Point Mutations in the abl SH2 Domain Coordinately Impair Phosphotyrosine Binding In Vitro and Transforming Activity In Vivo

REFERENCES

• Anderson, D., C. A. Koch, L. Grey, C. Ellis, M. F. Moran, and T. Pawson. 1990. Binding of SH2 domains of phospholipase Cγ1, GAP, and src to activated growth factor receptors. Science 250:979–982.
   PubMed Web of Science ®Google Scholar
• Birge, R. B., J. E. Fajardo, B. J. Mayer, and H. Hanafusa. Submitted for publication.
   Google 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
• Calnan, B. J., B. Tidor, S. Biancalana, D. Hudson, and A. D. Frankel. 1991. Arginine-mediated RNA recognition: the arginine fork. Science 252:1167–1171.
   PubMed Web of Science ®Google Scholar
• Cantley, L. C., K. R. Auger, C. Carpenter, B. Duckworth, A. Graziani, R. Kapeller, and S. Soltoff. 1991. Oncogenes and signal transduction. Cell 64:281–302.
   PubMed Web of Science ®Google Scholar
• Cross, F. R., E. A. Garber, D. Pellman, and H. Hanafusa. 1984. A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol. Cell. Biol. 4:1834–1842.
   PubMed Web of Science ®Google 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 proteintyrosine kinase with the host cell. Proc. Natl. Acad. Sci. USA 84:9064–9068.
   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
• Field, J., J.-I. Nikiwa, D. Broek, B. MacDonald, L. Rodgers, I. A. Wilson, R. A. Lerner, and M. Wigler. 1988. Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method. Mol. Cell. Biol. 8:2159–2165.
   PubMed Web of Science ®Google Scholar
• Fukui, Y., and H. Hanafusa. 1991. Requirement of phosphati- dylinositol-3 kinase modification for its association with p60src. Mol. Cell. Biol. 11:1972–1979.
   PubMedGoogle Scholar
• Fukui, Y., M. C. O'Brien, and H. Hanafusa. 1991. Deletions in the SH2 domain of p60v-src prevent association with the detergent-insoluble cellular matrix. Mol. Cell. Biol. 11:1207–1213.
   PubMedGoogle Scholar
• Glenney, J. R., and L. Zokas. 1989. Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton. J. Cell Biol. 108:2401–2408.
   PubMed Web of Science ®Google Scholar
• Glenney, J. R., L. Zokas, and M. P. Kamps. 1988. Monoclonal antibodies to phosphotyrosine. J. Immunol. Methods 109:277–285.
   PubMed Web of Science ®Google Scholar
• Goldschmidt-Clermont, P. J., J. W. Kim, L. M. Machesky, S. G. Rhee, and T. D. Pollard. 1991. Regulation of phospholipase C-γ1 by profilin and tyrosine phosphorylation. Science 251:1231–1233.
   PubMed Web of Science ®Google Scholar
• Hanks, S. K., A. M. Quinn, and T. Hunter. 1988. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241:42–52.
   PubMed Web of Science ®Google Scholar
• Hirai, H., and H. E. Varmus. 1990. Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src. Mol. Cell. Biol. 10:1307–1318.
   PubMed Web of Science ®Google Scholar
• Hirai, H., and H. E. Varmus. 1990. Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells. Proc. Natl. Acad. Sci. USA 87:8592–8596.
   PubMedGoogle Scholar
• Hirai, H., and H. E. Varmus. 1990. SH2 mutants of c-src that are host-dependent for transformation are trans-dominant inhibitors of mouse cell transformation by activated c-src. Genes Dev. 4:2342–2352.
   PubMedGoogle Scholar
• Jackson, P. Unpublished data.
   Google Scholar
• Jackson, P., and D. Baltimore. 1989. N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl. EMBO J. 8:449–456.
   PubMed Web of Science ®Google Scholar
• Jackson, P., M. Paskind, and D. Baltimore. Unpublished data.
   Google Scholar
• Jackson, P., R. A. Van Etten, G. Q. Daley, and D. Baltimore. Submitted for publication.
   Google Scholar
• Johnson, K. A., and J. C. Stone. 1990. Delineation of functional determinants in the transforming protein of Fujinami sarcoma virus. J. Virol. 643:3337–3349.
   Google Scholar
• Kamps, M. P., J. E. Buss, and B. M. Sefton. 1985. Mutation of NH2-terminal glycine of p60src prevents both myristylation and morphological transformation. Proc. Natl. Acad. Sci. USA 82:4625–4628.
   PubMed Web of Science ®Google Scholar
• Kim, H. K., J. W. Kim, A. Zilberstein, B. Margolis, J. G. Kim, J. Schlessinger, and S. G. Rhee. 1991. PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254. Cell 65:435–441.
   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
• 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.
   PubMed Web of Science ®Google Scholar
• Koch, C. A., D. Anderson, M. F. Moran, C. Ellis, and T. Pawson. 1991. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252:668–674.
   PubMed Web of Science ®Google Scholar
• Koch, C. A., M. F. 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
• Konopka, J. B., R. L. Davis, S. M. Watanabe, A. S. Ponticelli, L. Schiff-Maker, N. Rosenberg, and O. N. Witte. 1984. Only site-directed antibodies reactive with the highly conserved src- homologous region of the v-abl protein neutralize kinase activity. J. Virol. 51:223–232.
   PubMedGoogle Scholar
• Margolis, B., N. Li, A. Koch, M. Mohammadi, D. R. Hurwitz, A. Zilberstein, A. Ullrich, T. Pawson, and J. Schlessinger. 1990. The tyrosine-phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-7. EMBO J. 9:4375–4380.
   PubMedGoogle Scholar
• Matsuda, M., B. J. Mayer, Y. Fukui, and H. Hanafusa. 1990. Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science 248:1537–1539.
   PubMedGoogle Scholar
• Matsuda, M., B. J. Mayer, and H. Hanafusa. 1991. Identification of domains of the v-crk oncogene product sufficient for association with phosphotvrosine-containing proteins. Mol. Cell. Biol. 11:1607–1613.
   PubMedGoogle Scholar
• Mayer, B. J., M. Hamaguchi, and H. Hanafusa. 1988. Characterization of p47gag-crk, a novel oncogene product with sequence similarity to a putative modulatory domain of protein-tyrosine kinases and phospholipase C. Cold Spring Harbor Symp. Quant. Biol. 53:907–914.
   PubMedGoogle Scholar
• Mayer, B. J., and H. Hanafusa. 1990. Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activity. Proc. Natl. Acad. Sci. USA 87:2638–2642.
   PubMed Web of Science ®Google Scholar
• Mayer, B. J., and H. Hanafusa. 1990. Mutagenic analysis of the v-crk oncogene: requirement for SH2 and SH3 domains and correlation between increased cellular phosphotyrosine and transformation. J. Virol. 64:3581–3589.
   PubMedGoogle Scholar
• Mayer, B. J., and P. K. Jackson. Unpublished data.
   Google Scholar
• Mayer, B. J., P. K. Jackson, and D. Baltimore. 1991. The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity. Proc. Natl. Acad. Sci. USA 88:627–631.
   PubMedGoogle Scholar
• Moran, M. F., C. A. Koch, D. Anderson, C. Ellis, L. England, G. S. Martin, and T. Pawson. 1990. Src homology region 2 domains direct protein-protein interactions in signal transduction. Proc. Natl. Acad. Sci. USA 87:8622–8626.
   PubMed Web of Science ®Google Scholar
• Moran, M. F., P. Polakis, F. McCormick, T. Pawson, and C. Ellis. 1991. Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating protein. Mol. Cell. Biol. 11:1804–1812.
   PubMed Web of Science ®Google Scholar
• Nishibe, S., M. I. Wahl, S. M. T. Hernandez-Sotomayor, N. K. Tonks, S. G. Rhee, and G. Carpenter. 1990. Increase in the catalytic activity of phospholipase C-γ1 by tyrosine phosphorylation. Science 250:1253–1256.
   PubMed Web of Science ®Google Scholar
• O'Brien, M. C., Y. Fukui, and H. Hanafusa. 1990. Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain. Mol. Cell. Biol. 10:2855–2862.
   PubMedGoogle Scholar
• Parsons, J. T., D. Bryant, V. Wilkerson, G. Gilmartin, and S. J. Parsons. 1984. Site-directed mutagenesis of Rous sarcoma virus pp60src: identification of functional domains required for transformation, p. 37–42. In G. F. Vande Woude, A. J. Levine, W. C. Topp, and J. D. Watson (ed.), Cancer cells 2. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Pawson, T. 1988. Non-catalytic domains of cytoplasmic proteintyrosine kinases: regulatory elements in signal transduction. Oncogene 3:491–495.
   PubMed Web of Science ®Google Scholar
• Pendergast, A. M., A. J. Muller, M. H. Havlik, Y. Maru, and O. N. Witte. 1991. BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner. Cell 66:161–171.
   PubMed Web of Science ®Google Scholar
• 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.
   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
• Rosenberg, N. E., and O. N. Witte. 1988. The viral and cellular forms of the Abelson (abl) oncogene. Adv. Virus Res. 54:39–81.
   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 Fuji- nami sarcoma virus p130gag-fps Mol. Cell. Biol. 6:4396–4408.
   Google Scholar
• Schiff-Maker, L., M. C. Burns, J. B. Konopka, S. Clark, O. N. Witte, and N. Rosenberg. 1986. Monoclonal antibodies specific for v-abl- and c-abl-encoded molecules. J. Virol. 57:1182–1186.
   PubMedGoogle Scholar
• Scott, M. L., and D. Baltimore. Unpublished data.
   Google Scholar
• Skolnick, E. Y., B. Margolis, M. Mohammadi, E. Lowenstein, R. Fischer, A. Drepps, A. Ullrich, and J. Schlessinger. 1991. Cloning of P13 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases. Cell 65:83–90.
   PubMedGoogle Scholar
• Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31–40.
   PubMed Web of Science ®Google Scholar
• Snyder, M. A., J. M. Bishop, W. W. Colby, and A. D. Levinson. 1983. Phosphorylation of tyrosine-416 is not required for the transforming properties and kinase activity of pp60v-src. Cell 32:891–901.
   PubMed Web of Science ®Google Scholar
• Trahey, M., G. Wong, R. Halenbeck, B. Rubinfeld, G. A. Martin, M. Ladner, C. M. Long, W. J. Crosier, K. Watt, K. Koths, and F. McCormick. 1988. Molecular cloning of two types of GAP cDNA from human placenta. Science 242:1697–1700.
   PubMed Web of Science ®Google Scholar
• Ullrich, A., and J. Schlessinger. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell 61:203–212.
   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 hostdependent 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. Scoinick, 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., and J. T. Parsons. 1989. Deletions and insertions within an amino-terminal domain of pp60v-irc inactivate transformation and modulate membrane stability. J. Virol. 63:291–302.
   PubMedGoogle Scholar
• Wüthrich, K. 1986. NMR of proteins and nucleic acids, p. 28–31. John Wiley & Sons, Inc., New York.
   Google Scholar