Activation of the Proto-Oncogene p60^c-src by Point Mutations in the SH2 Domain

Literature Cited

• Brugge, J. S., and D. Darrow. 1984. Analysis of the catalytic domain of phosphotransferase activity of two avian sarcoma virus-transforming proteins. J. Biol. Chem. 259:4550–4557.
   PubMedGoogle Scholar
• Bryant, D., and J. T. Parsons. 1982. Site-directed mutagenesis of the src gene of Rous sarcoma virus: construction and characterization of a deletion mutant temperature sensitive for transformation. J. Virol. 44:683–691.
   PubMedGoogle Scholar
• Chackalaparampil, I., and D. Shalloway. 1988. Altered phosphorylation and activation of pp60c-src during fibroblast mitosis. Cell 52:801–810.
   PubMed Web of Science ®Google Scholar
• Courtneidge, S. A., and A. Heber. 1987. An 81 kd protein complexed with middle T antigen and pp60c-src: a possible phosphatidylinositol kinase. Cell 50:1031–1037.
   PubMed Web of Science ®Google Scholar
• Crawford, J. L., W. N. Lipscomb, and C. G. Schellman. 1973. The reverse turn as a polypeptide conformation in globular proteins. Proc. Natl. Acad. Sci. USA 70:538–542.
   PubMed Web of Science ®Google Scholar
• Cross, F. R., E. A. Garber, and H. Hanafusa. 1985. N-terminal deletions in Rous sarcoma virus p60src: effects on tyrosine kinase and biological activities and on recombination in tissue culture with the cellular src gene. Mol. Cell. Biol. 5:2789–2795.
   PubMedGoogle Scholar
• Cross, F. R., and H. Hanafusa. 1983. Local mutagenesis of Rous sarcoma virus: the major sites of tyrosine and serine phosphorylation of p60src are dispensable for transformation. Cell 34:597–607.
   PubMed Web of Science ®Google Scholar
• DeClue, J. E., and G. S. Martin. 1989. Linker insertion-deletion mutagenesis of the v-src gene: isolation of host- and temperature-dependent mutants. J. Virol. 63:542–554.
   PubMed Web of Science ®Google Scholar
• DeClue, J. E., I. Sadowski, G. S. Martin, and T. Pawson. 1987. A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell. Proc. Natl. Acad. Sci. USA 84:9064–9068.
   PubMedGoogle Scholar
• DeLorbe, W. J., P. A. Luciw, H. M. Goodman, H. E. Varmus, and J. M. Bishop. 1980. Molecular cloning and characterization of avian sarcoma virus circular DNA molecules. J. Virol. 36:50–61.
   PubMedGoogle Scholar
• Ellis, C., M. Moran, F. McCormick, and T. Pawson. 1990. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature (London) 343:377–381.
   PubMed Web of Science ®Google Scholar
• Fukui, Y., and H. Hanafusa. 1989. Phosphatidylinositol kinase activity associates with viral p60src protein. Mol. Cell. Biol. 9:1651–1658.
   PubMedGoogle Scholar
• Fukui, Y., S. Kornbluth, S.-M. Jong, L.-H. Wang, and H. Hanafusa. 1989. Phosphatidylinositol kinase type I activity associates with various oncogene products. Oncogene Res. 4:283–292.
   PubMedGoogle Scholar
• Gould, K. L., and T. Hunter. 1988. Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity. Mol. Cell. Biol. 8:3345–3356.
   PubMed Web of Science ®Google Scholar
• Hanafusa, H. 1969. Rapid transformation of cells by Rous sarcoma virus. Proc. Natl. Acad. Sci. USA 63:318–325.
   PubMedGoogle Scholar
• Hanafusa, H. 1986. Activation of the c-src gene, p. 100–105. In P. Kahn and T. Graf (ed.), Oncogenes and growth control. Springer-Verlag KG, Berlin.
   Google Scholar
• Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Hunter, T. 1987. A tail of two src's: mutatis mutandis. Cell 49:1–4.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Jove, R., and H. Hanafusa. 1987. Cell transformation by the viral src oncogene. Annu. Rev. Cell Biol. 3:31–56.
   PubMedGoogle Scholar
• Jove, R., T. Hanafusa, M. Hamaguchi, and H. Hanafusa. 1989. In vivo phosphorylation states and kinase activities of transforming p60c-src mutants. Oncogene Res. 5:49–60.
   PubMedGoogle Scholar
• Jove, R., S. Kornbluth, and H. Hanafusa. 1987. Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxyl-terminal regulatory region. Cell 50:937–943.
   PubMedGoogle Scholar
• Jove, R., B. J. Mayer, H. Iba, D. Laugier, F. Poirer, G. Calothy, T. Hanafusa, and H. Hanafusa. 1986. Genetic analysis of p60v-src domains involved in the induction of different cell transformation parameters. J. Virol. 60:840–848.
   PubMedGoogle Scholar
• Kamps, M. P., and B. M. Sefton. 1988. Identification of multiple novel polypeptide substrates of the v-src, v-yes, v-fps, v-ros, and v-erb-B oncogenic tyrosine protein kinases utilizing antisera against phosphotyrosine. Oncogene 2:305–315.
   PubMedGoogle Scholar
• Kaplan, D. R., M. Whitman, B. Schaffhausen, D. C. Pallas, M. White, L. Cantley, and T. M. Roberts. 1987. Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity. Cell 50:1021–1029.
   PubMed Web of Science ®Google Scholar
• Kaplan, J. M., G. Mardon, J. M. Bishop, and H. E. Varmus. 1988. The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: lysine 7 is a critical determinant. Mol. Cell. Biol. 8:2435–2441.
   PubMed Web of Science ®Google Scholar
• Kato, J.-Y., T. Takeya, C. Grandori, H. Iba, J. B. Levy, and H. Hanafusa. 1986. Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein. Mol. Cell. Biol. 6:4155–4160.
   PubMed Web of Science ®Google Scholar
• Kitamura, N., and M. Yoshida. 1983. Small deletion in src of Rous sarcoma virus modifying transformation phenotypes: identification of 207-nucleotide deletion and its smaller product with protein kinase activity. J. Virol. 46:985–992.
   PubMedGoogle Scholar
• Koch, C. A., M. Moran, I. Sadowski, and T. Pawson. 1989. The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function. Mol. Cell. Biol. 9:4131–4140.
   PubMedGoogle Scholar
• Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367–382.
   PubMed Web of Science ®Google Scholar
• Levinson, A. D., S. A. Courtneidge, and J. M. Bishop. 1981. Structural and functional domains of the Rous sarcoma virus transforming protein (pp60src). Proc. Natl. Acad. Sci. USA 78:1624–1628.
   PubMed Web of Science ®Google Scholar
• Levy, J. B., and J. S. Brugge. 1989. Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts. Mol. Cell. Biol. 9:3332–3341.
   PubMedGoogle Scholar
• Levy, J. B., T. Dorai, L.-H. Wang, and J. S. Brugge. 1987. The structurally distinct form of pp60c-src detected in neuronal cells is encoded by a unique c-src mRNA. Mol. Cell. Biol. 7:4142–4145.
   PubMedGoogle Scholar
• Levy, J. B., H. Iba, and H. Hanafusa. 1986. Activation of the transforming potential of p60c-src by a single amino acid change. Proc. Natl. Acad. Sci. USA 83:4228–4232.
   PubMed Web of Science ®Google Scholar
• Linder, M. E., and J. G. Burr. 1988. Immunological characterization of proteins detected by phosphotyrosine antibodies in cells transformed by Rous sarcoma virus. J. Virol. 62:2665–2673.
   PubMedGoogle Scholar
• Lipsich, L. A., A. J. Lewis, and J. S. Brugge. 1983. Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J. Virol. 48:352–360.
   PubMedGoogle Scholar
• Martinez, R., B. Mathey-Prevot, A. Bernards, and D. Baltimore. 1987. Neuronal pp60c-src contains a six-amino acid insertion relative to its non-neuronal counterpart. Science 237:411–415.
   PubMedGoogle Scholar
• Mayer, B. J., M. Hamaguchi, and H. Hanafusa. 1988. A novel viral oncogene with structural similarity to phospholipase C. Nature (London) 332:272–275.
   PubMed Web of Science ®Google Scholar
• Morgan, D. O., J. M. Kaplan, J. M. Bishop, and H. E. Varmus. 1989. Mitosis-specific phosphorylation of p60c-src by p34cdc2- associated protein kinase. Cell 57:775–786.
   PubMed Web of Science ®Google Scholar
• Nemeth, S. P., L. G. Fox, M. DeMarco, and J. S. Brugge. 1989. Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein. Mol. Cell. Biol. 9:1109–1119.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Pawson, T. 1988. Non-catalytic domains of cytoplasmic protein-tyrosine kinases: regulatory elements in signal transduction. Oncogene 3:491–495.
   PubMed Web of Science ®Google Scholar
• Potts, W. M., A. B. Reynolds, T. J. Lansing, and J. T. Parsons. 1988. Activation of pp60c-src transforming potential by mutations altering the structure of an amino terminal domain containing residues 90-95. Oncogene Res. 3:343–355.
   PubMedGoogle Scholar
• Raymond, V. W., and J. T. Parsons. 1987. Identification of an amino terminal domain required for the transforming activity of the Rous sarcoma virus src protein. Virology 160:400–410.
   PubMedGoogle Scholar
• Reddy, E. P., M. J. Smith, and A. Srinivasan. 1983. Nucleotide sequence of Abelson murine leukemia virus genome: structural similarity of its transforming gene product to other onc products with tyrosine-specific kinase activity. Proc. Natl. Acad. Sci. USA 80:3623–3627.
   PubMed Web of Science ®Google Scholar
• Reynolds, A. B., S. B. Kanner, H.-C. R. Wang, and J. T. Parsons. 1989. Stable association of activated pp60src with two tyrosine-phosphorylated cellular proteins. Mol. Cell. Biol. 9:3951–3958.
   PubMed Web of Science ®Google Scholar
• Reynolds, A. B., D. J. Roesel, S. B. Kanner, and J. T. Parsons. 1989. Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene. Mol. Cell. Biol. 9:629–638.
   PubMed Web of Science ®Google Scholar
• Rhee, S. G., P.-G. Suh, S.-H. Ryu, and S. Y. Lee. 1989. Studies of inositol phospholipid-specific phospholipase C. Science 244:546–550.
   PubMed Web of Science ®Google Scholar
• Sadowski, I., J. C. Stone, and T. Pawson. 1986. A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus p130gag-fps. Mol. Cell. Biol. 6:4396–4408.
   PubMed Web of Science ®Google Scholar
• Sato, M., J.-Y. Kato, and T. Takeya. 1989. Characterization of partially activated p60c-src in chicken embryo fibroblasts. J. Virol. 63:683–688.
   PubMedGoogle Scholar
• Shalloway, D., P. M. Coussens, and P. Yaciuk. 1984. Overexpression of the c-src protein does not induce transformation of NIH 3T3 cells. Proc. Natl. Acad. Sci. USA 81:7071–7075.
   PubMedGoogle Scholar
• Shenoy, S., J.-K. Choi, S. Bagrodia, T. D. Copeland, J. L. Mailer, and D. Shalloway. 1989. Purified muturation promoting factor phosphorylates pp60c-src at the sites phosphorylated during fibroblast mitosis. Cell 57:763–774.
   PubMedGoogle Scholar
• Shibuya, M., and H. Hanafusa. 1982. Nucleotide sequence of Fujinami sarcoma virus: evolutionary relationship of its transforming gene with transforming genes of other sarcoma viruses. Cell 30:787–795.
   PubMed Web of Science ®Google Scholar
• Stahl, M. L., C. R. Ferenz, K. L. Kelleher, R. W. Kriz, and J. L. Knopf. 1988. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature (London) 332:269–272.
   PubMed Web of Science ®Google Scholar
• Takeya, T., and H. Hanafusa. 1983. Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus. Cell 32:881–890.
   PubMed Web of Science ®Google Scholar
• Verderame, M. F., J. M. Kaplan, and H. E. Varmus. 1989. A mutation in v-src that removes a single conserved residue in the SH-2 domain of pp60v-src restricts transformation in a host-dependent manner. J. Virol. 63:338–348.
   PubMedGoogle Scholar
• Vogel, U. S., R. A. F. Dixon, M. D. Schaber, R. E. Diehl, M. S. Marshall, E. M. Scolnick, I. S. Sigal, and J. B. Gibbs. 1988. Cloning of bovine GAP and its interaction with oncogenic ras p21. Nature (London) 335:90–93.
   PubMed Web of Science ®Google Scholar
• Wang, H.-C. R., and J. T. Parsons. 1989. Deletions and insertions within an amino-terminal domain of pp60v-src inactivate transformation and modulate membrane stability. J. Virol. 63:291–302.
   PubMedGoogle Scholar
• Wang, J. Y. J. 1985. Isolation of antibodies for phosphotyrosine by immunization with a v-abl oncogene-encoded protein. Mol. Cell. Biol. 5:3640–3643.
   PubMedGoogle Scholar
• Wendler, P. A., and F. Boschelli. 1989. Src homology 2 domain deletion mutants of p60v-src do not phosphorylate cellular proteins of 120-150 kDa. Oncogene 4:231–236.
   PubMedGoogle Scholar
• Whitman, M., C. P. Downes, M. Keeler, T. Keller, and L. Cantley. 1988. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature (London) 332:644–646.
   PubMed Web of Science ®Google Scholar