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Gene Expression

pp60c-src Variants Containing Lesions That Affect Phosphorylation at Tyrosines 416 and 527

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Pages 3647-3656 | Received 22 Mar 1989, Accepted 01 Jun 1989, Published online: 31 Mar 2023

LITERATURE CITED

  • Bolen, J. B., C. J. Thiele, M. Israel, W. Yonemoto, L. A. Lipsich, and J. S. Brugge. 1984. Enhancement of cellular src gene product associated tyrosyl kinase activity following polyoma virus infection and transformation. Cell 38:767–777.
  • Buss, J. E., and B. M. Sefton. 1985. Myristic acid, a rare fatty acid, is the lipid attached to the transforming protein of Rous sarcoma virus and its cellular homolog. J. Virol. 53:7–12.
  • Cartwright, C. A., W. Eckhart, S. Simon, and P. L. Kaplan. 1987. Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain. Cell 49:83–91.
  • Cartwright, C. A., P. L. Kaplan, J. A. Cooper, T. Hunter, and W. Eckhart. 1986. Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen. Mol. Cell. Biol. 6:1562–1570.
  • Chakalaparampil, I., and D. Shalloway. 1988. Altered phosphorylation and activation of pp60c-src during fibroblast mitosis. Cell 52:801–810.
  • Cheng, S. H., R. Harvey, P. C. Espino, K. Semba, T. Yamamoto, K. Toyoshima, and A. E. Smith. 1988. Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus. EMBO J. 7:3845–3855.
  • Cheng, S. H., W. Markland, A. F. Markham, and A. E. Smith. 1986. Mutations around the NG59 lesion indicate an active association of polyoma virus middle-T antigen with pp60c-src is required for cell transformation. EMBO J. 5:325–334.
  • Cheng, S. H., H. Piwnica-Worms, R. W. Harvey, T. M. Roberts, and A. E. Smith. 1988. The carboxy terminus of pp60c-src is a regulatory domain and is involved in complex formation with the middle-T antigen of polyomavirus. Mol. Cell. Biol. 8:1736–1747.
  • Cleveland, D. W., S. G. Fischer, M. W. Kirschner, and U. K. Laemmli. 1977. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252:1102–1106.
  • Colledge, W. H., W. D. Richardson, M. D. Edge, and A. E. Smith. 1986. Extensive mutagenesis of the nuclear location signal of simian virus 40 large-T antigen. Mol. Cell. Biol. 6:4136–4139.
  • Collett, M. S., A. F. Purchio, and R. L. Erikson. 1980. Avian sarcoma virus transforming protein p60src shows protein kinase activity specific for tyrosine. Nature (London) 285:167–169.
  • Cooper, J. A., K. L. Gould, C. A. Cartwright, and T. Hunter. 1986. Tyr527 is phosphorylated in pp60c-src: implications for regulation. Science 231:1431–1434.
  • Cooper, J. A., and C. S. King. 1986. Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src. Mol. Cell. Biol. 6:4467–4477.
  • Cooper, J. A., and A. MacAuley. 1988. Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation. Proc. Natl. Acad. Sci. USA 85:4232–4236.
  • Courtneidge, S. A.. 1985. Activation of the pp60c-src kinase by middle-T binding or by dephosphorylation. EMBO J. 4:1471–1477.
  • Courtneidge, S. A., and A. E. Smith. 1983. Polyoma virus transforming protein associates with the product of the cellular src gene. Nature (London) 303:435–439.
  • Courtneidge, S. A., and A. E. Smith. 1984. The complex of polyoma virus middle-T antigen and pp60c-src. EMBO J. 3:585–591.
  • Coussens, P. M., J. A. Cooper, T. Hunter, and D. Shalloway. 1985. Restriction of the in vitro and in vivo tyrosine kinase activities of pp60c-src relative to pp60v-src. Mol. Cell. Biol. 5:2753–2763.
  • Gould, K. L., J. R. Woodgett, J. A. Cooper, J. E. Buss, D. Shalloway, and T. Hunter. 1985. Protein kinase C phosphorylates pp60c-src at a novel site. Cell 42:849–857.
  • Graham, F. L., and A. J. van der Eb. 1979. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52:456–467.
  • Hunter, T., and B. M. Sefton. 1980. Transforming gene product of Rous sarcoma virus phosphorylates tyrosines. Proc. Natl. Acad. Sci. USA 77:1311–1315.
  • Iba, H., F. R. Cross, E. A. Garber, and H. Hanafusa. 1985. Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src. Mol. Cell. Biol. 5:1058–1066.
  • Iba, H., T. Takeya, F. R. Cross, T. Hanafusa, and H. Hanafusa. 1984. Rous sarcoma virus variants that carry the cellular src gene instead of the viral src gene cannot transform chicken embryo fibroblasts. Proc. Natl. Acad. Sci. USA 81:4424–4428.
  • Johnson, P. J., P. M. Coussens, A. V. Danko, and D. Shalloway. 1985. Overexpressed pp60c-src can induce focus formation without complete transformation of NIH 3T3 cells. Mol. Cell. Biol. 5:1073–1083.
  • Kmiecik, T. E., P. J. Johnson, and D. Shalloway. 1988. Regulation by the autophosphorylation site in overexpressed pp60c-src. Mol. Cell. Biol. 8:4541–4546.
  • Kmiecik, T. E., and D. Shalloway. 1987. Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49:65–73.
  • Kornbluth, S., M. Sudol, and H. Hanafusa. 1987. Association of polyomavirus middle-T antigen with c-yes protein. Nature (London) 325:171–173.
  • Kypta, R. M., A. Hemming, and S. A. Courtneidge. 1988. Identification and characterization of p59fyn (a src-like protein tyrosine kinase) in normal and polyoma virus transformed cells. EMBO J. 7:3837–3844.
  • Levinson, A. D., H. Opperman, H. E. Varmus, and J. M. Bishop. 1980. The purified product of the transforming gene of avian sarcoma virus phosphorylates tyrosine. J. Biol. Chem. 255:11973–11980.
  • Levy, J. B., H. Iba, and H. Hanafusa. 1986. Activation of the transforming potential of pp60c-src by a single amino acid change. Proc. Natl. Acad. Sci. USA 83:4228–4232.
  • Louie, R. R., C. S. King, A. MacAuley, J. D. Marth, R. M. Perlmutter, W. Eckhart, and J. A. Cooper. 1988. p56lck protein-tyrosine kinase is cytoskeletal and does not bind to polyomavirus middle-T antigen. J. Virol. 62:4673–4679.
  • MacPherson, I., and L. Montagnier. 1964. Agar suspension culture for the selective assay of cells transformed by polyoma virus. Virology 23:291–294.
  • Mann, R., R. C. Mulligan, and D. Baltimore. 1983. Construction of a retrovirus packaging mutant and its use to produce helper-free defective retrovirus. Cell 33:153–159.
  • Parker, R. C., H. E. Varmus, and J. M. Bishop. 1984. Expression of v-src and chicken c-src in rat cells demonstrates qualitative differences between pp60v-src and pp60c-src. Cell 37:131–139.
  • Parsons, S. J., D. J. McCarley, C. M. Ely, D. C. Benjamin, and J. T. Parsons. 1984. Monoclonal antibodies to Rous sarcoma virus pp60src react with enzymatically active cellular pp60src of avian and mammalian origin. J. Virol. 51:272–282.
  • Patchinsky, T., T. Hunter, and B. M. Sefton. 1986. 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 of Prague sarcoma virus. J. Virol. 59:73–81.
  • Piwnica-Worms, H., D. R. Kaplan, M. Whitman, and T. M. Roberts. 1986. Retrovirus shuttle vector for study of kinase activities of pp60c-src synthesized in vitro and overproduced in vivo. Mol. Cell. Biol. 6:2033–2040.
  • Piwnica-Worms, H., K. B. Saunders, T. M. Roberts, A. E. Smith, and S. H. Cheng. 1987. Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src. Cell 49:75–82.
  • Ralston, R., and J. M. Bishop. 1985. The product of the protooncogene c-src is modified during the cellular response to platelet-derived growth factor. Proc. Natl. Acad. Sci. USA 82:7845–7849.
  • Reynolds, A. B., J. Vila, T. J. Lansing, W. M. Potts, M. J. Weber, and J. T. Parsons. 1987. Activation of the oncogenic potential of the avian cellular src protein by specific structural alteration of the carboxyl terminus. EMBO J. 6:2359–2364.
  • Schuh, S. M., and J. S. Brugge. 1988. Investigation of factors that influence phosphorylation of pp60c-src on tyrosine 527. Mol. Cell. Biol. 8:2465–2471.
  • Shalloway, D., P. M. Coussens, and P. Yacuik. 1984. Overex pression of the c-src protein does not induce transformation of NIH 3T3 cells. Proc. Natl. Acad. Sci. USA 81:7071–7075.
  • Yacuik, P., M. T. Cannella, and D. Shalloway. 1988. Comparison of the effects of carboxyl terminal truncation and point mutations on pp60c-src activities. Oncogene Res. 3:207–212.
  • Yacuik, P., and D. Shalloway. 1986. Features of the pp60v-src carboxyl terminus that are required for transformation. Mol. Cell. Biol. 6:2807–2819.
  • Yarden, Y., and A. Ullrich. 1988. Growth factor receptor tyrosine kinases. Annu. Rev. Biochem. 57:443–478.
  • Yonemoto, W., M. Jarvis-Morar, J. S. Brugge, J. B. Bolen, and M. A. Israel. 1985. Tyrosine phosphorylation within the amino-terminal domain of pp60c-src molecules associated with polyoma virus middle sized tumor antigen. Proc. Natl. Acad. Sci. USA 82:4568–4572.

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