gullo, M., Badaloni, A., Lewcock, J.W., Hunter, T., Pfaff, S.L. p190RhoGAP Filters Competing Signals to Resolve Axon Guidance Conflicts. (2019) Neuron. DOI: 10.1016/j.neuron.2019.02.034

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Lamarche, B.J., Orazio, N.I., Goben, B., Meisenhelder, J., You, Z., Weitzman, M.D., Hunter, T. Repair of protein-linked DNA double strand breaks: Using the adenovirus genome as a model substrate in cell-based assays. (2018) DNA Repair. DOI: 10.1016/j.dnarep.2018.12.001

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The DNA double strand breaks (DSBs) created during meiotic recombination and during some types of chemotherapy contain protein covalently attached to their 5′ termini. Removal of the end-blocking protein is a prerequisite to DSB processing by non-homologous end-joining or homologous recombination. One mechanism for removing the protein involves CtIP-stimulated Mre11-catalyzed nicking of the protein-linked strand distal to the DSB terminus, releasing the end-blocking protein while it remains covalently attached to an oligonucleotide. Much of what is known about this repair process has recently been deciphered through in vitro reconstitution studies. We present here a novel model system based on adenovirus (Ad), which contains the Ad terminal protein covalently linked to the 5′ terminus of its dsDNA genome, for studying the repair of 5′ protein-linked DSBs in vivo. It was previously shown that the genome of Ad mutants that lack early region 4 (E4) can be joined into concatemers in vivo, suggesting that the Ad terminal protein had been removed from the genome termini prior to ligation. Here we show that during infection with the E4-deleted Ad mutant dl1004, the Ad terminal protein is removed in a manner that recapitulates removal of end-blocking proteins from cellular DSBs. In addition to displaying a dependence on CtIP, and Mre11 acting as the endonuclease, the protein-linked oligonucleotides that are released from the viral genome are similar in size to the oligos that remain attached to Spo11 and Top2 after they are removed from the 5′ termini of DSBs during meiotic recombination and etoposide chemotherapy, respectively. The single nucleotide resolution that is possible with this assay, combined with the single sequence context in which the lesion is presented, make it a useful tool for further refining our mechanistic understanding of how blocking proteins are removed from the 5′ termini of DSBs.

Chou, A.C., Aslanian, A., Sun, H., Hunter, T. An internal ribosome entry site in the coding region of tyrosyl-DNA phosphodiesterase 2 drives alternative translation start. (2018) Journal of Biological Chemistry. DOI: 10.1074/jbc.RA118.006269

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Luhtala, N., Hunter, T. Failure to detect functional transfer of active K-Ras protein from extracellular vesicles into recipient cells in culture. (2018) PLOS One. 13(9):e0203290. DOI: 10.1371/journal.pone.0203290

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Exosomes, extracellular nanovesicles that carry nucleic acids, lipids, and proteins, have been the subject of several studies to assess their ability to transfer functional cargoes to cells. We recently characterized extracellular nanovesicles released from glioblastoma cells that carry active Ras in complex with proteins regulating exosome biogenesis. Here, we investigated whether a functional transfer of Ras from exosomes to other cells can initiate intercellular signaling. We observed that treatment of serum-starved, cultured glioblastoma cells with exogenous glioblastoma exosomes caused a significant increase in cellular viability over time. Moreover, we detected fluorescent signal transfer from lipophilic dye-labeled exogenous glioblastoma exosomes into cultured glioblastoma cells. To probe possible signaling from cell-to-cell, we utilized bimolecular luciferase complementation to examine the ability of K-Ras in exosomes to interact with the Raf-Ras Binding domain (Raf-RBD) expressed in a recipient cell line. Although the K-Ras/Raf-RBD interaction was readily detectable upon co-expression in a single cell line, or following lysis of co-cultured cell lines separately expressing K-Ras and RBD, bearing in mind the limitations of our assay, we were unable to detect the interaction in the intact, co-cultured cell lines or upon treatment of the Raf-RBD-expressing cells with exosomes containing K-Ras. Furthermore, HA-Tag-BFP fused to the K-Ras hypervariable region and CAAX sequence failed to be transferred at significant levels from extracellular vesicles into recipient cells, but remained detectable in the cell supernatants even after 96 hours of culture of naïve cells with extracellular vesicles. We conclude that if transfer of functional K-Ras from extracellular vesicles into the cytoplasm of recipient cells occurs, it must do so at an extremely low efficiency and therefore is unlikely to initiate Ras-ERK MAP kinase pathway signaling. These results suggest that studies claiming functional transfer of protein cargoes from exosomes should be interpreted with caution.

Wang, Z., Wu, C., Aslanian, A., Yates, J.R., Hunter, T. Defective RNA polymerase III is negatively regulated by the SUMO-Ubiquitin-Cdc48 pathway. (2018) Elife. 7. DOI: 10.7554/eLife.35447

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Chu, B., He, A., Tian, Y., He, W., Chen, P., Hu, J., Xu, R., Zhou, W., Zhang, M., Yang, P., Li, S.S.C., Sun, Y., Li, P., Hunter, T., Tian, R. Photoaffinity-engineered protein scaffold for systematically exploring native phosphotyrosine signaling complexes in tumor samples. (2018) Proceedings of the National Academy of Sciences of the United States of America. 115(38)::E8863-E8872. DOI: 10.1073/pnas.1805633115

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Kim, Y., Zheng, X., Ansari, Z., Bunnell, M.C., Herdy, J.R., Traxler, L., Lee, H., Paquola, A.C.M., Blithikioti, C., Ku, M., Schlachetzki, J.C.M., Winkler, J., Edenhofer, F., Glass, C.K., Paucar, A.A., Jaeger, B.N., Pham, S., Boyer, L., Campbell, B.C., Hunter, T., Mertens, J., Gage, F.H. Mitochondrial Aging Defects Emerge in Directly Reprogrammed Human Neurons due to Their Metabolic Profile. (2018) Cell Reports. 23(9):2550-2558. DOI: 10.1016/j.celrep.2018.04.105

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Zhu, Q., Hoong, N., Aslanian, A., Hara, T., Benner, C., Heinz, S., Miga, K.H., Ke, E., Verma, S., Soroczynski, J., Yates, J.R., Hunter, T., Verma, I.M. Heterochromatin-Encoded Satellite RNAs Induce Breast Cancer. (2018) Molecular Cell. DOI: 10.1016/j.molcel.2018.04.023

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Hsu, C.L., Lee, E.X., Gordon, K.L., Paz, E.A., Shen, W.C., Ohnishi, K., Meisenhelder, J., Hunter, T., La Spada, A.R. MAP4K3 mediates amino acid-dependent regulation of autophagy via phosphorylation of TFEB. (2018) Nature Communications. 9(1):942. DOI: 10.1038/s41467-018-03340-7

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Hindupur, S.K., Colombi, M., Fuhs, S.R., Matter, M.S., Guri, Y., Adam, K., Cornu, M., Piscuoglio, S., Ng, C.K.Y., Betz, C., Liko, D., Quagliata, L., Moes, S., Jenoe, P., Terracciano, L.M., Heim, M.H., Hunter, T., Hall, M.N. The protein histidine phosphatase LHPP is a tumour suppressor. (2018) Nature. 555(7698):678-682. DOI: 10.1038/nature26140

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Settleman, J., Sawyers, C.L., Hunter, T. Challenges in validating candidate therapeutic targets in cancer. (2018) Elife. 7. DOI: 10.7554/eLife.32402

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Lu, Z., Hunter, T. Metabolic Kinases Moonlighting as Protein Kinases. (2018) Trends in Biochemical Sciences. 43(4):301-310. DOI: 10.1016/j.tibs.2018.01.006

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Adam, K., Hunter, T. Histidine kinases and the missing phosphoproteome from prokaryotes to eukaryotes. (2017) Lab. Invest. 98(2):233-247. DOI: 10.1038/labinvest.2017.118

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Protein phosphorylation is the most common type of post-translational modification in eukaryotes. The phosphoproteome is defined as the complete set of experimentally detectable phosphorylation sites present in a cell’s proteome under various conditions. However, we are still far from identifying all the phosphorylation sites in a cell mainly due to the lack of information about phosphorylation events involving residues other than Ser, Thr and Tyr. Four types of phosphate-protein linkage exist and these generate nine different phosphoresidues-pSer, pThr, pTyr, pHis, pLys, pArg, pAsp, pGlu and pCys. Most of the effort in studying protein phosphorylation has been focused on Ser, Thr and Tyr phosphorylation. The recent development of 1- and 3-pHis monoclonal antibodies promises to increase our understanding of His phosphorylation and the kinases and phosphatases involved. Several His kinases are well defined in prokaryotes, especially those involved in two-component system (TCS) signaling. However, in higher eukaryotes, NM23, a protein originally characterized as a nucleoside diphosphate kinase, is the only characterized protein-histidine kinase. This ubiquitous and conserved His kinase autophosphorylates its active site His, and transfers this phosphate either onto a nucleoside diphosphate or onto a protein His residue. Studies of NM23 protein targets using newly developed anti-pHis antibodies will surely help illuminate the elusive His phosphorylation-based signaling pathways. This review discusses the role that the NM23/NME/NDPK phosphotransferase has, how the addition of the pHis phosphoproteome will expand the phosphoproteome and make His phosphorylation part of the global phosphorylation world. It also summarizes why our understanding of phosphorylation is still largely restricted to the acid stable phosphoproteome, and highlights the study of NM23 histidine kinase as an entrée into the world of histidine phosphorylation.Laboratory Investigation advance online publication, 23 October 2017; doi:10.1038/labinvest.2017.118.

Paudyal, S.C., Li, S., Yan, H., Hunter, T., You, Z. Dna2 initiates resection at clean DNA double-strand breaks. (2017) Nucleic Acids Research. 45(20):11766-11781. DOI: 10.1093/nar/gkx830

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Hoppmann, C., Wong, A., Yang, B., Li, S., Hunter, T., Shokat, K.M., Wang, L. Site-specific incorporation of phosphotyrosine using an expanded genetic code. (2017) Nature Chemical Biology. 13(8):842-844. DOI: 10.1038/nchembio.2406

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French, M.E., Klosowiak, J.L., Aslanian, A., Reed, S.I., Yates, J.R., Hunter, T. Mechanism of ubiquitin chain synthesis employed by a HECT domain ubiquitin ligase. (2017) Journal of Biological Chemistry. 292(25):10398-10413. DOI: 10.1074/jbc.M117.789479

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Fuhs, S.R., Hunter, T. pHisphorylation: the emergence of histidine phosphorylation as a reversible regulatory modification. (2017) Current Opinion in Cell Biology. 45:8-16. DOI: 10.1016/j.ceb.2016.12.010

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Luhtala, N., Aslanian, A., Yates, J.R., Hunter, T. Secreted Glioblastoma Nanovesicles Contain Intracellular Signaling Proteins and Active Ras Incorporated in a Farnesylation-dependent Manner. (2017) Journal of Biological Chemistry. 292(2):611-628. DOI: 10.1074/jbc.M116.747618

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Srivastava, S., Panda, S., Li, Z., Fuhs, S.R., Hunter, T., Thiele, D.J., Hubbard, S.R., Skolnik, E.Y. Histidine phosphorylation relieves copper inhibition in the mammalian potassium channel KCa3.1. (2016) Elife. 5. DOI: 10.7554/eLife.16093

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Panda, S., Srivastava, S., Li, Z., Vaeth, M., Fuhs, S.R., Hunter, T., Skolnik, E.Y. Identification of PGAM5 as a Mammalian Protein Histidine Phosphatase that Plays a Central Role to Negatively Regulate CD4(+) T Cells. (2016) Molecular Cell. 63(3):457-69. DOI: 10.1016/j.molcel.2016.06.021

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Zheng, X., Boyer, L., Jin, M., Mertens, J., Kim, Y., Ma, L., Ma, L., Hamm, M., Gage, F.H., Hunter, T. Metabolic reprogramming during neuronal differentiation from aerobic glycolysis to neuronal oxidative phosphorylation. (2016) Elife. 5. DOI: 10.7554/eLife.13374

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Zheng, X., Boyer, L., Jin, M., Kim, Y., Fan, W., Bardy, C., Berggren, T., Evans, R.M., Gage, F.H., Hunter, T. Alleviation of neuronal energy deficiency by mTOR inhibition as a treatment for mitochondria-related neurodegeneration. (2016) Elife. 5. DOI: 10.7554/eLife.13378

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Li, X., Jiang, Y., Meisenhelder, J., Yang, W., Hawke, D.H., Zheng, Y., Xia, Y., Aldape, K., He, J., Hunter, T., Wang, L., Lu, Z. Mitochondria-Translocated PGK1 Functions as a Protein Kinase to Coordinate Glycolysis and the TCA Cycle in Tumorigenesis. (2016) Molecular Cell. 61(5):705-719. DOI: 10.1016/j.molcel.2016.02.009

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Marusiak, A.A., Stephenson, N.L., Baik, H., Trotter, E.W., Li, Y., Blyth, K., Mason, S., Chapman, P., Puto, L.A., Read, J.A., Brassington, C., Pollard, H.K., Phillips, C., Green, I., Overman, R., Collier, M., Testoni, E., Miller, C.J., Hunter, T., Sansom, O.J., Brognard, J. Recurrent MLK4 Loss-of-Function Mutations Suppress JNK Signaling to Promote Colon Tumorigenesis. (2016) Cancer Research. 76(3):724-35. DOI: 10.1158/0008-5472.CAN-15-0701-T

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Heimbucher, T., Hunter, T. The C. elegans Ortholog of USP7 controls DAF-16 stability in Insulin/IGF-1-like signaling. (2015) Worm. 4(4):e1103429. DOI: 10.1080/21624054.2015.1103429

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Denli, A.M., Narvaiza, I., Kerman, B.E., Pena, M., Benner, C., Marchetto, M.C., Diedrich, J.K., Aslanian, A., Ma, J., Moresco, J.J., Moore, L., Hunter, T., Saghatelian, A., Gage, F.H. Primate-specific ORF0 contributes to retrotransposon-mediated diversity. (2015) Cell. 163(3):583-93. DOI: 10.1016/j.cell.2015.09.025

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Zheng, X., Hunter, T. How phosphoubiquitin activates Parkin. (2015) Cell Research. 25(10):1087-8. DOI: 10.1038/cr.2015.97

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Carrano, A.C., Hunter, T. Fitting WWP-1 in the dietary restriction network. (2015) Cell Cycle. 14(10):1485-6. DOI: 10.1080/15384101.2015.1032642

Heimbucher, T., Liu, Z., Bossard, C., McCloskey, R., Carrano, A.C., Riedel, C.G., Tanasa, B., Klammt, C., Fonslow, B.R., Riera, C.E., Lillemeier, B.F., Kemphues, K., Yates, J.R., O’Shea, C.C., Hunter, T., Dillin, A. The Deubiquitylase MATH-33 Controls DAF-16 Stability and Function in Metabolism and Longevity. (2015) Cell Metabolism. 22(1):151-63. DOI: 10.1016/j.cmet.2015.06.002

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Fuhs, S.R., Meisenhelder, J., Aslanian, A., Ma, L., Zagorska, A., Stankova, M., Binnie, A., Al-Obeidi, F., Mauger, J., Lemke, G., Yates, J.R., Hunter, T. Monoclonal 1- and 3-Phosphohistidine Antibodies: New Tools to Study Histidine Phosphorylation. (2015) Cell. 162(1):198-210. DOI: 10.1016/j.cell.2015.05.046

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Hunter, T. Discovering the first tyrosine kinase. (2015) Proceedings of the National Academy of Sciences of the United States of America. 112(26):7877-82. DOI: 10.1073/pnas.1508223112

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Puto, L.A., Brognard, J., Hunter, T. Transcriptional Repressor DAXX Promotes Prostate Cancer Tumorigenicity via Suppression of Autophagy. (2015) Journal of Biological Chemistry. 290(25):15406-20. DOI: 10.1074/jbc.M115.658765

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Puto, L.A., Benner, C., Hunter, T. The DAXX co-repressor is directly recruited to active regulatory elements genome-wide to regulate autophagy programs in a model of human prostate cancer. (2015) Oncoscience. 2(4):362-72. DOI: 10.18632/oncoscience.152

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Tian, R., Wang, H., Gish, G.D., Petsalaki, E., Pasculescu, A., Shi, Y., Mollenauer, M., Bagshaw, R.D., Yosef, N., Hunter, T., Gingras, A.C., Weiss, A., Pawson, T. Combinatorial proteomic analysis of intercellular signaling applied to the CD28 T-cell costimulatory receptor. (2015) Proceedings of the National Academy of Sciences of the United States of America. 112(13):E1594-603. DOI: 10.1073/pnas.1503286112

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Antal, C.E., Hudson, A.M., Kang, E., Zanca, C., Wirth, C., Stephenson, N.L., Trotter, E.W., Gallegos, L.L., Miller, C.J., Furnari, F.B., Hunter, T., Brognard, J., Newton, A.C. Cancer-associated protein kinase C mutations reveal kinase’s role as tumor suppressor. (2015) Cell. 160(3):489-502. DOI: 10.1016/j.cell.2015.01.001

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Wilkinson, D.S., Jariwala, J.S., Anderson, E., Mitra, K., Meisenhelder, J., Chang, J.T., Ideker, T., Hunter, T., Nizet, V., Dillin, A., Hansen, M. Phosphorylation of LC3 by the Hippo kinases STK3/STK4 is essential for autophagy. (2015) Molecular Cell. 57(1):55-68. DOI: 10.1016/j.molcel.2014.11.019

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Basnet, H., Su, X.B., Tan, Y., Meisenhelder, J., Merkurjev, D., Ohgi, K.A., Hunter, T., Pillus, L., Rosenfeld, M.G. Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation. (2014) Nature. 516(7530):267-71. DOI: 10.1038/nature13736

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Thorner, J., Hunter, T., Cantley, L.C., Sever, R. Signal transduction: From the atomic age to the post-genomic era. (2014) Cold Spring Harbor Perspectives in Biology. 6(12):a022913. DOI: 10.1101/cshperspect.a022913

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Sherman, M.H., Yu, R.T., Engle, D.D., Ding, N., Atkins, A.R., Tiriac, H., Collisson, E.A., Connor, F., Van Dyke, T., Kozlov, S., Martin, P., Tseng, T.W., Dawson, D.W., Donahue, T.R., Masamune, A., Shimosegawa, T., Apte, M.V., Wilson, J.S., Ng, B., Lau, S.L., Gunton, J.E., Wahl, G.M., Hunter, T., Drebin, J.A., O’Dwyer, P.J., Liddle, C., Tuveson, D.A., Downes, M., Evans, R.M. Vitamin D receptor-mediated stromal reprogramming suppresses pancreatitis and enhances pancreatic cancer therapy. (2014) Cell. 159(1):80-93. DOI: 10.1016/j.cell.2014.08.007

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Lu, Z., Hunter, T. Prolyl isomerase Pin1 in cancer. (2014) Cell Research. 24(9):1033-49. DOI: 10.1038/cr.2014.109

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Zheng, X., Hunter, T. Pink1, the first ubiquitin kinase. (2014) EMBO Journal. 33(15):1621-3. DOI: 10.15252/embj.201489185

Sun, H., Liu, Y., Hunter, T. Multiple Arkadia/RNF111 structures coordinate its Polycomb body association and transcriptional control. (2014) Molecular and Cellular Biology. 34(16):2981-95. DOI: 10.1128/MCB.00036-14

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Yang, W., Xia, Y., Hawke, D., Li, X., Liang, J., Xing, D., Aldape, K., Hunter, T., Yung, W.K.A., Lu, Z. PKM2 Phosphorylates Histone H3 and Promotes Gene Transcription and Tumorigenesis. (2014) Cell. 158(5):1210. DOI: 10.1016/j.cell.2014.08.003

Ma, L., Aslanian, A., Sun, H., Jin, M., Shi, Y., Yates, J.R., Hunter, T. Identification of small ubiquitin-like modifier substrates with diverse functions using the Xenopus egg extract system. (2014) Molecular & Cellular Proteomics. 13(7):1659-75. DOI: 10.1074/mcp.M113.035626

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Carrano, A.C., Dillin, A., Hunter, T. A Krüppel-like factor downstream of the E3 ligase WWP-1 mediates dietary-restriction-induced longevity in Caenorhabditis elegans. (2014) Nature Communications. 5:3772. DOI: 10.1038/ncomms4772

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Voog, J., Sandall, S.L., Hime, G.R., Resende, L.P., Loza-Coll, M., Aslanian, A., Yates, J.R., Hunter, T., Fuller, M.T., Jones, D.L. Escargot restricts niche cell to stem cell conversion in the Drosophila testis. (2014) Cell Reports. 7(3):722-34. DOI: 10.1016/j.celrep.2014.04.025

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Hunter, T. The genesis of tyrosine phosphorylation. (2014) Cold Spring Harbor Perspectives in Biology. 6(5):a020644. DOI: 10.1101/cshperspect.a020644

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Aslanian, A., Yates, J.R., Hunter, T. Mass spectrometry-based quantification of the cellular response to methyl methanesulfonate treatment in human cells. (2014) DNA Repair. 15:29-38. DOI: 10.1016/j.dnarep.2013.12.007

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Faithful transmission of genetic material is essential for cell viability and organism health. The occurrence of DNA damage, due to either spontaneous events or environmental agents, threatens the integrity of the genome. The consequences of these insults, if allowed to perpetuate and accumulate over time, are mutations that can lead to the development of diseases such as cancer. Alkylation is a relevant DNA lesion produced endogenously as well as by exogenous agents including certain chemotherapeutics. We sought to better understand the cellular response to this form of DNA damage using mass spectrometry-based proteomics. For this purpose, we performed sub-cellular fractionation to monitor the effect of methyl methanesulfonate (MMS) treatment on protein localization to chromatin. The levels of over 500 proteins were increased in the chromatin-enriched nuclear lysate including histone chaperones. Levels of ubiquitin and subunits of the proteasome were also increased within this fraction, suggesting that ubiquitin-mediated degradation by the proteasome has an important role in the chromatin response to MMS treatment. Finally, the levels of some proteins were decreased within the chromatin-enriched lysate including components of the nuclear pore complex. Our spatial proteomics data demonstrate that many proteins that influence chromatin organization are regulated in response to MMS treatment, presumably to open the DNA to allow access by other DNA damage response proteins. To gain further insight into the cellular response to MMS-induced DNA damage, we also performed phosphorylation enrichment on total cell lysates to identify proteins regulated via post-translational modification. Phosphoproteomic analysis demonstrated that many nuclear phosphorylation events were decreased in response to MMS treatment. This reflected changes in protein kinase and/or phosphatase activity in response to DNA damage rather than changes in total protein abundance. Using these two mass spectrometry-based approaches, we have identified a novel set of MMS-responsive proteins that will expand our understanding of DNA damage signaling.

Zhang, Y., Hunter, T. Roles of Chk1 in cell biology and cancer therapy. (2014) International Journal of Cancer. 134(5):1013-23. DOI: 10.1002/ijc.28226

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Ma, H., Han, B.K., Guaderrama, M., Aslanian, A., Yates, J.R., Hunter, T., Wittenberg, C. Psy2 targets the PP4 family phosphatase Pph3 to dephosphorylate Mth1 and repress glucose transporter gene expression. (2014) Molecular and Cellular Biology. 34(3):452-63. DOI: 10.1128/MCB.00279-13

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Hunter, T. Retrospective. Tony Pawson (1952-2013). (2013) Science. 341(6150):1078. DOI: 10.1126/science.1244986

Zheng, X., Hunter, T. Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism. (2013) Cell Research. 23(7):886-97. DOI: 10.1038/cr.2013.66

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Hunter, T. Translating experience: thinking outside the box. (2013) Nature Cell Biology. 15(6):545. DOI: 10.1038/ncb2771

Sun, H., Hunter, T. Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string search. (2012) Journal of Biological Chemistry. 287(50):42071-83. DOI: 10.1074/jbc.M112.410985

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Lu, C.S., Truong, L.N., Aslanian, A., Shi, L.Z., Li, Y., Hwang, P.Y., Koh, K.H., Hunter, T., Yates, J.R., Berns, M.W., Wu, X. The RING finger protein RNF8 ubiquitinates Nbs1 to promote DNA double-strand break repair by homologous recombination. (2012) Journal of Biological Chemistry. 287(52):43984-94. DOI: 10.1074/jbc.M112.421545

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Zhu, W., Pao, G.M., Satoh, A., Cummings, G., Monaghan, J.R., Harkins, T.T., Bryant, S.V., Randal Voss, S., Gardiner, D.M., Hunter, T. Activation of germline-specific genes is required for limb regeneration in the Mexican axolotl. (2012) Developmental Biology. 370(1):42-51. DOI: 10.1016/j.ydbio.2012.07.021

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Zhang, Q.C., Petrey, D., Deng, L., Qiang, L., Shi, Y., Thu, C.A., Bisikirska, B., Lefebvre, C., Accili, D., Hunter, T., Maniatis, T., Califano, A., Honig, B. Structure-based prediction of protein-protein interactions on a genome-wide scale. (2012) Nature. 490(7421):556-60. DOI: 10.1038/nature11503

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Zhu, W., Kuo, D., Nathanson, J., Satoh, A., Pao, G.M., Yeo, G.W., Bryant, S.V., Voss, S.R., Gardiner, D.M., Hunter, T. Retrotransposon long interspersed nucleotide element-1 (LINE-1) is activated during salamander limb regeneration. (2012) Dev. Growth Differ. 54(7):673-85. DOI: 10.1111/j.1440-169X.2012.01368.x

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Hunter, T. Why nature chose phosphate to modify proteins. (2012) Philos. Trans. R. Soc. Lond., B, Biol. Sci. 367(1602):2513-6. DOI: 10.1098/rstb.2012.0013

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Hunter, T., Pawson, T. The evolution of protein phosphorylation. Preface. (2012) Philos. Trans. R. Soc. Lond., B, Biol. Sci. 367(1602):2512. DOI: 10.1098/rstb.2012.0374

Yang, W., Xia, Y., Hawke, D., Li, X., Liang, J., Xing, D., Aldape, K., Hunter, T., Alfred Yung, W.K., Lu, Z. PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis. (2012) Cell. 150(4):685-96. DOI: 10.1016/j.cell.2012.07.018

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Wang, Z., Shah, O.J., Hunter, T. The transcriptional coactivators p/CIP and SRC-1 control insulin resistance through IRS1 in obesity models. (2012) PLOS One. 7(7):e36961. DOI: 10.1371/journal.pone.0036961

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Chaurushiya, M.S., Lilley, C.E., Aslanian, A., Meisenhelder, J., Scott, D.C., Landry, S., Ticau, S., Boutell, C., Yates, J.R., Schulman, B.A., Hunter, T., Weitzman, M.D. Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain. (2012) Molecular Cell. 46(1):79-90. DOI: 10.1016/j.molcel.2012.02.004

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Brognard, J., Zhang, Y.W., Puto, L.A., Hunter, T. Cancer-associated loss-of-function mutations implicate DAPK3 as a tumor-suppressing kinase. (2011) Cancer Research. 71(8):3152-61. DOI: 10.1158/0008-5472.CAN-10-3543

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Brognard, J., Hunter, T. Protein kinase signaling networks in cancer. (2011) Current Opinion in Genetics & Development. 21(1):4-11. DOI: 10.1016/j.gde.2010.10.012

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Olson, B.J., Oberholzer, M., Li, Y., Zones, J.M., Kohli, H.S., Bisova, K., Fang, S.C., Meisenhelder, J., Hunter, T., Umen, J.G. Regulation of the Chlamydomonas cell cycle by a stable, chromatin-associated retinoblastoma tumor suppressor complex. (2010) Plant Cell. 22(10):3331-47. DOI: 10.1105/tpc.110.076067

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Yoon, Y.S., Lee, M.W., Ryu, D., Kim, J.H., Ma, H., Seo, W.Y., Kim, Y.N., Kim, S.S., Lee, C.H., Hunter, T., Choi, C.S., Montminy, M.R., Koo, S.H. Suppressor of MEK null (SMEK)/protein phosphatase 4 catalytic subunit (PP4C) is a key regulator of hepatic gluconeogenesis. (2010) Proceedings of the National Academy of Sciences of the United States of America. 107(41):17704-9. DOI: 10.1073/pnas.1012665107

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Liew, C.W., Sun, H., Hunter, T., Day, C.L. RING domain dimerization is essential for RNF4 function. (2010) Biochemical Journal. 431(1):23-9. DOI: 10.1042/BJ20100957

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Lu, Z., Hunter, T. Ubiquitylation and proteasomal degradation of the p21(Cip1), p27(Kip1) and p57(Kip2) CDK inhibitors. (2010) Cell Cycle. 9(12):2342-52. DOI: 10.4161/cc.9.12.11988

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López-Otín, C., Hunter, T. The regulatory crosstalk between kinases and proteases in cancer. (2010) Nature Reviews Cancer. 10(4):278-92. DOI: 10.1038/nrc2823

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Hunter, T., Marais, R. Genetic and cellular mechanisms of oncogenesis. (2010) Current Opinion in Genetics & Development. 20(1):1-3. DOI: 10.1016/j.gde.2010.01.001

You, Z., Shi, L.Z., Zhu, Q., Wu, P., Zhang, Y.W., Basilio, A., Tonnu, N., Verma, I.M., Berns, M.W., Hunter, T. CtIP links DNA double-strand break sensing to resection. (2009) Molecular Cell. 36(6):954-69. DOI: 10.1016/j.molcel.2009.12.002

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Malumbres, M., Harlow, E., Hunt, T., Hunter, T., Lahti, J.M., Manning, G., Morgan, D.O., Tsai, L.H., Wolgemuth, D.J. Cyclin-dependent kinases: a family portrait. (2009) Nature Cell Biology. 11(11):1275-6. DOI: 10.1038/ncb1109-1275

Zhang, Y.W., Brognard, J., Coughlin, C., You, Z., Dolled-Filhart, M., Aslanian, A., Manning, G., Abraham, R.T., Hunter, T. The F box protein Fbx6 regulates Chk1 stability and cellular sensitivity to replication stress. (2009) Molecular Cell. 35(4):442-53. DOI: 10.1016/j.molcel.2009.06.030

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Carrano, A.C., Liu, Z., Dillin, A., Hunter, T. A conserved ubiquitination pathway determines longevity in response to diet restriction. (2009) Nature. 460(7253):396-9. DOI: 10.1038/nature08130

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Lu, Z., Hunter, T. Degradation of activated protein kinases by ubiquitination. (2009) Annual Review of Biochemistry. 78:435-75. DOI: 10.1146/annurev.biochem.013008.092711

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Pearson, G.W., Hunter, T. PI-3 kinase activity is necessary for ERK1/2-induced disruption of mammary epithelial architecture. (2009) Breast Cancer Research. 11(3):R29. DOI: 10.1186/bcr2259

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Hunter, T. Tyrosine phosphorylation: thirty years and counting. (2009) Current Opinion in Cell Biology. 21(2):140-6. DOI: 10.1016/j.ceb.2009.01.028

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Copp, J., Manning, G., Hunter, T. TORC-specific phosphorylation of mammalian target of rapamycin (mTOR): phospho-Ser2481 is a marker for intact mTOR signaling complex 2. (2009) Cancer Research. 69(5):1821-7. DOI: 10.1158/0008-5472.CAN-08-3014

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Smith, J.J., Putta, S., Zhu, W., Pao, G.M., Verma, I.M., Hunter, T., Bryant, S.V., Gardiner, D.M., Harkins, T.T., Voss, S.R. Genic regions of a large salamander genome contain long introns and novel genes. (2009) BMC Genomics. 10:19. DOI: 10.1186/1471-2164-10-19

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Monaghan, J.R., Epp, L.G., Putta, S., Page, R.B., Walker, J.A., Beachy, C.K., Zhu, W., Pao, G.M., Verma, I.M., Hunter, T., Bryant, S.V., Gardiner, D.M., Harkins, T.T., Voss, S.R. Microarray and cDNA sequence analysis of transcription during nerve-dependent limb regeneration. (2009) BMC Biology. 7:1. DOI: 10.1186/1741-7007-7-1

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Hunter, T., Sun, H. Crosstalk between the SUMO and ubiquitin pathways. (2008) Ernst Schering Found Symp Proc.(1):1-16

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Hashimoto, T., Yamauchi, L., Hunter, T., Kikkawa, U., Kamada, S. Possible involvement of caspase-7 in cell cycle progression at mitosis. (2008) Genes to Cells. 13(6):609-21. DOI: 10.1111/j.1365-2443.2008.01192.x

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Hunter, T. Tony Hunter: kinase king. Interview by Ruth Williams. (2008) Journal of Cell Biology. 181(4):572-3. DOI: 10.1083/jcb.1814pi

Bailis, J.M., Luche, D.D., Hunter, T., Forsburg, S.L. Minichromosome maintenance proteins interact with checkpoint and recombination proteins to promote s-phase genome stability. (2008) Molecular and Cellular Biology. 28(5):1724-38. DOI: 10.1128/MCB.01717-07

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Ghosh, S., Marquardt, T., Thaler, J.P., Carter, N., Andrews, S.E., Pfaff, S.L., Hunter, T. Instructive role of aPKCzeta subcellular localization in the assembly of adherens junctions in neural progenitors. (2008) Proceedings of the National Academy of Sciences of the United States of America. 105(1):335-40. DOI: 10.1073/pnas.0705713105

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Pearson, G.W., Hunter, T. Real-time imaging reveals that noninvasive mammary epithelial acini can contain motile cells. (2007) Journal of Cell Biology. 179(7):1555-67. DOI: 10.1083/jcb.200706099

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Hunter, T. The age of crosstalk: phosphorylation, ubiquitination, and beyond. (2007) Molecular Cell. 28(5):730-8. DOI: 10.1016/j.molcel.2007.11.019

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You, Z., Bailis, J.M., Johnson, S.A., Dilworth, S.M., Hunter, T. Rapid activation of ATM on DNA flanking double-strand breaks. (2007) Nature Cell Biology. 9(11):1311-8. DOI: 10.1038/ncb1651

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Sun, H., Leverson, J.D., Hunter, T. Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. (2007) EMBO Journal. 26(18):4102-12. DOI: 10.1038/sj.emboj.7601839

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Johnson, S.A., You, Z., Hunter, T. Monitoring ATM kinase activity in living cells. (2007) DNA Repair. 6(9):1277-84. DOI: 10.1016/j.dnarep.2007.02.025

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Hunter, T. Treatment for chronic myelogenous leukemia: the long road to imatinib. (2007) Journal of Clinical Investigation. 117(8):2036-43. DOI: 10.1172/JCI31691

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Zhang, Y., Daum, S., Wildemann, D., Zhou, X.Z., Verdecia, M.A., Bowman, M.E., Lücke, C., Hunter, T., Lu, K.P., Fischer, G., Noel, J.P. Structural basis for high-affinity peptide inhibition of human Pin1. (2007) ACS Chemical Biology. 2(5):320-8. DOI: 10.1021/cb7000044

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Fang, D., Hawke, D., Zheng, Y., Xia, Y., Meisenhelder, J., Nika, H., Mills, G.B., Kobayashi, R., Hunter, T., Lu, Z. Phosphorylation of beta-catenin by AKT promotes beta-catenin transcriptional activity. (2007) Journal of Biological Chemistry. 282(15):11221-9. DOI: 10.1074/jbc.M611871200

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Hunter, T., Simon, J. A not so brief history of the Oncogene Meeting and its cartoons. (2007) Oncogene. 26(9):1260-7. DOI: 10.1038/sj.onc.1210262

Bozulic, L., Morin, P., Hunter, T., Hemmings, B.A. Meeting report: targeting the kinome–20 years of tyrosine kinase inhibitor research in Basel. (2007) Sci. STKE. 2007(374):pe8. DOI: 10.1126/stke.3742007pe8

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Xia, Y., Wang, J., Liu, T.J., Yung, W.K., Hunter, T., Lu, Z. c-Jun downregulation by HDAC3-dependent transcriptional repression promotes osmotic stress-induced cell apoptosis. (2007) Molecular Cell. 25(2):219-32. DOI: 10.1016/j.molcel.2007.01.005

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Xia, Y., Wang, J., Xu, S., Johnson, G.L., Hunter, T., Lu, Z. MEKK1 mediates the ubiquitination and degradation of c-Jun in response to osmotic stress. (2007) Molecular and Cellular Biology. 27(2):510-7. DOI: 10.1128/MCB.01355-06

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Ghosh, S., Tergaonkar, V., Rothlin, C.V., Correa, R.G., Bottero, V., Bist, P., Verma, I.M., Hunter, T. Essential role of tuberous sclerosis genes TSC1 and TSC2 in NF-kappaB activation and cell survival. (2006) Cancer Cell. 10(3):215-26. DOI: 10.1016/j.ccr.2006.08.007

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Shah, O.J., Hunter, T. Turnover of the active fraction of IRS1 involves raptor-mTOR- and S6K1-dependent serine phosphorylation in cell culture models of tuberous sclerosis. (2006) Molecular and Cellular Biology. 26(17):6425-34. DOI: 10.1128/MCB.01254-05

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Joazeiro, C.A., Anderson, K.C., Hunter, T. Proteasome inhibitor drugs on the rise. (2006) Cancer Research. 66(16):7840-2. DOI: 10.1158/0008-5472.CAN-06-2033

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Wolff, S., Ma, H., Burch, D., Maciel, G.A., Hunter, T., Dillin, A. SMK-1, an essential regulator of DAF-16-mediated longevity. (2006) Cell. 124(5):1039-53. DOI: 10.1016/j.cell.2005.12.042

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Petersen, P., Chou, D.M., You, Z., Hunter, T., Walter, J.C., Walter, G. Protein phosphatase 2A antagonizes ATM and ATR in a Cdk2- and Cdc7-independent DNA damage checkpoint. (2006) Molecular and Cellular Biology. 26(5):1997-2011. DOI: 10.1128/MCB.26.5.1997-2011.2006

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Wang, Z., Qi, C., Krones, A., Woodring, P., Zhu, X., Reddy, J.K., Evans, R.M., Rosenfeld, M.G., Hunter, T. Critical roles of the p160 transcriptional coactivators p/CIP and SRC-1 in energy balance. (2006) Cell Metabolism. 3(2):111-22. DOI: 10.1016/j.cmet.2006.01.002

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Zhang, Y.W., Hunter, T., Abraham, R.T. Turning the replication checkpoint on and off. (2006) Cell Cycle. 5(2):125-8. DOI: 10.4161/cc.5.2.2308

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Hunter, T., Schulman, H. CaMKII structure–an elegant design. (2005) Cell. 123(5):765-7. DOI: 10.1016/j.cell.2005.11.017

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Kamada, S., Kikkawa, U., Tsujimoto, Y., Hunter, T. A-kinase-anchoring protein 95 functions as a potential carrier for the nuclear translocation of active caspase 3 through an enzyme-substrate-like association. (2005) Molecular and Cellular Biology. 25(21):9469-77. DOI: 10.1128/MCB.25.21.9469-9477.2005

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Huang, H.K., Bailis, J.M., Leverson, J.D., Gómez, E.B., Forsburg, S.L., Hunter, T. Suppressors of Bir1p (Survivin) identify roles for the chromosomal passenger protein Pic1p (INCENP) and the replication initiation factor Psf2p in chromosome segregation. (2005) Molecular and Cellular Biology. 25(20):9000-15. DOI: 10.1128/MCB.25.20.9000-9015.2005

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Watanabe, N., Arai, H., Iwasaki, J., Shiina, M., Ogata, K., Hunter, T., Osada, H. Cyclin-dependent kinase (CDK) phosphorylation destabilizes somatic Wee1 via multiple pathways. (2005) Proceedings of the National Academy of Sciences of the United States of America. 102(33):11663-8. DOI: 10.1073/pnas.0500410102

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You, Z., Chahwan, C., Bailis, J., Hunter, T., Russell, P. ATM activation and its recruitment to damaged DNA require binding to the C terminus of Nbs1. (2005) Molecular and Cellular Biology. 25(13):5363-79. DOI: 10.1128/MCB.25.13.5363-5379.2005

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Wang, X., Li, X., Meisenhelder, J., Hunter, T., Yoshida, S., Asami, T., Chory, J. Autoregulation and homodimerization are involved in the activation of the plant steroid receptor BRI1. (2005) Developmental Cell. 8(6):855-65. DOI: 10.1016/j.devcel.2005.05.001

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Marquardt, T., Shirasaki, R., Ghosh, S., Andrews, S.E., Carter, N., Hunter, T., Pfaff, S.L. Coexpressed EphA receptors and ephrin-A ligands mediate opposing actions on growth cone navigation from distinct membrane domains. (2005) Cell. 121(1):127-39. DOI: 10.1016/j.cell.2005.01.020

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Takagi, Y., Masuda, C.A., Chang, W.H., Komori, H., Wang, D., Hunter, T., Joazeiro, C.A., Kornberg, R.D. Ubiquitin ligase activity of TFIIH and the transcriptional response to DNA damage. (2005) Molecular Cell. 18(2):237-43. DOI: 10.1016/j.molcel.2005.03.007

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Woodring, P.J., Hunter, T., Wang, J.Y. Mitotic phosphorylation rescues Abl from F-actin-mediated inhibition. (2005) Journal of Biological Chemistry. 280(11):10318-25. DOI: 10.1074/jbc.M410658200

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Papin, J.A., Hunter, T., Palsson, B.O., Subramaniam, S. Reconstruction of cellular signalling networks and analysis of their properties. (2005) Nature Reviews Molecular Cell Biology. 6(2):99-111. DOI: 10.1038/nrm1570

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Johnson, S.A., Hunter, T. Kinomics: methods for deciphering the kinome. (2005) Nature Methods. 2(1):17-25. DOI: 10.1038/nmeth731

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Shah, O.J., Hunter, T. Tuberous sclerosis and insulin resistance. Unlikely bedfellows reveal a TORrid affair. (2005) Cell Cycle. 4(1):46-51. DOI: 10.4161/cc.4.1.1343

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Kamada, S., Kikkawa, U., Tsujimoto, Y., Hunter, T. Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s). (2005) Journal of Biological Chemistry. 280(2):857-60. DOI: 10.1074/jbc.C400538200

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York, J.D., Hunter, T. Signal transduction. Unexpected mediators of protein phosphorylation. (2004) Science. 306(5704):2053-5. DOI: 10.1126/science.1107225

Grabbe, C., Zervas, C.G., Hunter, T., Brown, N.H., Palmer, R.H. Focal adhesion kinase is not required for integrin function or viability in Drosophila. (2004) Development. 131(23):5795-805. DOI: 10.1242/dev.01462

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Shah, O.J., Wang, Z., Hunter, T. Inappropriate activation of the TSC/Rheb/mTOR/S6K cassette induces IRS1/2 depletion, insulin resistance, and cell survival deficiencies. (2004) Current Biology. 14(18):1650-6. DOI: 10.1016/j.cub.2004.08.026

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Johnson, S.A., Hunter, T. Phosphoproteomics finds its timing. (2004) Nature Biotechnology. 22(9):1093-4. DOI: 10.1038/nbt0904-1093

Caenepeel, S., Charydczak, G., Sudarsanam, S., Hunter, T., Manning, G. The mouse kinome: discovery and comparative genomics of all mouse protein kinases. (2004) Proceedings of the National Academy of Sciences of the United States of America. 101(32):11707-12. DOI: 10.1073/pnas.0306880101

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Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., Mustelin, T. Protein tyrosine phosphatases in the human genome. (2004) Cell. 117(6):699-711. DOI: 10.1016/j.cell.2004.05.018

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Fukunaga, R., Hunter, T. Identification of MAPK substrates by expression screening with solid-phase phosphorylation. (2004) Methods in Molecular Biology. 250:211-36. DOI: 10.1385/1-59259-671-1:211

Woodring, P.J., Meisenhelder, J., Johnson, S.A., Zhou, G.L., Field, J., Shah, K., Bladt, F., Pawson, T., Niki, M., Pandolfi, P.P., Wang, J.Y., Hunter, T. c-Abl phosphorylates Dok1 to promote filopodia during cell spreading. (2004) Journal of Cell Biology. 165(4):493-503. DOI: 10.1083/jcb.200312171

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Shah, O.J., Hunter, T. Critical role of T-loop and H-motif phosphorylation in the regulation of S6 kinase 1 by the tuberous sclerosis complex. (2004) Journal of Biological Chemistry. 279(20):20816-23. DOI: 10.1074/jbc.M400957200

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Lu, Z., Hunter, T. Wnt-independent beta-catenin transactivation in tumor development. (2004) Cell Cycle. 3(5):571-3.

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Watanabe, N., Arai, H., Nishihara, Y., Taniguchi, M., Watanabe, N., Hunter, T., Osada, H. M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP. (2004) Proceedings of the National Academy of Sciences of the United States of America. 101(13):4419-24. DOI: 10.1073/pnas.0307700101

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Hunter, T., Eckhart, W. The discovery of tyrosine phosphorylation: it’s all in the buffer! (2004) Cell. 116(2 Suppl):S35-9, 1 p following S48.

Lu, Z., Ghosh, S., Wang, Z., Hunter, T. Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherin, increased transcriptional activity of beta-catenin, and enhanced tumor cell invasion. (2003) Cancer Cell. 4(6):499-515.

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Lorén, C.E., Englund, C., Grabbe, C., Hallberg, B., Hunter, T., Palmer, R.H. A crucial role for the Anaplastic lymphoma kinase receptor tyrosine kinase in gut development in Drosophila melanogaster. (2003) EMBO Reports. 4(8):781-6. DOI: 10.1038/sj.embor.embor897

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Sonnenburg, E.D., Bilwes, A., Hunter, T., Noel, J.P. The structure of the membrane distal phosphatase domain of RPTPalpha reveals interdomain flexibility and an SH2 domain interaction region. (2003) Biochemistry. 42(26):7904-14. DOI: 10.1021/bi0340503

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Woodring, P.J., Hunter, T., Wang, J.Y. Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases. (2003) Journal of Cell Science. 116(Pt 13):2613-26. DOI: 10.1242/jcs.00622

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Liou, Y.C., Sun, A., Ryo, A., Zhou, X.Z., Yu, Z.X., Huang, H.K., Uchida, T., Bronson, R., Bing, G., Li, X., Hunter, T., Lu, K.P. Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration. (2003) Nature. 424(6948):556-61. DOI: 10.1038/nature01832

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Shah, O.J., Ghosh, S., Hunter, T. Mitotic regulation of ribosomal S6 kinase 1 involves Ser/Thr, Pro phosphorylation of consensus and non-consensus sites by Cdc2. (2003) Journal of Biological Chemistry. 278(18):16433-42. DOI: 10.1074/jbc.M300435200

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O’Connell, M.J., Krien, M.J., Hunter, T. Never say never. The NIMA-related protein kinases in mitotic control. (2003) Trends in Cell Biology. 13(5):221-8.

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Xia, Y., Pao, G.M., Chen, H.W., Verma, I.M., Hunter, T. Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein. (2003) Journal of Biological Chemistry. 278(7):5255-63. DOI: 10.1074/jbc.M204591200

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Verdecia, M.A., Joazeiro, C.A., Wells, N.J., Ferrer, J.L., Bowman, M.E., Hunter, T., Noel, J.P. Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. (2003) Molecular Cell. 11(1):249-59.

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Uchida, T., Takamiya, M., Takahashi, M., Miyashita, H., Ikeda, H., Terada, T., Matsuo, Y., Shirouzu, M., Yokoyama, S., Fujimori, F., Hunter, T. Pin1 and Par14 peptidyl prolyl isomerase inhibitors block cell proliferation. (2003) Chemistry & Biology. 10(1):15-24.

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Gilman, A.G., Simon, M.I., Bourne, H.R., Harris, B.A., Long, R., Ross, E.M., Stull, J.T., Taussig, R., Bourne, H.R., Arkin, A.P., Cobb, M.H., Cyster, J.G., Devreotes, P.N., Ferrell, J.E., Fruman, D., Gold, M., Weiss, A., Stull, J.T., Berridge, M.J., Cantley, L.C., Catterall, W.A., Coughlin, S.R., Olson, E.N., Smith, T.F., Brugge, J.S., Botstein, D., Dixon, J.E., Hunter, T., Lefkowitz, R.J., Pawson, A.J., Sternberg, P.W., Varmus, H., Subramaniam, S., Sinkovits, R.S., Li, J., Mock, D., Ning, Y., Saunders, B., Sternweis, P.C., Hilgemann, D., Scheuermann, R.H., DeCamp, D., Hsueh, R., Lin, K.M., Ni, Y., Seaman, W.E., Simpson, P.C., O’Connell, T.D., Roach, T., Simon, M.I., Choi, S., Eversole-Cire, P., Fraser, I., Mumby, M.C., Zhao, Y., Brekken, D., Shu, H., Meyer, T., Chandy, G., Heo, W.D., Liou, J., O’Rourke, N., Verghese, M., Mumby, S.M., Han, H., Brown, H.A., Forrester, J.S., Ivanova, P., Milne, S.B., Casey, P.J., Harden, T.K., Arkin, A.P., Doyle, J., Gray, M.L., Meyer, T., Michnick, S., Schmidt, M.A., Toner, M., Tsien, R.Y., Natarajan, M., Ranganathan, R., Sambrano, G.R., . Overview of the Alliance for Cellular Signaling. (2002) Nature. 420(6916):703-6. DOI: 10.1038/nature01304

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Manning, G., Whyte, D.B., Martinez, R., Hunter, T., Sudarsanam, S. The protein kinase complement of the human genome. (2002) Science. 298(5600):1912-34. DOI: 10.1126/science.1075762

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Manning, G., Plowman, G.D., Hunter, T., Sudarsanam, S. Evolution of protein kinase signaling from yeast to man. (2002) Trends in Biochemical Sciences. 27(10):514-20.

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Carter, N., Nakamoto, T., Hirai, H., Hunter, T. EphrinA1-induced cytoskeletal re-organization requires FAK and p130(cas). (2002) Nature Cell Biology. 4(8):565-73. DOI: 10.1038/ncb823

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Hunter, T. Tyrosine phosphorylation in cell signaling and disease. (2002) Keio J Med. 51(2):61-71.

Mollinari, C., Kleman, J.P., Jiang, W., Schoehn, G., Hunter, T., Margolis, R.L. PRC1 is a microtubule binding and bundling protein essential to maintain the mitotic spindle midzone. (2002) Journal of Cell Biology. 157(7):1175-86. DOI: 10.1083/jcb.200111052

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Lu, Z., Xu, S., Joazeiro, C., Cobb, M.H., Hunter, T. The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2. (2002) Molecular Cell. 9(5):945-56.

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Asahara, H., Tartare-Deckert, S., Nakagawa, T., Ikehara, T., Hirose, F., Hunter, T., Ito, T., Montminy, M. Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro. (2002) Molecular and Cellular Biology. 22(9):2974-83.

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Leverson, J.D., Huang, H.K., Forsburg, S.L., Hunter, T. The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis. (2002) Molecular Biology of the Cell. 13(4):1132-43. DOI: 10.1091/mbc.01-07-0330

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Woodring, P.J., Litwack, E.D., O’Leary, D.D., Lucero, G.R., Wang, J.Y., Hunter, T. Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension. (2002) Journal of Cell Biology. 156(5):879-92. DOI: 10.1083/jcb.200110014

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Fang, D., Elly, C., Gao, B., Fang, N., Altman, Y., Joazeiro, C., Hunter, T., Copeland, N., Jenkins, N., Liu, Y.C. Dysregulation of T lymphocyte function in itchy mice: a role for Itch in TH2 differentiation. (2002) Nature Immunology. 3(3):281-7. DOI: 10.1038/ni763

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Liou, Y.C., Ryo, A., Huang, H.K., Lu, P.J., Bronson, R., Fujimori, F., Uchida, T., Hunter, T., Lu, K.P. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. (2002) Proceedings of the National Academy of Sciences of the United States of America. 99(3):1335-40. DOI: 10.1073/pnas.032404099

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Mustelin, T., Hunter, T. Meeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalpha. (2002) Sci. STKE. 2002(115):pe3. DOI: 10.1126/stke.2002.115.pe3

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Buck, M., Zhang, L., Halasz, N.A., Hunter, T., Chojkier, M. Nuclear export of phosphorylated C/EBPbeta mediates the inhibition of albumin expression by TNF-alpha. (2001) EMBO Journal. 20(23):6712-23. DOI: 10.1093/emboj/20.23.6712

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Huang, H.K., Forsburg, S.L., John, U.P., O’Connell, M.J., Hunter, T. Isolation and characterization of the Pin1/Ess1p homologue in Schizosaccharomyces pombe. (2001) Journal of Cell Science. 114(Pt 20):3779-88.

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Pin1/Ess1p is a highly conserved WW domain-containing peptidyl-prolyl isomerase (PPIase); its WW domain binds specifically to phospho-Ser/Thr-Pro sequences and its catalytic domain isomerizes phospho-Ser/Thr-Pro bonds. Pin1 PPIase activity can alter protein conformation in a phosphorylation-dependent manner and/or promote protein dephosphorylation. Human Pin1 interacts with mitotic phosphoproteins, such as NIMA, Cdc25 and Wee1, and inhibits G(2)/M progression in Xenopus extracts. Depletion of Pin1 in HeLa cells and deletion of ESS1 in S. cerevisiae result in mitotic arrest. In addition, Pin1/Ess1p play roles in transcription in S. cerevisiae and in mammalian somatic cells. The S. pombe genome sequence has an open reading frame (ORF) that has 47% identity with Pin1. Expression of this ORF rescued the growth defect caused by ess1 deletion in S. cerevisiae, indicating that S. pombe Pin1p is a functional Pin1 homologue. Overexpression of pin1(+) in S. pombe caused slow growth and a G(1) delay. Deletion of pin1(+) (pin1 Delta) did not affect cell cycle progression or cell growth, but increased sensitivity to the cyclophilin inhibitor, cyclosporin A, suggesting that cyclophilin family PPIases have overlapping functions with the Pin1p PPIase. Deletion of pin1(+) did not affect the DNA replication checkpoint, but conferred a modest increase in UV sensitivity. Furthermore, the pin1 Delta allele caused a synthetic growth defect when combined with either cdc25-22 or wee1-50 but not the cdc24-1 temperature-sensitive mutant. The pin1 Delta strain showed increased sensitivity to the PP1/PP2A family phosphatase inhibitor, okadaic acid, suggesting that Pin1p plays a role in protein dephosphorylation as a result of its ability to increase the population of phospho-Ser/Thr-Pro peptide bonds in the trans conformation that is required for PP2A-mediated dephosphorylation. Our genetic data also suggest that Pin1p might function as a positive regulator of Cdc25p and Wee1p.

Buck, M., Poli, V., Hunter, T., Chojkier, M. C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survival. (2001) Molecular Cell. 8(4):807-16.

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Woodring, P.J., Hunter, T., Wang, J.Y. Inhibition of c-Abl tyrosine kinase activity by filamentous actin. (2001) Journal of Biological Chemistry. 276(29):27104-10. DOI: 10.1074/jbc.M100559200

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Lu, Z., Jiang, G., Blume-Jensen, P., Hunter, T. Epidermal growth factor-induced tumor cell invasion and metastasis initiated by dephosphorylation and downregulation of focal adhesion kinase. (2001) Molecular and Cellular Biology. 21(12):4016-31. DOI: 10.1128/MCB.21.12.4016-4031.2001

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Lorén, C.E., Scully, A., Grabbe, C., Edeen, P.T., Thomas, J., McKeown, M., Hunter, T., Palmer, R.H. Identification and characterization of DAlk: a novel Drosophila melanogaster RTK which drives ERK activation in vivo. (2001) Genes to Cells. 6(6):531-44.

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Tertoolen, L.G., Blanchetot, C., Jiang, G., Overvoorde, J., Gadella, T.W., Hunter, T., den Hertog, J. Dimerization of receptor protein-tyrosine phosphatase alpha in living cells. (2001) BMC Cell Biology. 2:8.

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Meisenhelder, J., Hunter, T., van der Geer, P. Phosphopeptide mapping and identification of phosphorylation sites. (2001) Current Protocols in Protein Science. Chapter 13:Unit13.9. DOI: 10.1002/0471140864.ps1309s18

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Meisenhelder, J., Hunter, T., van der Geer, P. Phosphopeptide mapping and identification of phosphorylation sites. (2001) Current Protocols in Molecular Biology. Chapter 18:Unit 18.9. DOI: 10.1002/0471142727.mb1809s48

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Blume-Jensen, P., Hunter, T. Oncogenic kinase signalling. (2001) Nature. 411(6835):355-65. DOI: 10.1038/35077225

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Hauck, C.R., Hunter, T., Schlaepfer, D.D. The v-Src SH3 domain facilitates a cell adhesion-independent association with focal adhesion kinase. (2001) Journal of Biological Chemistry. 276(21):17653-62. DOI: 10.1074/jbc.M009329200

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Integrins facilitate cell attachment to the extracellular matrix, and these interactions generate cell survival, proliferation, and motility signals. Integrin signals are relayed in part by focal adhesion kinase (FAK) activation and the formation of a transient signaling complex initiated by Src homology 2 (SH2)-dependent binding of Src family protein-tyrosine kinases to the FAK Tyr-397 autophosphorylation site. Here we show that in viral Src (v-Src)-transformed NIH3T3 fibroblasts, an adhesion-independent FAK-Src signaling complex occurs. Co-expression studies in human 293T cells showed that v-Src could associate with and phosphorylate a Phe-397 FAK mutant at Tyr-925 promoting Grb2 binding to FAK in suspended cells. In vitro, glutathione S-transferase fusion proteins of the v-Src SH3 but not c-Src SH3 domain bound to FAK in lysates of NIH3T3 fibroblasts. The v-Src SH3-binding sites were mapped to known proline-X-X-proline (PXXP) SH3-binding motifs in the FAK N- (residues 371-377) and C-terminal domains (residues 712-718 and 871-882) by in vitro pull-down assays, and these sites are composed of a PXXPXXPhi (where Phi is a hydrophobic residue) v-Src SH3 binding consensus. Sequence comparisons show that residues in the RT loop region of the c-Src and v-Src SH3 domains differ. Substitution of c-Src RT loop residues (Arg-97 and Thr-98) for those found in the v-Src SH3 domain (Trp-97 and Ile-98) enhanced the binding of distinct NIH3T3 cellular proteins to a glutathione S-transferase fusion protein of the c-Src (Trp-97 + Ile-98) SH3 domain. FAK was identified as a c-Src (Trp-97 + Ile-98) SH3 domain target in fibroblasts, and co-expression studies in 293T cells showed that full-length c-Src (Trp-97 + Ile-98) could associate in vivo with Phe-397 FAK in an SH2-independent manner. These studies establish a functional role for the v-Src SH3 domain in stabilizing an adhesion-independent signaling complex with FAK.

Ruffner, H., Joazeiro, C.A., Hemmati, D., Hunter, T., Verma, I.M. Cancer-predisposing mutations within the RING domain of BRCA1: loss of ubiquitin protein ligase activity and protection from radiation hypersensitivity. (2001) Proceedings of the National Academy of Sciences of the United States of America. 98(9):5134-9. DOI: 10.1073/pnas.081068398

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Blume-Jensen, P., Hunter, T. Two-dimensional phosphoamino acid analysis. (2001) Methods in Molecular Biology. 124:49-65.

Moniakis, J., Funamoto, S., Fukuzawa, M., Meisenhelder, J., Araki, T., Abe, T., Meili, R., Hunter, T., Williams, J., Firtel, R.A. An SH2-domain-containing kinase negatively regulates the phosphatidylinositol-3 kinase pathway. (2001) Genes & Development. 15(6):687-98. DOI: 10.1101/gad.871001

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Potter, L.R., Hunter, T. Activation of protein kinase C stimulates the dephosphorylation of natriuretic peptide receptor-B at a single serine residue: a possible mechanism of heterologous desensitization. (2000) Journal of Biological Chemistry. 275(40):31099-106. DOI: 10.1074/jbc.M005506200

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Joazeiro, C.A., Hunter, T. Biochemistry. Ubiquitination–more than two to tango. (2000) Science. 289(5487):2061-2.

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Huang, H.k., Joazeiro, C.A., Bonfoco, E., Kamada, S., Leverson, J.D., Hunter, T. The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. (2000) Journal of Biological Chemistry. 275(35):26661-4. DOI: 10.1074/jbc.C000199200

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Friedrichsen, D.M., Joazeiro, C.A., Li, J., Hunter, T., Chory, J. Brassinosteroid-insensitive-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase. (2000) Plant Physiology. 123(4):1247-56.

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Jiang, G., den Hertog, J., Hunter, T. Receptor-like protein tyrosine phosphatase alpha homodimerizes on the cell surface. (2000) Molecular and Cellular Biology. 20(16):5917-29.

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We reported previously that the N-terminal D1 catalytic domain of receptor protein-tyrosine phosphatase alpha (RPTPalpha) forms a symmetrical, inhibited dimer in a crystal structure, in which a helix-turn-helix wedge element from one monomer is inserted into the catalytic cleft of the other monomer. Previous functional studies also suggested that dimerization inhibits the biological activity of a CD45 chimeric RPTP and the catalytic activity of an isolated RPTPsigma D1 catalytic domain. Most recently, we have also shown that enforced dimerization inhibits the biological activity of full-length RPTPalpha in a wedge-dependent manner. The physiological significance of such inhibition is unknown, due to a lack of understanding of how RPTPalpha dimerization is regulated in vivo. In this study, we show that transiently expressed cell surface RPTPalpha exists predominantly as homodimers, suggesting that dimerization-mediated inhibition of RPTPalpha biological activity is likely to be physiologically relevant. Consistent with our published and unpublished crystallographic data, we show that mutations in the wedge region of D1 catalytic domain and deletion of the entire D2 catalytic domain independently reduced but did not abolish RPTPalpha homodimerization, suggesting that both domains are critically involved but that neither is essential for homodimerization. Finally, we also provide evidence that both the RPTPalpha extracellular domain and the transmembrane domain were independently able to homodimerize. These results lead us to propose a zipper model in which inactive RPTPalpha dimers are stabilized by multiple, relatively weak dimerization interfaces. Dimerization in this manner would provide a potential mechanism for negative regulation of RPTPalpha. Such RPTPalpha dimers could be activated by extracellular ligands or intracellular binding proteins that induce monomerization or by intracellular signaling events that induce an open conformation of the dimer.

Verdecia, M.A., Bowman, M.E., Lu, K.P., Hunter, T., Noel, J.P. Structural basis for phosphoserine-proline recognition by group IV WW domains. (2000) Nature Structural Biology. 7(8):639-43. DOI: 10.1038/77929

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Leverson, J.D., Joazeiro, C.A., Page, A.M., Huang, H.k., Hieter, P., Hunter, T. The APC11 RING-H2 finger mediates E2-dependent ubiquitination. (2000) Molecular Biology of the Cell. 11(7):2315-25.

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Verdecia, M.A., Huang, H., Dutil, E., Kaiser, D.A., Hunter, T., Noel, J.P. Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement. (2000) Nature Structural Biology. 7(7):602-8. DOI: 10.1038/76838

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Xu, S., Huang, H.K., Kaiser, P., Latterich, M., Hunter, T. Phosphorylation and spindle pole body localization of the Cdc15p mitotic regulatory protein kinase in budding yeast. (2000) Current Biology. 10(6):329-32.

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Pao, G.M., Janknecht, R., Ruffner, H., Hunter, T., Verma, I.M. CBP/p300 interact with and function as transcriptional coactivators of BRCA1. (2000) Proceedings of the National Academy of Sciences of the United States of America. 97(3):1020-5.

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Blume-Jensen, P., Jiang, G., Hyman, R., Lee, K.F., O’Gorman, S., Hunter, T. Kit/stem cell factor receptor-induced activation of phosphatidylinositol 3′-kinase is essential for male fertility. (2000) Nature Genetics. 24(2):157-62. DOI: 10.1038/72814

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Hunter, T. Signaling–2000 and beyond. (2000) Cell. 100(1):113-27.

Buck, M., Poli, V., van der Geer, P., Chojkier, M., Hunter, T. Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP beta is required for hepatocyte proliferation induced by TGF alpha. (1999) Molecular Cell. 4(6):1087-92.

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Palmer, R.H., Fessler, L.I., Edeen, P.T., Madigan, S.J., McKeown, M., Hunter, T. DFak56 is a novel Drosophila melanogaster focal adhesion kinase. (1999) Journal of Biological Chemistry. 274(50):35621-9.

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Potter, L.R., Hunter, T. Identification and characterization of the phosphorylation sites of the guanylyl cyclase-linked natriuretic peptide receptors A and B. (1999) Methods. 19(4):506-20. DOI: 10.1006/meth.1999.0893

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Jiang, G., den Hertog, J., Su, J., Noel, J., Sap, J., Hunter, T. Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha. (1999) Nature. 401(6753):606-10. DOI: 10.1038/44170

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Jiang, W., McDonald, D., Hope, T.J., Hunter, T. Mammalian Cdc7-Dbf4 protein kinase complex is essential for initiation of DNA replication. (1999) EMBO Journal. 18(20):5703-13. DOI: 10.1093/emboj/18.20.5703

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Joazeiro, C.A., Wing, S.S., Huang, H., Leverson, J.D., Hunter, T., Liu, Y.C. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. (1999) Science. 286(5438):309-12.

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Wells, N.J., Watanabe, N., Tokusumi, T., Jiang, W., Verdecia, M.A., Hunter, T. The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts with Cdc2 complexes and is required for inhibition of G(2)/M progression. (1999) Journal of Cell Science. 112 ( Pt 1:3361-71.

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Jiang, G., Hunter, T. Receptor signaling: when dimerization is not enough. (1999) Current Biology. 9(15):R568-71.

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Ruffner, H., Jiang, W., Craig, A.G., Hunter, T., Verma, I.M. BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site. (1999) Molecular and Cellular Biology. 19(7):4843-54.

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Potter, L.R., Hunter, T. A constitutively “phosphorylated” guanylyl cyclase-linked atrial natriuretic peptide receptor mutant is resistant to desensitization. (1999) Molecular Biology of the Cell. 10(6):1811-20.

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Dephosphorylation of the natriuretic peptide receptor-A (NPR-A) is hypothesized to mediate its desensitization in response to atrial natriuretic peptide (ANP) binding. Recently, we identified six phosphorylation sites within the kinase homology domain of NPR-A and determined that the conversion of these residues to alanine abolished the ability of the receptor to be phosphorylated or to be activated by ANP and ATP. In an attempt to generate a form of NPR-A that mimics a fully phosphorylated receptor but that is resistant to dephosphorylation, we engineered a receptor variant (NPR-A-6E) containing glutamate substitutions at all six phosphorylation sites. Consistent with the known ability of negatively charged glutamate residues to substitute functionally, in some cases, for phosphorylated residues, we found that NPR-A-6E was activated 10-fold by ANP and ATP. As determined by guanylyl cyclase assays, the hormone-stimulated activity of the wild-type receptor declined over time in membrane preparations in vitro, and this loss was blocked by the serine/threonine protein phosphatase inhibitor microcystin. In contrast, the activity of NPR-A-6E was more linear with time and was unaffected by microcystin. The nonhydrolyzable ATP analogue adenosine 5′-(beta,gamma-imino)-triphosphate was half as effective as ATP in stimulating the wild-type receptor but was equally as potent in stimulating NPR-A-6E, suggesting that ATP is required to keep the wild-type but not 6E variant phosphorylated. Finally, the desensitization of NPR-A-6E in whole cells was markedly blunted compared with that of the wild-type receptor, consistent with its inability to shed the negative charge from its kinase homology domain via dephosphorylation. These data provide the first direct test of the requirement for dephosphorylation in guanylyl cyclase desensitization and they indicate that it is an essential component of this process.

Biggs, W.H., Meisenhelder, J., Hunter, T., Cavenee, W.K., Arden, K.C. Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1. (1999) Proceedings of the National Academy of Sciences of the United States of America. 96(13):7421-6.

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Jiang, W., Wells, N.J., Hunter, T. Multistep regulation of DNA replication by Cdk phosphorylation of HsCdc6. (1999) Proceedings of the National Academy of Sciences of the United States of America. 96(11):6193-8.

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Sekiguchi, T., Nishimoto, T., Hunter, T. Overexpression of D-type cyclins, E2F-1, SV40 large T antigen and HPV16 E7 rescue cell cycle arrest of tsBN462 cells caused by the CCG1/TAF(II)250 mutation. (1999) Oncogene. 18(10):1797-806. DOI: 10.1038/sj.onc.1202508

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Hunter, T. The role of tyrosine phosphorylation in cell growth and disease. (1998) Harvey Lect. 94:81-119.

Jiang, W., Jimenez, G., Wells, N.J., Hope, T.J., Wahl, G.M., Hunter, T., Fukunaga, R. PRC1: a human mitotic spindle-associated CDK substrate protein required for cytokinesis. (1998) Molecular Cell. 2(6):877-85.

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Janknecht, R., Wells, N.J., Hunter, T. TGF-beta-stimulated cooperation of smad proteins with the coactivators CBP/p300. (1998) Genes & Development. 12(14):2114-9.

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Blume-Jensen, P., Janknecht, R., Hunter, T. The kit receptor promotes cell survival via activation of PI 3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136. (1998) Current Biology. 8(13):779-82.

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Potter, L.R., Hunter, T. Identification and characterization of the major phosphorylation sites of the B-type natriuretic peptide receptor. (1998) Journal of Biological Chemistry. 273(25):15533-9.

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Hunter, T. The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease. (1998) Philos. Trans. R. Soc. Lond., B, Biol. Sci. 353(1368):583-605. DOI: 10.1098/rstb.1998.0228

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Potter, L.R., Hunter, T. Phosphorylation of the kinase homology domain is essential for activation of the A-type natriuretic peptide receptor. (1998) Molecular and Cellular Biology. 18(4):2164-72.

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Schlaepfer, D.D., Hunter, T. Integrin signalling and tyrosine phosphorylation: just the FAKs? (1998) Trends in Cell Biology. 8(4):151-7.

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Jiang, W., Hunter, T. Analysis of cell-cycle profiles in transfected cells using a membrane-targeted GFP. (1998) BioTechniques. 24(3):349-50, 352, 354.

Sekiguchi, T., Hunter, T. Induction of growth arrest and cell death by overexpression of the cyclin-Cdk inhibitor p21 in hamster BHK21 cells. (1998) Oncogene. 16(3):369-80. DOI: 10.1038/sj.onc.1201539

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Hunter, T. Prolyl isomerases and nuclear function. (1998) Cell. 92(2):141-3.

Majeti, R., Bilwes, A.M., Noel, J.P., Hunter, T., Weiss, A. Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge. (1998) Science. 279(5347):88-91.

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Jiang, W., Hunter, T. Identification and characterization of a human protein kinase related to budding yeast Cdc7p. (1997) Proceedings of the National Academy of Sciences of the United States of America. 94(26):14320-5.

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Fischer, W.H., Hoeger, C.A., Meisenhelder, J., Hunter, T., Craig, A.G. Determination of phosphorylation sites in peptides and proteins employing a volatile Edman reagent. (1997) J. Protein Chem. 16(5):329-34.

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Ranganathan, R., Lu, K.P., Hunter, T., Noel, J.P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. (1997) Cell. 89(6):875-86.

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Schlaepfer, D.D., Hunter, T. Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src. (1997) Journal of Biological Chemistry. 272(20):13189-95.

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Fukunaga, R., Hunter, T. MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. (1997) EMBO Journal. 16(8):1921-33. DOI: 10.1093/emboj/16.8.1921

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Hunter, T., Poon, R.Y. Cdc37: a protein kinase chaperone? (1997) Trends in Cell Biology. 7(4):157-61. DOI: 10.1016/S0962-8924(97)01027-1

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Janknecht, R., Hunter, T. Convergence of MAP kinase pathways on the ternary complex factor Sap-1a. (1997) EMBO Journal. 16(7):1620-7. DOI: 10.1093/emboj/16.7.1620

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Schlaepfer, D.D., Broome, M.A., Hunter, T. Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins. (1997) Molecular and Cellular Biology. 17(3):1702-13.

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Poon, R.Y., Lew, J., Hunter, T. Identification of functional domains in the neuronal Cdk5 activator protein. (1997) Journal of Biological Chemistry. 272(9):5703-8.

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Janknecht, R., Hunter, T. Activation of the Sap-1a transcription factor by the c-Jun N-terminal kinase (JNK) mitogen-activated protein kinase. (1997) Journal of Biological Chemistry. 272(7):4219-24.

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Hunter, T. Oncoprotein networks. (1997) Cell. 88(3):333-46.

Broome, M.A., Hunter, T. The PDGF receptor phosphorylates Tyr 138 in the c-Src SH3 domain in vivo reducing peptide ligand binding. (1997) Oncogene. 14(1):17-34. DOI: 10.1038/sj.onc.1200798

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Hunter, T., Plowman, G.D. The protein kinases of budding yeast: six score and more. (1997) Trends in Biochemical Sciences. 22(1):18-22.

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Poon, R.Y., Toyoshima, H., Hunter, T. On the masking of signals on immunoblots by cellular proteins. (1996) J. Immunol. Methods. 199(2):155-8.

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Horwitz, A.F., Hunter, T. Cell adhesion: integrating circuitry. (1996) Trends in Cell Biology. 6(12):460-1.

Schlaepfer, D.D., Hunter, T. Signal transduction from the extracellular matrix–a role for the focal adhesion protein-tyrosine kinase FAK. (1996) Cell Structure and Function. 21(5):445-50.

Schlaepfer, D.D., Hunter, T. Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases. (1996) Molecular and Cellular Biology. 16(10):5623-33.

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Bilwes, A.M., den Hertog, J., Hunter, T., Noel, J.P. Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization. (1996) Nature. 382(6591):555-9. DOI: 10.1038/382555a0

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Janknecht, R., Hunter, T. Versatile molecular glue. Transcriptional control. (1996) Current Biology. 6(8):951-4.

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Broome, M.A., Hunter, T. Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling. (1996) Journal of Biological Chemistry. 271(28):16798-806.

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The Src family protein-tyrosine kinases are required for mitogenic signaling from the platelet-derived growth factor (PDGF), colony stimulating factor-1, and epidermal growth factor (EGF) receptor protein-tyrosine kinases (RPTK) (Twamley-Stein, G. M., Pepperkok, R., Ansorge, W., and Courtneidge, S. A. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 7696-7700; Roche, S., Koegl, M., Barone, M. V., Roussel, M. F., and Courtneidge, S. A.(1995) Mol. Cell. Biol. 15, 1102-1109). In NIH3T3 fibroblasts, c-Src, Fyn, and c-Yes associate with the activated PDGF receptor, are substrates for receptor phosphorylation, and are themselves activated. Src family catalytic function is required for RPTK mitogenic signaling as evidenced by the SH2-dependent dominant negative phenotype exhibited by kinase-inactive Src and Fyn mutants (Twamley-Stein, G. M., Pepperkok, R., Ansorge, W., and Courtneidge, S. A.(1993) Proc. Natl. Acad. Sci. U. S. A. 90, 7696-7700). Here, we have generated clonal Src- murine fibroblast cell lines overexpressing various murine c-Src mutants and studied the effect of these mutant Src proteins on PDGF- and EGF-induced mitogenesis. Two c-Src SH3 domain mutants, Y133F and Y138F, each inhibited PDGF BB- and EGF-induced DNA synthesis in quiescent cells. This demonstrates an involvement of the Src SH3 domain in PDGFbeta and EGF receptor mitogenic signaling. Since both Tyr-133 and Tyr-138 are located on the ligand binding surface of the SH3 domain, these results suggest that the c-Src SH3 domain is required for PDGF and EGF mitogenic signaling. The dominant negative effect of either single mutant on PDGF receptor signaling was reversed by a second SH2-inactivating mutation. We conclude that the c-Src SH3 domain function requires the SH2 domain in the case of the PDGF receptor, presumably because binding of c-Src to the receptor via its SH2 domain is a prerequisite for the SH3 domain function. In contrast, SH2 function is apparently not essential for the SH3 function in EGF receptor signaling.

Hunter, T. Solid-state protein networks? (1996) Trends in Cell Biology. 6(7):254-5.

Sekiguchi, T., Noguchi, E., Hayashida, T., Nakashima, T., Toyoshima, H., Nishimoto, T., Hunter, T. D-type cyclin expression is decreased and p21 and p27 CDK inhibitor expression is increased when tsBN462 CCG1/TAFII250 mutant cells arrest in G1 at the restrictive temperature. (1996) Genes to Cells. 1(7):687-705.

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Winston, L.A., Hunter, T. Intracellular signalling: putting JAKs on the kinase MAP. (1996) Current Biology. 6(6):668-71.

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Poon, R.Y., Jiang, W., Toyoshima, H., Hunter, T. Cyclin-dependent kinases are inactivated by a combination of p21 and Thr-14/Tyr-15 phosphorylation after UV-induced DNA damage. (1996) Journal of Biological Chemistry. 271(22):13283-91.

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Hunter, T. Tyrosine phosphorylation: past, present and future. (1996) Biochemical Society Transactions. 24(2):307-27.

Fey, M.F., Moffat, G.J., Vik, D.P., Meisenhelder, J., Saris, C.J., Hunter, T., Tack, B.F. Complete structure of the murine p36 (annexin II) gene. Identification of mRNAs for both the murine and the human gene with alternatively spliced 5′ noncoding exons. (1996) Biochimica et Biophysica Acta. 1306(2-3):160-70.

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p36 (also termed annexin II) is a 39 kDa Ca2+/phospholipid-binding, membrane-associated protein that is a protein-tyrosine kinase substrate. We report here studies of the noncoding exons of p36, which combined with our earlier studies of the coding exons, allow us to conclude that the murine p36 gene is 34 kb in length with 14 exons. Comparison of the genes coding for mouse and human p36 (annexin II) and mouse, rat and human p35 (annexin I) and pigeon cp35 (an annexin I-related protein) shows strong genomic structural conservation supporting the hypothesis that these genes had a common ancestor. Both human and murine p36 mRNAs were found to be alternatively spliced in their 5′ noncoding region. In both cases exon 2 is a cassette exon, which is present in a small fraction of p36 mRNAs. In type 1 mouse p36 mRNA the first noncoding 44 base exon 1 is joined to exon 3, the first of the 12 coding exons. In type 2 mRNA a 70 base noncoding exon (exon 2) is inserted between exon 1 and exon 3. Type 1 mRNA was present in all cell types studied as revealed by Northern analysis and primer extension, whereas type 2 mRNA could only be detected by RACE or PCR, indicating that it is of very low abundance. The major transcription start site of the mouse p36 gene was mapped by primer extension to be 61 bp upstream of the AUG initiation codon, which corresponds to type 1 mRNA, The murine p36 gene enhancer/promoter region contains a putative TATA box and several other potential regulatory sequences. The two alternatively-spliced human p36 mRNAs differ by the presence or absence of a noncoding 81 base exon (exon 2) inserted after exon 1, with exon 2-containing mRNAs representing approximately 10% of total p36 mRNA. The 300 bp spanning the promoter and exons 1-3 of the human and murine p36 genes show strong sequence homology immediately before and after the major transcription start site except in the region corresponding to exon 2, where homology is more limited.

Lu, K.P., Hanes, S.D., Hunter, T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. (1996) Nature. 380(6574):544-7. DOI: 10.1038/380544a0

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Ofir, R., Weinstein, Y., Bazarsky, E., Blagerman, S., Wolfson, M., Hunter, T., Rager-Zisman, B. Tyrosine phosphorylation of measles virus P-phosphoprotein in persistently infected neuroblastoma cells. (1996) Virus Genes. 13(3):203-10.

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Neet, K., Hunter, T. Vertebrate non-receptor protein-tyrosine kinase families. (1996) Genes to Cells. 1(2):147-69.

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Winston, L.A., Hunter, T. JAK2, Ras, and Raf are required for activation of extracellular signal-regulated kinase/mitogen-activated protein kinase by growth hormone. (1995) Journal of Biological Chemistry. 270(52):30837-40.

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Poon, R.Y., Hunter, T. Cell regulation. Innocent bystanders or chosen collaborators? (1995) Current Biology. 5(11):1243-7.

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Haley, A., Hunter, T., Kiberstis, P., Zimmern, D. Multiple serine phosphorylation sites on the 30 kDa TMV cell-to-cell movement protein synthesized in tobacco protoplasts. (1995) Plant Journal. 8(5):715-24.

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Poon, R.Y., Hunter, T. Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin. (1995) Science. 270(5233):90-3.

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Hunter, T. When is a lipid kinase not a lipid kinase? When it is a protein kinase. (1995) Cell. 83(1):1-4.

Poon, R.Y., Toyoshima, H., Hunter, T. Redistribution of the CDK inhibitor p27 between different cyclin.CDK complexes in the mouse fibroblast cell cycle and in cells arrested with lovastatin or ultraviolet irradiation. (1995) Molecular Biology of the Cell. 6(9):1197-213.

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Lu, K.P., Hunter, T. The NIMA kinase: a mitotic regulator in Aspergillus nidulans and vertebrate cells. (1995) Progress in Cell Cycle Research. 1:187-205.

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Lu, K.P., Hunter, T. Evidence for a NIMA-like mitotic pathway in vertebrate cells. (1995) Cell. 81(3):413-24.

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Tracy, S., van der Geer, P., Hunter, T. The receptor-like protein-tyrosine phosphatase, RPTP alpha, is phosphorylated by protein kinase C on two serines close to the inner face of the plasma membrane. (1995) Journal of Biological Chemistry. 270(18):10587-94.

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Watanabe, N., Broome, M., Hunter, T. Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle. (1995) EMBO Journal. 14(9):1878-91.

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Hunter, T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. (1995) Cell. 80(2):225-36.

Schlaepfer, D.D., Hanks, S.K., Hunter, T., van der Geer, P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. (1994) Nature. 372(6508):786-91.

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Hunter, T. 1001 protein kinases redux–towards 2000. (1994) Seminars in Cell Biology. 5(6):367-76.

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Hunter, T., Pines, J. Cyclins and cancer. II: Cyclin D and CDK inhibitors come of age. (1994) Cell. 79(4):573-82.

Toyoshima, H., Hunter, T. p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21. (1994) Cell. 78(1):67-74.

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Zhang, S.H., Broome, M.A., Lawton, M.A., Hunter, T., Lamb, C.J. atpk1, a novel ribosomal protein kinase gene from Arabidopsis. II. Functional and biochemical analysis of the encoded protein. (1994) Journal of Biological Chemistry. 269(26):17593-9.

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Zhang, S.H., Lawton, M.A., Hunter, T., Lamb, C.J. atpk1, a novel ribosomal protein kinase gene from Arabidopsis. I. Isolation, characterization, and expression. (1994) Journal of Biological Chemistry. 269(26):17586-92.

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den Hertog, J., Tracy, S., Hunter, T. Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo. (1994) EMBO Journal. 13(13):3020-32.

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Rigaudy, P., Simon, S., Hunter, T., Sollazzo, M., Billetta, R., Zanetti, M., Eckhart, W. Antibodies specific for the neuronal form of the Src protein elicited by an antigenized antibody. (1994) DNA and Cell Biology. 13(6):585-91. DOI: 10.1089/dna.1994.13.585

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van der Geer, P., Hunter, T., Lindberg, R.A. Receptor protein-tyrosine kinases and their signal transduction pathways. (1994) Annual Review of Cell Biology. 10:251-337. DOI: 10.1146/annurev.cb.10.110194.001343

van der Geer, P., Hunter, T. Phosphopeptide mapping and phosphoamino acid analysis by electrophoresis and chromatography on thin-layer cellulose plates. (1994) Electrophoresis. 15(3-4):544-54.

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Middlemas, D.S., Meisenhelder, J., Hunter, T. Identification of TrkB autophosphorylation sites and evidence that phospholipase C-gamma 1 is a substrate of the TrkB receptor. (1994) Journal of Biological Chemistry. 269(7):5458-66.

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van der Geer, P., Hunter, T. Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase binding site, abrogates signal transduction by the murine CSF-1 receptor expressed in Rat-2 fibroblasts. (1993) EMBO Journal. 12(13):5161-72.

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Hunter, T. Braking the cycle. (1993) Cell. 75(5):839-41.

Sebastian, B., Kakizuka, A., Hunter, T. Cdc25M2 activation of cyclin-dependent kinases by dephosphorylation of threonine-14 and tyrosine-15. (1993) Proceedings of the National Academy of Sciences of the United States of America. 90(8):3521-4.

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Lindberg, R.A., Fischer, W.H., Hunter, T. Characterization of a human protein threonine kinase isolated by screening an expression library with antibodies to phosphotyrosine. (1993) Oncogene. 8(2):351-9.

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Meisenhelder, J., Hunter, T. The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth fact (1992) Molecular and Cellular Biology. 12(12):5843-56.

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Kikkawa, U., Mann, S.K., Firtel, R.A., Hunter, T. Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle. (1992) Molecular and Cellular Biology. 12(12):5711-23.

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Pines, J., Hunter, T. Cyclins A and B1 in the human cell cycle. (1992) Ciba Found. Symp. 170:187-96; discussion 196-204.

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Hunter, T. Regulation of the eukaryotic cell cycle. Introduction. (1992) Ciba Found. Symp. 170:1-6.

Krieg, J., Hunter, T. Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin. (1992) Journal of Biological Chemistry. 267(27):19258-65.

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Hunter, T., Karin, M. The regulation of transcription by phosphorylation. (1992) Cell. 70(3):375-87.

DeMaggio, A.J., Lindberg, R.A., Hunter, T., Hoekstra, M.F. The budding yeast HRR25 gene product is a casein kinase I isoform. (1992) Proceedings of the National Academy of Sciences of the United States of America. 89(15):7008-12.

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Hunter, T., Lindberg, R.A., Middlemas, D.S., Tracy, S., van der Geer, P. Receptor protein tyrosine kinases and phosphatases. (1992) Cold Spring Harbor Symposia on Quantitative Biology. 57:25-41.

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Kakizuka, A., Sebastian, B., Borgmeyer, U., Hermans-Borgmeyer, I., Bolado, J., Hunter, T., Hoekstra, M.F., Evans, R.M. A mouse cdc25 homolog is differentially and developmentally expressed. (1992) Genes & Development. 6(4):578-90.

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Freed, E., Hunter, T. A 41-kilodalton protein is a potential substrate for the p210bcr-abl protein-tyrosine kinase in chronic myelogenous leukemia cells. (1992) Molecular and Cellular Biology. 12(3):1312-23.

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Lindberg, R.A., Quinn, A.M., Hunter, T. Dual-specificity protein kinases: will any hydroxyl do? (1992) Trends in Biochemical Sciences. 17(3):114-9.

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Pines, J., Hunter, T. Cyclin-dependent kinases: a new cell cycle motif? (1991) Trends in Cell Biology. 1(5):117-21.

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Pines, J., Hunter, T. Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport. (1991) Journal of Cell Biology. 115(1):1-17.

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Hunter, T., Pines, J. Cyclins and cancer. (1991) Cell. 66(6):1071-4.

van der Geer, P., Hunter, T. Tyrosine 706 and 807 phosphorylation site mutants in the murine colony-stimulating factor-1 receptor are unaffected in their ability to bind or phosphorylate phosphatidylinositol-3 kinase but show dif (1991) Molecular and Cellular Biology. 11(9):4698-709.

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The receptor for colony-stimulating factor-1 (CSF-1) is a receptor protein-tyrosine kinase. To study the possible function of CSF-1 receptor autophosphorylation, two autophosphorylation sites, Tyr-706, located in the kinase insert, and Tyr-807, a residue conserved in all protein-tyrosine kinases, were changed independently to either phenylalanine or glycine. Wild-type and mutant receptors were stably expressed in Rat-2 cells. In response to CSF-1, cells expressing Phe- or Gly-706 mutant receptors showed increased growth rate and altered cell morphology. Both the Phe- and Gly-706 mutant receptors associated with and phosphorylated phosphatidylinositol-3 kinase at levels comparable with those of wild-type receptors. However, these mutant receptors differed subtly from each other and from the wild-type receptor in their ability to induce different aspects of the response to CSF-1. The Phe-706 mutant receptor was most strongly affected in its ability to increase growth rate or elevate the levels of c-fos and NGF1A mRNAs, whereas the Gly-706 mutant receptor was most markedly affected in its ability to induce a change in cell morphology or increase the levels of c-jun and NGF1A mRNAs. These findings indicate that Tyr-706 itself, or this region of the receptor, may be important for interaction of the CSF-1 receptor with different signalling pathways. Gly-807 mutant receptors lacked protein-tyrosine kinase activity, failed to respond to CSF-1, and were defective in biosynthetic processing. Phe-807 mutant receptors had 40 to 60% reduced protein-tyrosine kinase activity in vitro. Although cells expressing Phe-807 receptors were able to respond to CSF-1, the changes in growth rate and cell morphology were significantly less than seen with wild-type receptors, and the induction of early response genes was also slightly lower than for the wild-type receptor. In contrast, Phe-807 receptors were equivalent to wild-type receptors when tested for their ability to interact with phosphatidylinositol-3 kinase. These findings indicate that phosphorylation of Tyr-807 may be important for full activation of the receptor.

Jähner, D., Hunter, T. The stimulation of quiescent rat fibroblasts by v-src and v-fps oncogenic protein-tyrosine kinases leads to the induction of a subset of immediate early genes. (1991) Oncogene. 6(7):1259-68.

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Jähner, D., Hunter, T. The ras-related gene rhoB is an immediate-early gene inducible by v-Fps, epidermal growth factor, and platelet-derived growth factor in rat fibroblasts. (1991) Molecular and Cellular Biology. 11(7):3682-90.

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Pines, J., Hunter, T. Human cell division: the involvement of cyclins A and B1, and multiple cdc2s. (1991) Cold Spring Harbor Symposia on Quantitative Biology. 56:449-63.

Meisenhelder, J., Hunter, T. Phosphorylation of phospholipase C in vivo and in vitro. (1991) Meth. Enzymol. 197:288-305.

Boyle, W.J., van der Geer, P., Hunter, T. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. (1991) Meth. Enzymol. 201:110-49.

Nevins, J.R., Chellappan, S.P., Mudryj, M., Hiebert, S., Devoto, S., Horowitz, J., Hunter, T., Pines, J. E2F transcription factor is a target for the RB protein and the cyclin A protein. (1991) Cold Spring Harbor Symposia on Quantitative Biology. 56:157-62.

Hunter, T. Protein kinase classification. (1991) Meth. Enzymol. 200:3-37.

Inoue, J., Kerr, L.D., Ransone, L.J., Bengal, E., Hunter, T., Verma, I.M. c-rel activates but v-rel suppresses transcription from kappa B sites. (1991) Proceedings of the National Academy of Sciences of the United States of America. 88(9):3715-9.

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Boyle, W.J., Smeal, T., Defize, L.H., Angel, P., Woodgett, J.R., Karin, M., Hunter, T. Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity. (1991) Cell. 64(3):573-84.

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Hunter, T. Protein-serine kinase receptors? (1991) Current Biology. 1(1):15-6.

Hunter, T. Cooperation between oncogenes. (1991) Cell. 64(2):249-70.

Middlemas, D.S., Lindberg, R.A., Hunter, T. trkB, a neural receptor protein-tyrosine kinase: evidence for a full-length and two truncated receptors. (1991) Molecular and Cellular Biology. 11(1):143-53.

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Cochet, C., Filhol, O., Payrastre, B., Hunter, T., Gill, G.N. Interaction between the epidermal growth factor receptor and phosphoinositide kinases. (1991) Journal of Biological Chemistry. 266(1):637-44.

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Lindberg, R.A., Hunter, T. cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases. (1990) Molecular and Cellular Biology. 10(12):6316-24.

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Yamashita, K., Yasuda, H., Pines, J., Yasumoto, K., Nishitani, H., Ohtsubo, M., Hunter, T., Sugimura, T., Nishimoto, T. Okadaic acid, a potent inhibitor of type 1 and type 2A protein phosphatases, activates cdc2/H1 kinase and transiently induces a premature mitosis-like state in BHK21 cells. (1990) EMBO Journal. 9(13):4331-8.

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Bull, P., Morley, K.L., Hoekstra, M.F., Hunter, T., Verma, I.M. The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain. (1990) Molecular and Cellular Biology. 10(10):5473-85.

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Pines, J., Hunter, T. Human cyclin A is adenovirus E1A-associated protein p60 and behaves differently from cyclin B. (1990) Nature. 346(6286):760-3. DOI: 10.1038/346760a0

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van der Geer, P., Hunter, T. Identification of tyrosine 706 in the kinase insert as the major colony-stimulating factor 1 (CSF-1)-stimulated autophosphorylation site in the CSF-1 receptor in a murine macrophage cell line. (1990) Molecular and Cellular Biology. 10(6):2991-3002.

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Isacke, C.M., van der Geer, P., Hunter, T., Trowbridge, I.S. p180, a novel recycling transmembrane glycoprotein with restricted cell type expression. (1990) Molecular and Cellular Biology. 10(6):2606-18.

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Pines, J., Hunter, T. p34cdc2: the S and M kinase? (1990) New Biol. 2(5):389-401.

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Hunter, T., Lindberg, R.A., Middlemas, D.S. Novel receptor protein-tyrosine kinases. (1990) Adv. Second Messenger Phosphoprotein Res. 24:260-5.

Amiguet, P., D’Eustachio, P., Kristensen, T., Wetsel, R.A., Saris, C.J., Hunter, T., Chaplin, D.D., Tack, B.F. Structure and chromosome assignment of the murine p36 (calpactin I heavy chain) gene. (1990) Biochemistry. 29(5):1226-32.

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Gould, K.L., Bretscher, A., Esch, F.S., Hunter, T. cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1. (1989) EMBO Journal. 8(13):4133-42.

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Hunter, T. Protein modification: phosphorylation on tyrosine residues. (1989) Current Opinion in Cell Biology. 1(6):1168-81.

Bull, P., Hunter, T., Verma, I.M. Transcriptional induction of the murine c-rel gene with serum and phorbol-12-myristate-13-acetate in fibroblasts. (1989) Molecular and Cellular Biology. 9(11):5239-43.

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Defize, L.H., Boonstra, J., Meisenhelder, J., Kruijer, W., Tertoolen, L.G., Tilly, B.C., Hunter, T., van Bergen en Henegouwen, P.M., Moolenaar, W.H., de Laat, S.W. Signal transduction by epidermal growth factor occurs through the subclass of high affinity receptors. (1989) Journal of Cell Biology. 109(5):2495-507.

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Freed, E., Gailit, J., van der Geer, P., Ruoslahti, E., Hunter, T. A novel integrin beta subunit is associated with the vitronectin receptor alpha subunit (alpha v) in a human osteosarcoma cell line and is a substrate for protein kinase C. (1989) EMBO Journal. 8(10):2955-65.

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Hunter, T. Protein-tyrosine phosphatases: the other side of the coin. (1989) Cell. 58(6):1013-6.

Pines, J., Hunter, T. Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2. (1989) Cell. 58(5):833-46.

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Meisenhelder, J., Suh, P.G., Rhee, S.G., Hunter, T. Phospholipase C-gamma is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro. (1989) Cell. 57(7):1109-22.

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Hunter, T. The functions of oncogene products. (1989) Prog. Clin. Biol. Res. 288:25-34.

Nunn, M.F., Hunter, T. The ets sequence is required for induction of erythroblastosis in chickens by avian retrovirus E26. (1989) Journal of Virology. 63(1):398-402.

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Isacke, C.M., Lindberg, R.A., Hunter, T. Synthesis of p36 and p35 is increased when U-937 cells differentiate in culture but expression is not inducible by glucocorticoids. (1989) Molecular and Cellular Biology. 9(1):232-40.

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Gould, K.L., Bilezikjian, L.M., Hunter, T. AtT20 cells express modified forms of pp60c-src. (1989) Molecular Endocrinology. 3(1):79-88. DOI: 10.1210/mend-3-1-79

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Lindberg, R.A., Thompson, D.P., Hunter, T. Identification of cDNA clones that code for protein-tyrosine kinases by screening expression libraries with antibodies against phosphotyrosine. (1988) Oncogene. 3(6):629-33.

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Weinmaster, G.A., Hunter, T. Investigation of the role of P130gag-fps in transformation: generation and use of a temperature-sensitive mutant P130gag-fps. (1988) Journal of Virology. 62(10):3849-54.

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Meisenhelder, J., Hunter, T. Radioactive protein-labelling techniques. (1988) Nature. 335(6186):120. DOI: 10.1038/335120a0

Defize, L.H., Arndt-Jovin, D.J., Jovin, T.M., Boonstra, J., Meisenhelder, J., Hunter, T., de Hey, H.T., de Laat, S.W. A431 cell variants lacking the blood group A antigen display increased high affinity epidermal growth factor-receptor number, protein-tyrosine kinase activity, and receptor turnover. (1988) Journal of Cell Biology. 107(3):939-49.

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The epidermal growth factor receptor (EGF-R) of human A431 cells bears an antigenic determinant that is closely related to the human blood group A carbohydrate structure. Labeling studies with blood group A reactive anti-EGF-R monoclonal antibodies and various lectins revealed that A431 cultures are heterogeneous with respect to blood group A expression. We have isolated clonal variants of these cells that either express (A431A+ cells) or completely lack (A431A- cells) the blood group A specific N-acetyl-D-galactosamine (GalNAc) residue. We show that this difference is due to the absence of a UDP-GalNAc:Gal transferase activity in A431A- cells. Subsequently, we have compared EGF-R functioning in these cell lines. Scatchard analysis of EGF-binding shows that in A431A- cells 6.3% of the EGF-R belongs to a high affinity subclass (Kd = 0.4 nM) while in A431A+ this subclass represents only 3.2% of the total receptor pool. The elevated level of high affinity receptors in A431A- cells is accompanied by a parallel increase in receptor protein- tyrosine kinase activity. In membrane preparations of A431A- cells, receptor autophosphorylation as well as phosphorylation of a tyrosine-containing peptide substrate is 2-3-fold higher as compared with A431A+ cells. In intact A431A-cells, the difference in receptor activity is measured as a 2-3-fold elevated level of receptor phosphorylation and a 2-3-fold higher abundance of phosphotyrosine in total cellular protein in A431A- cells. In addition, [35S]methionine pulse-chase experiments showed a ligand-independent increase in turnover of EGF-R in A431A- cells: the receptor’s half life in these cells is 10 h as compared with 17 h in A431A+ cells. Our results suggest a possible involvement of GalNAc residue(s) in determining EGF-R affinity, protein-tyrosine kinase activity and turnover in A431 cells. Furthermore, our results indicate that high affinity EGF-R are the biologically active species with respect to protein-tyrosine kinase activity.

Gould, K.L., Hunter, T. Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity. (1988) Molecular and Cellular Biology. 8(8):3345-56.

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Chiu, R., Boyle, W.J., Meek, J., Smeal, T., Hunter, T., Karin, M. The c-Fos protein interacts with c-Jun/AP-1 to stimulate transcription of AP-1 responsive genes. (1988) Cell. 54(4):541-52.

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Hanks, S.K., Quinn, A.M., Hunter, T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. (1988) Science. 241(4861):42-52.

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Weinmaster, G.A., Middlemas, D.S., Hunter, T. A major site of tyrosine phosphorylation within the SH2 domain of Fujinami sarcoma virus P130gag-fps is not required for protein-tyrosine kinase activity or transforming potential. (1988) Journal of Virology. 62(6):2016-25.

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Hunter, T., Angel, P., Boyle, W.J., Chiu, R., Freed, E., Gould, K.L., Isacke, C.M., Karin, M., Lindberg, R.A., van der Geer, P. Targets for signal-transducing protein kinases. (1988) Cold Spring Harbor Symposia on Quantitative Biology. 53 Pt 1:131-42.

Cartwright, C.A., Simantov, R., Cowan, W.M., Hunter, T., Eckhart, W. pp60c-src expression in the developing rat brain. (1988) Proceedings of the National Academy of Sciences of the United States of America. 85(10):3348-52.

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Hunter, T. The Ca2+/phospholipid-binding proteins of the submembraneous skeleton. (1988) Advances in Experimental Medicine and Biology. 234:169-93.

Angel, P., Allegretto, E.A., Okino, S.T., Hattori, K., Boyle, W.J., Hunter, T., Karin, M. Oncogene jun encodes a sequence-specific trans-activator similar to AP-1. (1988) Nature. 332(6160):166-71. DOI: 10.1038/332166a0

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Hunter, T. A thousand and one protein kinases. (1987) Cell. 50(6):823-9.

Bilezikjian, L.M., Woodgett, J.R., Hunter, T., Vale, W.W. Phorbol ester-induced down-regulation of protein kinase C abolishes vasopressin-mediated responses in rat anterior pituitary cells. (1987) Molecular Endocrinology. 1(8):555-60. DOI: 10.1210/mend-1-8-555

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Saris, C.J., Kristensen, T., D’Eustachio, P., Hicks, L.J., Noonan, D.J., Hunter, T., Tack, B.F. cDNA sequence and tissue distribution of the mRNA for bovine and murine p11, the S100-related light chain of the protein-tyrosine kinase substrate p36 (calpactin I). (1987) Journal of Biological Chemistry. 262(22):10663-71.

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Woodgett, J.R., Hunter, T. Regulation of protein kinase C by activators, Ca2+, and phosphorylation. (1987) Prog. Clin. Biol. Res. 249:237-47.

Cartwright, C.A., Simantov, R., Kaplan, P.L., Hunter, T., Eckhart, W. Alterations in pp60c-src accompany differentiation of neurons from rat embryo striatum. (1987) Molecular and Cellular Biology. 7(5):1830-40.

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Woodgett, J.R., Hunter, T. Isolation and characterization of two distinct forms of protein kinase C. (1987) Journal of Biological Chemistry. 262(10):4836-43.

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Woodgett, J.R., Hunter, T. Immunological evidence for two physiological forms of protein kinase C. (1987) Molecular and Cellular Biology. 7(1):85-96.

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Our recently described purification scheme for rat brain protein kinase C yields an enzyme consisting of a 78/80-kilodalton (kDa) doublet upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis (submitted for publication). Antisera against this preparation were raised in two rabbits. One of the antisera detected only the 80-kDa component by immunoblotting of purified protein kinase C and immunoprecipitated an 80-kDa [35S]methionine-labeled protein from a variety of human, rodent, and bovine cells, which was shown to represent protein kinase C by comparative one-dimensional peptide mapping. In contrast, the second antiserum detected both 78- and 80-kDa enzyme forms by immunoblotting and immunoprecipitated a [35S]methionine-labeled 78/80-kDa doublet from mammalian cells. One-dimensional peptide maps of these 78- and 80-kDa proteins were similar to those derived from the 78- and 80-kDa forms of purified protein kinase C, respectively. The two forms were not related by either partial proteolysis or differential phosphorylation, showing that two distinct forms of this enzyme exist in mammalian cells. Treatment of mouse B82 L cells with 2.5 micrograms of 12-O-tetradecanoylphorbol-13-acetate (TPA) per ml for 18 h resulted in complete loss of immunoprecipitable protein kinase C with a half time of disappearance of 48 min. Since the normal half-life of protein kinase C was greater than 24 h and the biosynthetic rate of the protein was not decreased after 18 h by TPA treatment, TPA induces down-regulation by increasing the degradation rate of the enzyme. Treatment of cells with 50 ng of TPA per ml followed by resolution of the membrane and cytosol in the presence of ethylene glycol-bis(beta-aminoethyl ether)N,N,N’,N’-tetraacetic acid (EGTA) promoted an apparent translocation of both 78- and 80-kDa proteins from the cytosol to the membrane fraction. A similar translocation was effected by cell lysis in the presence of Ca2+, indicating the subcellular localization of protein kinase C to be sensitive to the presence of both activators and micromolar amounts of Ca2+.

Woodgett, J.R., Gould, K.L., Hunter, T. Substrate specificity of protein kinase C. Use of synthetic peptides corresponding to physiological sites as probes for substrate recognition requirements. (1986) European Journal of Biochemistry. 161(1):177-84.

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Isacke, C.M., Meisenhelder, J., Brown, K.D., Gould, K.L., Gould, S.J., Hunter, T. Early phosphorylation events following the treatment of Swiss 3T3 cells with bombesin and the mammalian bombesin-related peptide, gastrin-releasing peptide. (1986) EMBO Journal. 5(11):2889-98.

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Glenney, J.R., Boudreau, M., Galyean, R., Hunter, T., Tack, B. Association of the S-100-related calpactin I light chain with the NH2-terminal tail of the 36-kDa heavy chain. (1986) Journal of Biological Chemistry. 261(23):10485-8.

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Kristensen, T., Saris, C.J., Hunter, T., Hicks, L.J., Noonan, D.J., Glenney, J.R., Tack, B.F. Primary structure of bovine calpactin I heavy chain (p36), a major cellular substrate for retroviral protein-tyrosine kinases: homology with the human phospholipase A2 inhibitor lipocortin. (1986) Biochemistry. 25(16):4497-503.

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Tripp, M.L., Piñon, R., Meisenhelder, J., Hunter, T. Identification of phosphoproteins correlated with proliferation and cell cycle arrest in Saccharomyces cerevisiae: positive and negative regulation by cAMP-dependent protein kinase. (1986) Proceedings of the National Academy of Sciences of the United States of America. 83(16):5973-7.

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Saris, C.J., Tack, B.F., Kristensen, T., Glenney, J.R., Hunter, T. The cDNA sequence for the protein-tyrosine kinase substrate p36 (calpactin I heavy chain) reveals a multidomain protein with internal repeats. (1986) Cell. 46(2):201-12.

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Hunter, T. Cancer. Cell growth control mechanisms. (1986) Nature. 322(6074):14-6. DOI: 10.1038/322014a0

Isacke, C.M., Trowbridge, I.S., Hunter, T. Modulation of p36 phosphorylation in human cells: studies using anti-p36 monoclonal antibodies. (1986) Molecular and Cellular Biology. 6(7):2745-51.

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Gould, K.L., Woodgett, J.R., Isacke, C.M., Hunter, T. The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo. (1986) Molecular and Cellular Biology. 6(7):2738-44.

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Patschinsky, T., Hunter, T., Sefton, B.M. Phosphorylation of the transforming protein of Rous sarcoma virus: direct demonstration of phosphorylation of serine 17 and identification of an additional site of tyrosine phosphorylation in p60v-src (1986) Journal of Virology. 59(1):73-81.

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Sefton, B.M., Hunter, T. From c-src to v-src, or the case of the missing C terminus. (1986) Cancer Surveys. 5(2):159-72.

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Cartwright, C.A., Kaplan, P.L., Cooper, J.A., Hunter, T., Eckhart, W. Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen. (1986) Molecular and Cellular Biology. 6(5):1562-70.

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Cooper, J.A., Gould, K.L., Cartwright, C.A., Hunter, T. Tyr527 is phosphorylated in pp60c-src: implications for regulation. (1986) Science. 231(4744):1431-4.

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Gould, K.L., Cooper, J.A., Bretscher, A., Hunter, T. The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein. (1986) Journal of Cell Biology. 102(2):660-9.

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Cooper, J.A., Hunter, T. Major substrate for growth factor-activated protein-tyrosine kinases is a low-abundance protein. (1985) Molecular and Cellular Biology. 5(11):3304-9.

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Gould, K.L., Woodgett, J.R., Cooper, J.A., Buss, J.E., Shalloway, D., Hunter, T. Protein kinase C phosphorylates pp60src at a novel site. (1985) Cell. 42(3):849-57.

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Coussens, P.M., Cooper, J.A., Hunter, T., Shalloway, D. Restriction of the in vitro and in vivo tyrosine protein kinase activities of pp60c-src relative to pp60v-src. (1985) Molecular and Cellular Biology. 5(10):2753-63.

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Hunter, T., Cooper, J.A. Protein-tyrosine kinases. (1985) Annual Review of Biochemistry. 54:897-930. DOI: 10.1146/annurev.bi.54.070185.004341

Hunter, T. Cell-surface proteins. At last the insulin receptor. (1985) Nature. 313(6005):740-1.

Hunter, T., Alexander, C.B., Cooper, J.A. Protein phosphorylation and growth control. (1985) Ciba Found. Symp. 116:188-204.

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Kruijer, W., Cooper, J.A., Hunter, T., Verma, I.M. Platelet-derived growth factor induces rapid but transient expression of the c-fos gene and protein. (1984) Nature. 312(5996):711-6.

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Voronova, A.F., Buss, J.E., Patschinsky, T., Hunter, T., Sefton, B.M. Characterization of the protein apparently responsible for the elevated tyrosine protein kinase activity in LSTRA cells. (1984) Molecular and Cellular Biology. 4(12):2705-13.

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Hunter, T., Ling, N., Cooper, J.A. Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane. (1984) Nature. 311(5985):480-3.

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The receptor for epidermal growth factor (EGF) is a 170,000-180,000 molecular weight single-chain glycoprotein of 1,186 amino acids. Its sequence suggests that it has an external EGF-binding domain, formed by the NH2-terminal 621 amino acids, linked to a cytoplasmic region by a single membrane-spanning segment. In the cytoplasmic portion, starting 50 residues from the membrane, there is a 250-residue stretch similar to the catalytic domain of the src gene family of retroviral tyrosine protein kinases, and, indeed, a tyrosine-specific protein kinase activity intrinsic to the receptor is stimulated when EGF is bound. Increased tyrosine phosphorylation of cellular proteins, detected in A431 cells following EGF binding, may be important in the mitogenic signal pathway. Tumour promoters such as 12-O-tetradecanoyl-phorbol-13-acetate (TPA), counteract this increase, as well as causing loss of a high affinity class of EGF binding sites. The major receptor for TPA has been identified as the serine/threonine-specific Ca2+/phospholipid-dependent diacylglycerol-activated protein kinase, protein kinase C. By substituting for diacylglycerol, TPA stimulates protein kinase C. Protein kinase C phosphorylates purified EGF receptor at specific sites, and this reduces EGF-stimulated tyrosine protein kinase activity. TPA treatment of A431 cells increases serine and threonine phosphorylation of the EGF receptor at the same sites, which suggests that the reduction of EGF receptor kinase activity in TPA-treated cells is a consequence of the receptor’s phosphorylation by the kinase. We have attempted to identify these phosphorylation sites and show here that protein kinase C phosphorylates threonine 654 in the human EGF receptor. This threonine is in a very basic sequence nine residues from the cytoplasmic face of the plasma membrane in the region before the protein kinase domain; it is thus in a position to modulate signalling between this internal domain and the external EGF-binding domain.

Hunter, T. The epidermal growth factor receptor gene and its product. (1984) Nature. 311(5985):414-6.

Hunter, T., Gould, K.L., Cooper, J.A. Tyrosine protein kinases, viral transformation and the control of cell proliferation. (1984) Biochemical Society Transactions. 12(5):757-9.

Hunter, T. Oncogenes and proto-oncogenes: how do they differ? (1984) J. Natl. Cancer Inst. 73(4):773-86.

Hunter, T. The proteins of oncogenes. (1984) Sci. Am. 251(2):70-9.

Cooper, J.A., Esch, F.S., Taylor, S.S., Hunter, T. Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro. (1984) Journal of Biological Chemistry. 259(12):7835-41.

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Hunter, T., Cooper, J.A. Tyrosine protein kinases and their substrates: an overview. (1984) Adv Cyclic Nucleotide Protein Phosphorylation Res. 17:443-55.

Donoghue, D.J., Anderson, C., Hunter, T., Kaplan, P.L. Transmission of the polyoma virus middle T gene as the oncogene of a murine retrovirus. (1984) Nature. 308(5961):748-50.

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Cochet, C., Gill, G.N., Meisenhelder, J., Cooper, J.A., Hunter, T. C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity. (1984) Journal of Biological Chemistry. 259(4):2553-8.

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Gould, K.L., Cooper, J.A., Hunter, T. The 46,000-dalton tyrosine protein kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues. (1984) Journal of Cell Biology. 98(2):487-97.

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Hunter, T., Hutchinson, M.A., Eckhart, W. Polyoma middle-sized T antigen can be phosphorylated on tyrosine at multiple sites in vitro. (1984) EMBO Journal. 3(1):73-9.

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Cooper, J.A., Sefton, B.M., Hunter, T. Diverse mitogenic agents induce the phosphorylation of two related 42,000-dalton proteins on tyrosine in quiescent chick cells. (1984) Molecular and Cellular Biology. 4(1):30-7.

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Sefton, B.M., Hunter, T. Tyrosine protein kinases. (1984) Adv Cyclic Nucleotide Protein Phosphorylation Res. 18:195-226.

Cooper, J.A., Scolnick, E.M., Ozanne, B., Hunter, T. Epidermal growth factor receptor metabolism and protein kinase activity in human A431 cells infected with Snyder-Theilen feline sarcoma virus or harvey or Kirsten murine sarcoma virus. (1983) Journal of Virology. 48(3):752-64.

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When human A431 cells, which carry high numbers of epidermal growth factor (EGF) receptors, are exposed to EGF, the total content of phosphotyrosine in cell protein is increased, the EGF receptor becomes phosphorylated at tyrosine, and new phosphotyrosine-containing 36,000- and 81,000-dalton proteins are detected. We examined the properties of A431 cells infected with Snyder-Theilen feline sarcoma virus, whose transforming protein has associated tyrosine protein kinase activity, and Harvey and Kirsten sarcoma viruses, whose transforming proteins do not. In all cases, the infected cells were more rounded and more capable of anchorage-independent growth than the uninfected cells. EGF receptors were assayed functionally by measuring EGF binding and structurally by metabolic labeling and immunoprecipitation. In no case did infection appear to alter the rate of EGF receptor synthesis, but infection reduced EGF receptor stability by about 50% for cloned Harvey sarcoma virus-infected cells and by 80% for cloned feline sarcoma virus-infected cells. The corresponding reductions in EGF binding were 70 and 90%, respectively. The proteins of feline sarcoma virus-infected A431 cells contained an increased amount of phosphotyrosine, and the 36,000- and 81,000-dalton phosphoproteins were detected. The EGF receptor was not detectably phosphorylated at tyrosine, however, unless the cells were exposed to EGF. The Harvey and Kirsten sarcoma virus-infected cells did not exhibit elevated levels of phosphotyrosine either in the total cell proteins or in the EGF receptor, nor were the 36,000- and 81,000-dalton proteins detectable. However, these phosphoproteins were found in the infected cells after EGF treatment. Thus, all of the infected A431 cells exhibited reduced EGF binding and increased degradation of EGF receptors, yet their patterns of protein phosphorylation were distinct from those of EGF-treated A431 cells.

Kiberstis, P.A., Pessi, A., Atherton, E., Jackson, R., Hunter, T., Zimmern, D. Analysis of in vitro and in vivo products of the TMV 30kDa open reading frame using antisera raised against a synthetic peptide. (1983) FEBS Lett. 164(2):355-360. DOI: 10.1016/0014-5793(83)80316-0

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Zimmern, D., Hunter, T. Point mutation in the 30-K open reading frame of TMV implicated in temperature-sensitive assembly and local lesion spreading of mutant Ni 2519. (1983) EMBO Journal. 2(11):1893-900.

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Nigg, E.A., Cooper, J.A., Hunter, T. Immunofluorescent localization of a 39,000-dalton substrate of tyrosine protein kinases to the cytoplasmic surface of the plasma membrane. (1983) Journal of Cell Biology. 96(6):1601-9.

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Cooper, J.A., Sefton, B.M., Hunter, T. Detection and quantification of phosphotyrosine in proteins. (1983) Meth. Enzymol. 99:387-402.

Papkoff, J., Nigg, E.A., Hunter, T. The transforming protein of Moloney murine sarcoma virus is a soluble cytoplasmic protein. (1983) Cell. 33(1):161-72.

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Cooper, J., Nakamura, K.D., Hunter, T., Weber, M.J. Phosphotyrosine-containing proteins and expression of transformation parameters in cells infected with partial transformation mutants of Rous sarcoma virus. (1983) Journal of Virology. 46(1):15-28.

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Cooper, J.A., Reiss, N.A., Schwartz, R.J., Hunter, T. Three glycolytic enzymes are phosphorylated at tyrosine in cells transformed by Rous sarcoma virus. (1983) Nature. 302(5905):218-23.

Papkoff, J., Hunter, T. Detection of an 85,000-dalton phosphoprotein in ts110 murine sarcoma virus-infected cells with antiserum against a v-mos peptide. (1983) Journal of Virology. 45(3):1177-82.

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Hunter, T., Cooper, J.A. Role of tyrosine phosphorylation in malignant transformation by viruses and in cellular growth control. (1983) Progress in Nucleic Acid Research and Molecular Biology. 29:221-32.

Hunter, T., Jackson, R., Zimmern, D. Multiple proteins and subgenomic mRNAs may be derived from a single open reading frame on tobacco mosaic virus RNA. (1983) Nucleic Acids Research. 11(3):801-21.

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Donoghue, D.J., Hunter, T. Recombinational junctions of variants of Moloney murine sarcoma virus: generation and divergence of a mammalian transforming gene. (1983) Journal of Virology. 45(2):607-17.

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Cooper, J.A., Hunter, T. Regulation of cell growth and transformation by tyrosine-specific protein kinases: the search for important cellular substrate proteins. (1983) Current Topics in Microbiology and Immunology. 107:125-61.

Cooper, J.A., Hunter, T. Identification and characterization of cellular targets for tyrosine protein kinases. (1983) Journal of Biological Chemistry. 258(2):1108-15.

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Sefton, B.M., Hunter, T., Cooper, J.A. Some lymphoid cell lines transformed by Abelson murine leukemia virus lack a major 36,000-dalton tyrosine protein kinase substrate. (1983) Molecular and Cellular Biology. 3(1):56-63.

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Cooper, J.A., Bowen-Pope, D.F., Raines, E., Ross, R., Hunter, T. Similar effects of platelet-derived growth factor and epidermal growth factor on the phosphorylation of tyrosine in cellular proteins. (1982) Cell. 31(1):263-73.

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Nigg, E.A., Sefton, B.M., Hunter, T., Walter, G., Singer, S.J. Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide. (1982) Proceedings of the National Academy of Sciences of the United States of America. 79(17):5322-6.

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Adkins, B., Hunter, T. Two structurally and functionally different forms of the transforming protein of PRC II avian sarcoma virus. (1982) Molecular and Cellular Biology. 2(8):890-6.

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Papkoff, J., Hunter, T. Identification of proteins encoded by the Gazdar murine sarcoma virus genome by in vitro translation and comparison with Moloney murine sarcoma virus 124. (1982) Journal of Virology. 43(2):533-43.

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Adkins, B., Hunter, T., Sefton, B.M. The transforming proteins of PRCII virus and Rous sarcoma virus form a complex with the same two cellular phosphoproteins. (1982) Journal of Virology. 43(2):448-55.

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Cooper, J.A., Hunter, T. Discrete primary locations of a tyrosine-protein kinase and of three proteins that contain phosphotyrosine in virally transformed chick fibroblasts. (1982) Journal of Cell Biology. 94(2):287-96.

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Walter, G., Hutchinson, M.A., Hunter, T., Eckhart, W. Purification of polyoma virus medium-size tumor antigen by immunoaffinity chromatography. (1982) Proceedings of the National Academy of Sciences of the United States of America. 79(13):4025-9.

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Hunter, T. Phosphotyrosine – a new protein modification. (1982) Trends in Biochemical Sciences. 7(7):246-249. DOI: 10.1016/0968-0004(82)90035-4

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Papkoff, J., Verma, I.M., Hunter, T. Detection of a transforming gene product in cells transformed by Moloney murine sarcoma virus. (1982) Cell. 29(2):417-26.

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Sefton, B.M., Hunter, T., Nigg, E.A., Singer, S.J., Walter, G. Cytoskeletal targets for viral transforming proteins with tyrosine protein kinase activity. (1982) Cold Spring Harbor Symposia on Quantitative Biology. 46 Pt 2:939-51.

Hunter, T. Synthetic peptide substrates for a tyrosine protein kinase. (1982) Journal of Biological Chemistry. 257(9):4843-8.

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Donoghue, D.J., Hunter, T. A generalized method of subcloning DNA fragments by restriction site reconstruction: application to sequencing the amino-terminal coding region of the transforming gene of Gazdar murine sarcoma virus. (1982) Nucleic Acids Research. 10(8):2549-64.

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Papkoff, J., Lai, M.H., Hunter, T. Analysis of v-mos encoded proteins in cells transformed by several related murine sarcoma viruses. (1982) J. Cell. Biochem. 19(4):349-62. DOI: 10.1002/jcb.240190405

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Sefton, B.M., Patschinsky, T., Berdot, C., Hunter, T., Elliott, T. Phosphorylation and metabolism of the transforming protein of Rous sarcoma virus. (1982) Journal of Virology. 41(3):813-20.

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Patschinsky, T., Hunter, T., Esch, F.S., Cooper, J.A., Sefton, B.M. Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation. (1982) Proceedings of the National Academy of Sciences of the United States of America. 79(4):973-7.

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Donoghue, D.J., Hunter, T. Expression of transforming region of Moloney murine sarcoma virus in Escherichia coli as a fusion protein with small tumor antigen of polyoma virus. (1982) Proceedings of the National Academy of Sciences of the United States of America. 79(3):800-4.

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Cooper, J.A., Hunter, T. Similarities and differences between the effects of epidermal growth factor and Rous sarcoma virus. (1981) Journal of Cell Biology. 91(3 Pt 1):878-83.

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Papkoff, J., Lai, M.H., Hunter, T., Verma, I.M. Analysis of transforming gene products from Moloney murine sarcoma virus. (1981) Cell. 27(1 Pt 2):109-19.

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Walter, G., Hutchinson, M.A., Hunter, T., Eckhart, W. Antibodies specific for the polyoma virus middle-size tumor antigen. (1981) Proceedings of the National Academy of Sciences of the United States of America. 78(8):4882-6.

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Adkins, B., Hunter, T. Identification of a packaged cellular mRNA in virions of rous sarcoma virus. (1981) Journal of Virology. 39(2):471-80.

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Hunter, T., Cooper, J.A. Epidermal growth factor induces rapid tyrosine phosphorylation of proteins in A431 human tumor cells. (1981) Cell. 24(3):741-52.

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Cooper, J.A., Hunter, T. Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins. (1981) Molecular and Cellular Biology. 1(5):394-407.

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Sefton, B.M., Hunter, T., Ball, E.H., Singer, S.J. Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. (1981) Cell. 24(1):165-74.

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Sefton, B.M., Hunter, T., Raschke, W.C. Evidence that the Abelson virus protein functions in vivo as a protein kinase that phosphorylates tyrosine. (1981) Proceedings of the National Academy of Sciences of the United States of America. 78(3):1552-6.

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Cooper, J.A., Hunter, T. Changes in protein phosphorylation in Rous sarcoma virus-transformed chicken embryo cells. (1981) Molecular and Cellular Biology. 1(2):165-78.

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Eckhart, W., Delbrück, S., Deininger, P., Friedmann, T., Hunter, T. A mutation increasing the size of the polyoma virion proteins, VP2 and VP3. (1981) Virology. 109(1):35-46.

Hunter, T. Protein phosphorylated by the RSV transforming function. (1980) Cell. 22(3):647-8.

Mann, K., Hunter, T. Phosphorylation of SV40 large T antigen in SV40 nucleoprotein complexes. (1980) Virology. 107(2):526-32.

Sefton, B.M., Hunter, T., Beemon, K., Eckhart, W. Evidence that the phosphorylation of tyrosine is essential for cellular transformation by Rous sarcoma virus. (1980) Cell. 20(3):807-16.

Hunter, T., Sefton, B.M., Beemon, K. Studies on the structure and function of the avian sarcoma virus transforming-gene product. (1980) Cold Spring Harbor Symposia on Quantitative Biology. 44 Pt 2,:931-41.

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Sefton, B.M., Hunter, T., Beemon, K. Relationship of polypeptide products of the transforming gene of Rous sarcoma virus and the homologous gene of vertebrates. (1980) Proceedings of the National Academy of Sciences of the United States of America. 77(4):2059-63.

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Hunter, T., Hutchinson, M.A., Eckhart, W., Friedmann, T., Esty, A., La Porte, P., Deininger, P. Organization of T antigens in the polyoma virus genome. (1980) Cold Spring Harbor Symposia on Quantitative Biology. 44 Pt 1,:131-9.

Hunter, T., Sefton, B.M. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. (1980) Proceedings of the National Academy of Sciences of the United States of America. 77(3):1311-5.

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Papkoff, J., Hunter, T., Beemon, K. In vitro translation of virion RNA from Moloney murine sarcoma virus. (1980) Virology. 101(1):91-103.

Sefton, B.M., Hunter, T., Beemon, K. Temperature-sensitive transformation by Rous sarcoma virus and temperature-sensitive protein kinase activity. (1980) Journal of Virology. 33(1):220-9.

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The transforming protein of Rous sarcoma virus, p60src, has associated with it a protein kinase activity. We examined whether a correlation exists between the cellular concentration of enzymatically active p60src and the degree to which chick cells are transformed by mutants of Rous sarcoma virus which are temperature-sensitive for transformation. Such a correlation does exist, but cells infected with some mutants could be shown to contain, at the nonpermissive temperature, an amount of protein kinase activity equal to 30 to 40% of that in a wild-type transformed cell. We quantified the amount of virus-induced protein kinase activity by precipitation of p60src with an excess of antitumor antiserum. Our initial measurements of activity were serious underestimates, due to the lability of the protein kinase activity associated with p60src of at least four temperature-sensitive mutants. In fact, no activity at all was associated with p60src of tsLA90 when immunoprecipitation was performed by standard means. However, when immunoprecipitation was performed with procedures which minimize inactivation, it became apparent both that cells transformed by tsLA90 contained protein kinase activity and that cells infected with either NY68 or BK5 contained at the nonpermissive temperature, one-third to one-half as much activity as wild-type transformed cells. This level of activity was much more than that arising from p60sarc in uninfected cells. In uninfected cells we found an amount of protein kinase activity which varied from 3 to 5% as much as that in a virally transformed cell. The lability of the protein kinase activity of each of these mutants is a further demonstration that this activity is essential for the transformation of cells by Rous sarcoma virus. So as to explain the high protein kinase levels in cells infected with NY68 and BK5 at the nonpermissive temperature, the idea that transformation may be a response to a small quantitative change in the total activity of p60src and the possibility that there may be more than one viral function which is essential for transformation are discussed.

Hunter, T., Hutchinson, M.A., Eckhart, W., Friedmann, T., Esty, A., LaPorte, P., Deininger, P. Regions of the polyoma genome coding for T antigens. (1979) Nucleic Acids Research. 7(8):2275-88.

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Eckhart, W., Hutchinson, M.A., Hunter, T. An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates. (1979) Cell. 18(4):925-33.

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Garrels, J.I., Hunter, T. Post-translational modification of actins synthesized in vitro. (1979) Biochimica et Biophysica Acta. 564(3):517-25.

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Lawrence, C., Hunter, T., Walter, G. Characterization of the simian virus 40-specific messenger RNAs isolated from HeLa cells infected with the non-defective adenovirus 2-simian virus 40 hybrid viruses Ad2+ND2 and Ad2+ND4. (1979) Journal of Molecular Biology. 134(1):95-108.

Hunter, T. Functional characterization of the early and late mRNAs of simian virus 40. (1979) Virology. 95(2):511-22.

Westphal, H., Lai, S.P., Lawrence, C., Hunter, T., Walter, G. Mosaic adenovirus-SV40 RNA specified by the non-defective hybrid virus Ad2+ND4. (1979) Journal of Molecular Biology. 130(3):337-51.

Sefton, B.M., Hunter, T., Beemon, K. Product of in vitro translation of the Rous sarcoma virus src gene has protein kinase activity. (1979) Journal of Virology. 30(1):311-8.

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Beemon, K., Hunter, T., Sefton, B.M. Polymorphism of avian sarcoma virus src proteins. (1979) Journal of Virology. 30(1):190-200.

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Linke, H.K., Hunter, T., Walter, G. Structural relationship between the 100,000- and 17,000- molecular-weight T antigens of simian virus 40 (SV40) as deduced by comparison with the SV40-specific proteins coded by the nondefective adenov (1979) Journal of Virology. 29(1):390-4.

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Mann, K., Hunter, T. Association of simian virus 40 T antigen with simian virus 40 nucleoprotein complexes. (1979) Journal of Virology. 29(1):232-41.

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Hunter, T., Hutchinson, M.A., Eckhart, W. Translation of polyoma virus T antigens in vitro. (1978) Proceedings of the National Academy of Sciences of the United States of America. 75(12):5917-21.

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Sefton, B.M., Beemon, K., Hunter, T. Comparison of the expression of the src gene of Rous sarcoma virus in vitro and in vivo. (1978) Journal of Virology. 28(3):957-71.

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We have compared the polypeptide products of the src gene of several strains of Rous sarcoma virus produced by in vitro translation of heat-denatured 70S virion RNA in the nuclease-treated reticulocyte lysate with those present in chick cells transformed by these viruses. We have done this by immunoprecipitation, using sera from rabbits injected at birth with Schmidt-Ruppin Rous sarcoma virus. In vitro translation results in the synthesis of at least nine polypeptides which appear to be encoded by the src gene. These range in size from 17,000 to 60,000 daltons. The sera from tumor-bearing rabbits precipitated these polypeptides arising from the in vitro translation of RNA from Schmidt-Ruppin Rous sarcoma virus of both subgroup A and subgroup D and from one stock of Prague Rous sarcoma virus of subgroup C. In each case, all of this family of related polypeptides could be precipitated except the smallest, the 17,000-dalton polypeptide. No precipitation of analogous polypeptides resulting from the translation of RNA from other strains of Rous sarcoma virus was observed. Cells transformed by these three strains of Rous sarcoma virus contain easily detectable amounts of a polypeptide, p60src, essentially identical to the 60,000-dalton in vitro product. With one exception, they do not contain significant amounts of polypeptides analogous to the smaller in vitro products which can be precipitated by these sera. Cells transformed by one stock of Schmidt-Ruppin Rous sarcoma virus of subgroup A did contain a 39,000-dalton polypeptide, which was related, by peptide mapping, to the 60,000-dalton polypeptide and was similar in size to a precipitable in vitro product. The 60,000-dalton polypeptide present in transformed cells appeared to be phosphorylated 10 to 25 min after its synthesis, metabolically very stable, and not derived from a precursor polypeptide. All immunoprecipitates from transformed cells which contained p60src also contained an 80,000-dalton phosphoprotein. This polypeptide is unrelated to p60src, as determined by peptide mapping, and may well be a host cell polypeptide which is specifically associated with p60src.

Beemon, K., Hunter, T. Characterization of Rous sarcoma virus src gene products synthesized in vitro. (1978) Journal of Virology. 28(2):551-66.

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Hunter, T., Gibson, W. Characterization of the mRNA’s for the polyoma virus capsid proteins VP1, VP2, and VP3. (1978) Journal of Virology. 28(1):240-53.

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Hutchinson, M.A., Hunter, T., Eckhart, W. Characterization of T antigens in polyoma-infected and transformed cells. (1978) Cell. 15(1):65-77.

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Elwood, W.J., Beveridge, M.D., Hunter, T.R., Sutherland, R.B., Ryder, T., Woodcock, R.C. The Bolton TV “hospital” series. 1. How did it happen? (1978) Hosp Health Serv Rev. 74(1):7-10.

Hunter, T., Francke, B., Bacheler, L. In vitro polyoma DNA synthesis: asymmetry of short DNA chains. (1977) Cell. 12(4):1021-8.

Hunter, T., Garrels, J.I. Characterization of the mRNAs for alpha-, beta- and gamma-actin. (1977) Cell. 12(3):767-81.

Mann, K., Hunter, T., Walter, G., Linke, H. Evidence for simian virus 40 (SV40) coding of SV40 T-antigen and the SV40-specific proteins in HeLa cells infected with nondefective adenovirus type 2-SV40 hybrid viruses. (1977) Journal of Virology. 24(1):151-69.

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Beemon, K., Hunter, T. In vitro translation yields a possible Rous sarcoma virus src gene product. (1977) Proceedings of the National Academy of Sciences of the United States of America. 74(8):3302-6.

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Gibson, W., Hunter, T., Cogen, B., Eckhart, W. Altered virion proteins of a temperature-sensitive mutant of polyoma virus, ts59. (1977) Virology. 80(1):21-41.

Hunter, A.R., Jackson, R.J., Hunt, T. The role of complexes between the 40-S ribosomal subunit and Met-tRNA-Met-f in the initiation of protein synthesis in the wheat-germ system. (1977) European Journal of Biochemistry. 75(1):159-70. DOI: 10.1111/j.1432-1033.1977.tb11513.x

Hunter, A.R., Farrell, P.J., Jackson, R.J., Hunt, T. The role of polyamines in cell-free protein synthesis in the wheat-germ system. (1977) European Journal of Biochemistry. 75(1):149-57. DOI: 10.1111/j.1432-1033.1977.tb11512.x

Hunter, T.R., Hunt, T., Knowland, J., Zimmern, D. Messenger RNA for the coat protein of tobacco mosaic virus. (1976) Nature. 260(5554):759-64.

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Robbins, J.C., Hunter, T.R., Nicolson, G.L. Ricinus communis toxin-mediated inhibition of protein synthesis in cell-free extracts of a toxin-resistant variant mouse lymphoma cell line. (1976) Journal of Supramolecular Structure. 5(4):515(367)-520(372). DOI: 10.1002/jss.400050408

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Hunter, A.R., Jackson, R.J. Control of haemoglobin synthesis. The effects of iron deprivation, cobalt and temperature on the rate and extent of globin synthesis in reticulocytes. (1975) European Journal of Biochemistry. 58(2):421-30. DOI: 10.1111/j.1432-1033.1975.tb02389.x

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A detailed examination of the kinetics of protein synthesis in rabbit reticulocytes in the presence of the iron chelating agent 2,2′-dipyridyl showed that between 30 degrees C and 42 degrees C there were characteristically two distinct phases of protein synthesis. An initial phase (I), in which no inhibition of protein synthesis was apparent, was followed by a gradual decline in the rate of protein synthesis leading to the second phase (II) in which protein synthesis occurred at a linear but inhibited rate for extended periods. In contrast, below 30 degrees C, incubation in the presence of dipyridyl caused no inhibition of protein synthesis. Between 30 degrees C and 42 degrees C the duration and amount of protein synthesis occurring in phase I before the onset of inhibition were inversely related of the inhibition as was the final rate of incorporation in phase II. During phase II, a partial reversal of the inhibition caused by dipyridyl was obtained by lowering the incubation temperature. This resulted in a burst of protein synthesis at the uninhibited rate until the amount of protein synthesis reached the same level as that in reticulocytes maintained continuously with dipyridyl at the lower incubation temperature. This burst of synthesis was observed in reticulocytes which had been held in phase II for as long as 90 min. It was also possible to reverse the inhibition by addition of haemin to cells in phase II. At any particular incubation temperature, a fixed number of rounds of protein synthesis had to occur before the onset of phase II became apparent. By the use of puromycin we showed that this was not a requirement for the synthesis of globin or of any other protein. We believe that this critical amount of protein synthesis reflects the residual ability of reticulocytes to initiate new protein chains in the absence of concurrent haem synthesis. Reticulocytes preincubated in the presence of cobaltous ions showed almost no inhibition of protein synthesis upon subsequent incubation with dipyridyl. The results are compared to those obtained in reticulocyte lysates and are discussed in terms of current theories to account for control of protein chain initiation by haemin.

Rudland, P.S., Weil, S., Hunter, A.R. Changes in RNA metabolism and accumulation of presumptive messenger RNA during transition from the growing to the quiescent state of cultured mouse fibroblasts. (1975) Journal of Molecular Biology. 96(4):745-66. DOI: 10.1016/0022-2836(75)90150-3

Hunter, T., Francke, B. In vitro polyoma DNA synthesis: inhibition by 1-beta-d-arabinofuranosyl CTP. (1975) Journal of Virology. 15(4):759-75.

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The effects of 1-beta-D-arabinofuranosyl CTP (ara-CTP) on DNA replication were studied in an in vitro system from polyoma-infected BALB/3T3 cells. Ara-CTP concentrations of larger than or equal to 150 muM were found to block in vitro DNA synthesis completely, and concentrations of smaller than or equal to 0.3 muM had no inhibitory effect. Intermediate concentrations resulted in a concentration-dependent reduction of the in vitro synthesis rate. Long-term labeling with [alpha-32-P]ara-CTP demonstrated the incorporation of the analogue into cellular and viral DNA concomitantly with [3-H]TTP. In pulse-labeling experiments, at noninhibitory concentrations of the analogue, ara-CTP was incorporated into short DNA fragments and long growing strands to relatively the same extent as TTP. Partial venom phosphodiesterase digestion liberated the incoporated are-CTP at essentially the same rate as incorporated TTP, excluding a predominantly terminal incorporation, and after total venom phosphodiesterase digestion greater than 80% of the incorporated ara-CTP was recovered as 5′-ara-CMP. Analysis of the long-term in vitro viral DNA product made in the presence of partially inhibiting ara-CTP concentrations demonstrated that none of the steps leading to mature viral DNA were totally inhibited at the ara-CTP concentrations used. Pulse labeling of replicating viral DNA in the presence of ara-CTP revealed two consistent differences in the pattern found in control pulses: (i) predominant labeling of short chains (5S) with reduced amounts of radioactivity in the longer growing viral DNA strands (smaller than or equal to 16S), and (ii) a one-third to one-half reduction in size for short DNA chains labeled in the presence of ara-CTP. Release of the ara-CTP inhibition with excess dCTP resulted in covalent extension of these smaller short chans to approximately the size of regular short chains labeled in the absence of the inhibitor. Isolated short chains synthesized in the presence of ara-CTP exhibited a slightly lower degree of self-complementarity than regular short chains. The predominant labeling of short chains during pulses is, therefore, not a consequence of discontinuous growth on both sides of the replication fork. Similar results were obtained with ara-ATP and N-ethylmaleimide. The experiments indicate that ara-CTP acts primarily on DNA-polymerizing activities, affecting different DNA polymerases to varying degrees. The results are discussed in terms of the possible number and identity of polymerases involved in viral (and cellular) DNA replication.

Robertson, H.D., Hunter, T. Sensitive methods for the detection and characterization of double helical ribonucleic acid. (1975) Journal of Biological Chemistry. 250(2):418-25.

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Hunter, T., Hunt, T., Jackson, R.J., Robertson, H.D. The characteristics of inhibition of protein synthesis by double-stranded ribonucleic acid in reticulocyte lysates. (1975) Journal of Biological Chemistry. 250(2):409-17.

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Francke, B., Hunter, T. In vitro polyoma DNA synthesis: requirement for cytoplasmic factors. (1975) Journal of Virology. 15(1):97-107.

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Nicolson, G.L., Lacorbiere, M., Hunter, T.R. Mechanism of cell entry and toxicity of an affinity- purified lectin from Ricinus communis and its differential effects on normal and virus-transformed fibroblasts. (1975) Cancer Research. 35(1):144-55.

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An affinity-purified plant lectin from Ricinus communis (RCAII) was shown to exhibit differential toxicity toward SV40-transformed 3T3 fibroblasts grown in vitro. When macromolecular synthesis was examined in SV3T3 and 3T3 cells, RCAII suppressed cell protein synthesis in the transformed line at lower concentrations (1/50 to 1/100) compared to the 3T3 line, and these effects were blocked by the RCAII inhibitors D-galactose or lactose. RNA and DNA synthesis and L-leucine transport were relatively unaffected by RCAII concentrations (greater than 1 mug/ml) that completely suppressed protein synthesis in both cell lines. The RCAII-mediated inhibition of cell protein synthesis required incubation times longer than 60 min, but quantitative cell binding studies with 125-I-RCAII indicated that the lectin binds to maximal levels in approximately 5 to 10 min, even at 4 degrees. During 10-min labeling experiments with 125-I-RCAII (1 mug/ml), it was demonstrated that the cell-bound lectin could be almost quantitatively removed from cells up to an additional 15 min after labeling without subsequent inhibition of protein synthesis. However, longer incubation times (greater than 30 min) after RCAII cell labeling and washing resulted in incomplete removal of cell-bound lectin (less than 20 to 30% of cell-bound lectin could be removed after a 60-min incubation). The longer incubation times (greater than 60 min) also resulted in almost complete inhibition of protein synthesis. Ferritin-conjugated RCAII (ferritin-RCAII) was used to follow the fate of the cell-bound lectin. Ferritin-RCAII bound rapidly (less than 10 min) to SV3T3 cell surfaces and could be blocked from labeling with lactose. After a 10-min incubation at 4 degrees in ferritin-RCAII solutions, the ferritin label was exclusively located at the extracellular surface in a random distribution. After washing and incubation at 37 degrees, the ferritin-RCAII induced clustering of its receptors (15 to 30 min) and eventually induced endocytosis (30 to 60 min). Further incubation (greater than 60 min) resulted in a predominantly intracellular localization of ferritin-RCAII inside endocytotic vesicles and free in the cell cytoplasm. That RCAII acts directly on protein synthesis after cell entry was confirmed with rabbit reticulocyte and mouse Krebs II ascites S30 cell-free protein synthesis system in diameter wit

Francke, B., Hunter, T. In vitro polyoma DNA synthesis: discontinuous chain growth. (1974) Journal of Molecular Biology. 83(1):99-121.

Hunter, T., Francke, B. Letter: In vitro polyoma DNA synthesis: involvement of RNA in discontinuous chain growth. (1974) Journal of Molecular Biology. 83(1):123-30.

Francke, B., Hunter, T. In vitro polyoma DNA synthesis: studies on an early temperature-sensitive mutant. (1974) Journal of Virology. 13(1):241-3.

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Hunter, T., Francke, B. In vitro polyoma DNA synthesis: characterization of a system from infected 3T3 cells. (1974) Journal of Virology. 13(1):125-39.

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A lysate from hypotonically swollen polyoma-infected BALB/3T3 cells incorporated labeled deoxynucleotide triphosphates into both viral and cellular DNAs. The incorporation was stimulated by the presence of ATP, deoxynucleotide triphosphates, thiols, and magnesium ions. Strong inhibition of incorporation was observed with thiol reagents and arabinosyl nucleotide triphosphates. The rate of in vitro synthesis increased with the temperature of incubation as expected. Incorporation into cellular DNA for up to 2 h was observed in lysates from virus-infected and serum-stimulated cells but not from resting cells. Synthesis in the system, therefore, appeared to reflect the physiological state of the cells before preparation of the lysate. Incorporation into viral DNA stopped far sooner than that into cellular DNA. During the initial phase of the in vitro incubation, incorporation occurred into viral replicative intermediates (RI). These RIs had identical properties to those isolated after in vivo pulse labeling and a substantial proportion of them was matured to form I DNA at later times in the incubation through all the stages known to occur in vivo. Density labeling of the in vitro product showed that practically all of the RIs pre-existing in the infected cell took part in the in vitro reaction. Analysis of DNA labeled in vitro in the presence of 5-bromodeoxyuridine triphosphate showed that synthesis occurred on RIs at all stages of replication and that the progeny strands were elongated by up to 80% of unit viral DNA length. Pre-existing RIs, pulse labeled in vivo, showed evidence of a pool at a late stage of replication which required elongation of their progeny strands by approximately 25% during conversion to form I molecules. From density-labeling experiments, we were also able to show that viral DNA synthesis in vitro was semiconservative. The major reason for cessation of viral DNA synthesis in vitro was the very limited ability of the lysate to initiate new rounds of viral DNA synthesis.

Hunter, A.R., Jackson, R.J. Control of haemoglobin synthesis: coordination of alpha and beta chain synthesis. (1972) Hamatol. Bluttransfus. 10:95-108.

Hunter, A.R., Hunt, R.T., Jackson, R.J., Robertson, H.D. Initiation of globin synthesis in rabbit reticulocyte cell-free systems: inhibition by double-stranded RNA. (1972) Hamatol. Bluttransfus. 10:133-45.

Hunter, A.R., Jackson, R.J. The origin and nature of the methionine residue initiating the synthesis of haemoglobin in vivo and in vitro. (1971) European Journal of Biochemistry. 19(3):316-22. DOI: 10.1111/j.1432-1033.1971.tb01321.x

Jackson, R., Hunter, T. Role of methionine in the initiation of haemoglobin synthesis. (1970) Nature. 227(5259):672-6.

Hunter, A.R., Jackson, R.J. Miscoding by Escherichia coli tRNAs for methionine, cysteine and valine in the synthesis of rabbit globin. (1970) European Journal of Biochemistry. 15(2):381-90. DOI: 10.1111/j.1432-1033.1970.tb01019.x

Jackson, R., Hunter, T. The effect of cobalt on the synthesis of globin and haem in reticulocytes. (1970) FEBS Lett. 9(2):61-63.

Hunter, T., Munro, A. Allelic variants in the amino-acid sequence of the alpha chain of rabbit haemoglobin. (1969) Nature. 223(5212):1270-2.

Hunt, R.T., Hunter, A.R., Munro, A.J. The control of haemoglobin synthesis: factors controlling the output of alpha and beta chains. (1969) Proc Nutr Soc. 28(2):248-54. DOI: 10.1079/pns19690046

Hunt, T., Hunter, T., Munro, A. Control of haemoglobin synthesis: rate of translation of the messenger RNA for the alpha and beta chains. (1969) Journal of Molecular Biology. 43(1):123-33.

Hunt, T., Hunter, A., Munro, A.J. Factors affecting haemoglobin biosynthesis. (1969) Biochemical Journal. 113(2):5P. DOI: 10.1042/bj1130005pa

Hunter, A.R., Korner, A. The response of rat liver polysomes to added homopolynucleotides: the removal of inactive ribosomes. (1969) Biochimica et Biophysica Acta. 179(1):115-28. DOI: 10.1016/0005-2787(69)90127-0

Hunter, A.R., Korner, A. Exonuclease activity in rat liver cell sap. (1968) Biochimica et Biophysica Acta. 169(2):488-93. DOI: 10.1016/0005-2787(68)90057-9

Hunt, R.T., Hunter, A.R., Munro, A.J. Control of haemoglobin synthesis: a difference in the size of the polysomes making alpha and beta chains. (1968) Nature. 220(5166):481-3. DOI: 10.1038/220481a0

Hunt, T., Hunter, T., Munro, A. Control of haemoglobin synthesis: distribution of ribosomes on the messenger RNA for alpha and beta chains. (1968) Journal of Molecular Biology. 36(1):31-45.

Hunter, A.R., Jefferson, L.S. Perfusion of rat liver with adenosine monophosphate. (1967) Biochemical Journal. 104(3):60P-61P.