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Cell Growth and Development

Identification and Sequence Analysis of cDNAs Encoding a 110-Kilodalton Actin Filament-Associated pp60src Substrate

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Pages 7892-7900 | Received 23 Jun 1993, Accepted 22 Sep 1993, Published online: 31 Mar 2023

References

  • Burridge, K., K. Fath, T. Kelly, G. Nuckolls, and C. Turner. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487–525.
  • Buss, J. E., M. P. Kamps, K. Gould, and B. M. Sefton. 1986. The absence of myristic acid decreases membrane binding of pp60src but does not affect tyrosine protein kinase activity. J. Virol. 58:468–474.
  • Buss, J. E., M. P. Kamps, and B. M. Sefton. 1984. Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein. Mol. Cell. Biol. 4:2697–2704.
  • 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.
  • Cicchetti, P., B. J. Mayer, G. Thiel, and D. Baltimore. 1992. Identification of a protein that binds to the SH3 region of Abl and is similar to BCR and GAP-rho. Science 257:803–806.
  • Cooper, J. A.. 1990. The Src family of protein-tyrosine kinases, p. 85–113. In B. E. Kemp (ed.), Peptides and protein phosphorylation. CRC Press, Boca Raton, Fla.
  • David-Pfeuty, T., and S. J. Singer. 1980. Altered distribution of the cytoskeletal proteins vinculin and α-actinin in cultured fibroblasts transformed by Rous sarcoma virus. Proc. Natl. Acad. Sci. USA 77:6687–6691.
  • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387–395.
  • Drubin, D. G., J. Mulholland, Z. Zhu, and D. Botstein. 1990. Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I. Nature (London) 343:288–290.
  • Felice, G. R., P. Eason, M. V. Nermut, and S. Kellie. 1990. pp60v-src association with the cytoskeleton induces actin reorganization without affecting polymerization status. Eur. J. Cell Biol. 52:47–59.
  • Flynn, D. C., K. C. Fluharty, M. W. Hill, and A. C. Guappone. Unpublished data.
  • Flynn, D. C., and J. T. Parsons. Unpublished data.
  • Flynn, D. C., M. D. Schaller, and J. T. Parsons. 1992. Tyrosine phosphorylation of a 120,000 Dalton membrane-associated protein by the neural form of pp60c-src, pp60csrc+. Oncogene 7:579–583.
  • Gersten, D. M., and J. J. Marchalonis. 1978. A rapid, novel method for the solid-phase derivatization of IgG antibodies for immune-afifinity chromatography. J. Immunol. Methods 24:305–309.
  • Guappone, A. C., M. W. Hill, J. T. Parsons, and D. C. Flynn. Unpublished data.
  • Hu, P., B. Margolis, E. Y. Skolnik, R. Lammers, A. Ullrich, and J. Schlessinger. 1992. Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors. Mol. Cell. Biol. 12:981–990.
  • Huff, J. A., M. A. Jelinek, C. A. Borgman, T. J. Lansing, and J. T. Parsons. 1993. The protooncogene c-sea encodes a transmembrane protein-tyrosine kinase related to the Met/hepato-cyte growth factor/scatter factor receptor. Proc. Natl. Acad. Sci. USA 90:6140–6144.
  • Kamps, M. P., J. E. Buss, and B. M. Sefton. 1985. Mutation of the NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation. Proc. Natl. Acad. Sci. USA 82:4625–4628.
  • Kanner, S. B., A. B. Reynolds, and J. T. Parsons. 1989. Immunoaffinity purification of tyrosine-phosphorylated cellular proteins. J. Immunol. Methods 120:115–124.
  • Kanner, S. B., A. B. Reynolds, R. R. Vines, and J. T. Parsons. 1990. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene encoded tyrosine kinases. Proc. Natl. Acad. Sci. USA 87:3328–3332.
  • Kanner, S. B., A. B. Reynolds, H.-C. Wang, and J. T. Parsons. 1991. The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins pl30 and pllO. EMBO J. 10:1689–1698.
  • Kemp, B. E., and R. B. Pearson. 1990. Protein kinase recognition sequence motifs. Trends Biochem. Sci. 17:342–346.
  • Klippel, A., J. A. Escobedo, W. J. Fantl, and L. T. Williams. 1992. The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor. Mol. Cell. Biol. 12:1451–1459.
  • Kmiecik, T. E., and D. Shalloway. 1987. Activation and suppression of pp60c-src transforming ability by mutation of its primary site of tyrosine phosphorylation. Cell 49:65–73.
  • Koch, 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.
  • Koerner, T. J., J. E. Hill, A. M. Myers, and A. Tzafoloff. 1991. High-expression vectors with multiple cloning sites for construction of trpE fusion genes: pATH vectors. Methods Enzy-mol. 194:477–490.
  • Kozak, M. 1987. An analysis of 5′ noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 20:8125–8130.
  • Lowenstein, E. J., R. J. Daly, A. G. Batzer, W. Li, B. Margolis, R. Lammers, A. Ullrich, E. Y. Skolnik, D. Bar-Sagi, and J. Schlessinger. 1992. The SIC and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell 70:431–442.
  • Mayer, B. J., M. Hamaguchi, and H. Hanafusa. 1988. A novel viral oncogene with structural similarity to phospholipase C. Nature (London) 332:272–275.
  • McGlade, C. J., C. Ellis, M. Reedyk, D. Anderson, G. Mbamalu, A. D. Reith, G. Panayotou, P. End, A. Bernstein, A. Kazlauskas, M. D. Waterfield, and T. Pawson. 1992. SIC domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors. Mol. Cell. Biol. 12:991–997.
  • Olivier, J. P., T. Raabe, M. Henkemeyer, B. Dickson, G. Mbamalu, B. Margolis, J. Schlessinger, E. Hafen, and T. Pawson. 1993. A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of ras guanine nucleotide exchange, SOS. Cell 73:179–192.
  • Parsons, J. T., and M. J. Weber. 1989. Genetics of Src: structure and functional organization of a protein tyrosine kinase. Curr. Top. Microbiol. Immunol. 147:79–127.
  • Pawson, T., and G. D. Gish. 1992. SH2 and SH3 domains: from structure to function. Cell 71:359–362.
  • Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444–2448.
  • 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.
  • Ren, R., B. J. Mayer, P. Cicchetti, and D. Baltimore. 1993. Identification of a ten-amino acid proline-rich SH3 binding site. Science 259:1157–1161.
  • Reynolds, A. B., S. B. Kanner, H.-C. Wang, and J. T. Parsons. 1989. Stable association of activated pp60src with two tyrosine-phosphorylated cellular proteins. Mol. Cell. Biol. 9:3951–3958.
  • 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.
  • 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 carboxy terminus. EMBO J. 6:2359–2364.
  • Rodaway, A. R. F., M. J. E. Sternberg, and D. L. Bentley. 1989. Similarity in membrane proteins. Nature (London) 342:624.
  • Sadowski, I., and T. Pawson. 1987. Catalytic and non-catalytic domains of the Fujinami sarcoma virus p60gap-fps protein-tyrosine kinase distinguished by the expression of v-fps polypeptides in Escherichia coli. Oncogene 1:181–191.
  • Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
  • Schaller, M. D., C. A. Borgman, B. S. Cobb, R. R. Vines, A. B. Reynolds, and J. T. Parsons. 1992. Ppl25FAK, a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc. Natl. Acad. Sci. USA 89:5192–5196.
  • Schaller, M. D., A. H. Bouton, D. C. Flynn, and J. T. Parsons. 1992. Identification and characterization of novel substrates for protein tyrosine kinases. Prog. Nucleic Acid Res. Mol. Biol. 44:205–227.
  • Schultz, A. M., L. E. Henderson, S. Oroszlan, E. A. Garber, and H. Hanafusa. 1985. Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein. Science 227: 427–429.
  • Simon, M. A., G. S. Dodson, and G. M. Rubin. 1993. An SH3-SH2-SH3 protein is required for p21ras1 activation and binds to sevenless and sos proteins, in vitro. Cell 73:169–178.
  • 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.
  • Songyang, Z., S. E. Shoelson, M. Chaudhuri, G. Gish, T. Pawson, W. G. Haser, F. King, T. Roberts, S. Ratnofsky, R. J. Lechleider, B. G. Neel, R. B. Birge, J. E. Fqjardo, M. M. Chou, H. Hanafusa, B. Schaffhausen, and L. C. Cantley. 1993. SH2 domains recognize specific phosphopeptide sequences. Cell 72:767–778.
  • Stahl, M. L., C. R. Ferenz, K. L. Kelleher, R. W. Kriz, and J. Knopp. 1988. Sequence similarity of phospholipase C with the non-catalytic region of Src. Nature (London) 332:269–272.
  • Takeya, T. H., 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.
  • Trahey, M., B. 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 GAP complementary DNA from human placenta. Science 242:1697–1700.
  • Vogel, U. S., R. A. R. Dixon, M. D. Schaber, R. E. Diehl, M. S. Marshall, E. M. Scolnick, I. S. Sigal, and J. A. Gibbs. 1988. Cloning of bovine GAP and its interaction with oncogenic ras p21. Nature (London) 335:90–93.
  • Wu, H., A. B. Reynolds, S. B. Kanner, R. R. Vines, and J. T. Parsons. 1991. Identification and characterization of a novel cytoskeleton-associated pp60src substrate. Mol. Cell. Biol. 11: 5113–5124.
  • Yu, H., M. K. Rosen, T. B. Shin, C. Seidel-Dugan, J. S. Brugge, and S. L. Schreiber. 1992. Solution structure of the SH3 domain of Src and identification of its ligand-binding site. Science 258:1665–1670.

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