Functional Specificity of Cytoplasmic and Transmembrane Tyrosine Kinases: Identification of 130- and 75-Kilodalton Substrates of c-fps/fes Tyrosine Kinase in Macrophages

Refrences

• Baccarini, M., D. M. Sabatini, H. App, U. R. Rapp, and E. R. Stanley. 1990. Colony stimulating factor-1 (CSF-1) stimulates temperature dependent phosphorylation and activation of the RAF-1 proto-oncogene product. EMBO J. 9: 3649–3657.
   PubMedGoogle Scholar
• Birge, R. B., and H. Hanafusa. 1993. Closing in on SH2 specificity. Science 262: 1522–1524.
   PubMedGoogle Scholar
• Brott, B. K., S. Decker, M. O'Brien, and R. Jove. 1991. Molecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein. Mol. Cell. Biol. 11: 5059–5067.
   PubMedGoogle Scholar
• Cantley, L., 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
• Cooper, J. A., B. M. Sefton, and T. Hunter. 1984. Diverse mitogenic agents induce the phosphorylation of two related 42,000-dalton proteins on tyrosine in quiescent chick cells. Mol. Cell. Biol. 4: 30–37.
   PubMed Web of Science ®Google Scholar
• DeClue, J. E., K. Zhang, P. Redford, W. C. Vass, and D. R. Lowy. 1991. Suppression of src transformation by overexpression of full-length GTPase-activating protein (GAP) or the GAP C terminus. Mol. Cell. Biol. 11: 2819–2825.
   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
• Fantl, W. J., J. A. Escobedo, G. A. Martin, C. W. Turck, M. del Rosario, F. McCormick, and L. T. Williams. 1992. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways. Cell 69: 413–423.
   PubMedGoogle Scholar
• Fantl, W. J., D. E. Johnson, and L. T. Williams. 1993. Signalling by receptor tyrosine kinases. Annu. Rev. Biochem. 62: 453–481.
   PubMed Web of Science ®Google Scholar
• Feldman, R. A, J. L. Gabrilove, J. P. Tarn, M. A. S. Moore, and H. Hanafusa. 1985. Specific expression of the cellular fps/fes-encoded protein NCP92 in normal and leukemic myeloid cells. Proc. Natl. Acad. Sci. USA 82: 2379–2383.
   PubMed Web of Science ®Google Scholar
• Feldman, R. A, D. R. Lowy, and W. C. Vass. 1990. Selective potentiation of c-fps/fes transforming activity by a phosphatase inhibitor. Oncogene Res. 5: 187–197.
   PubMedGoogle Scholar
• Feldman, R. A, D. R. Lowy, W. C. Vass, and T. J. Velu. 1989. A highly efficient retroviral vector allows detection of the transforming activity of the human c-fps/fes proto-oncogene. J. Virol. 63: 5469–5474.
   PubMedGoogle Scholar
• Feldman, R. A, W. C. Vass, and P. E. Tambourin. 1987. Human cellular fps/fes cDNA rescued via retroviral shuttle vector encodes myeloid cell NCP92 and has transforming potential. Oncogene Res. 1: 441–458.
   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
• Gutkind, J. S., P. M. Lacal, and K. C. Robbins. 1990. Thrombin-dependent association of phosphatidylinositol-3 kinase with p60c-src and p59fyn in human platelets. Mol. Cell. Biol. 10: 3806–3809.
   PubMedGoogle Scholar
• Gutkind, J. S., and K. C. Robbins. 1992. Activation of transforming G protein-coupled receptors induces rapid tyrosine phosphorylation of cellular proteins, including pl25FAK and the pl30 v-src substrate. Biochem. Biophys. Res. Commun. 188: 155–161.
   PubMedGoogle Scholar
• Hanafusa, H. 1988. The fps/fes oncogene, p. 39–57. In E. P. Reddy, A. M. Skalka, and T. Curran (ed.), The oncogene handbook. Elsevier Science Publishing, Inc., New York.
   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
• Jücker, M., M. Schaadt, V. Diehl, S. Poppema, D. Jones, and H. Tesch. 1990. Heterogeneous expression of proto-oncogenes in Hodgkin's disease derived cell lines. Hematol. Oncol. 8: 191–204.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Kanner, S. B., A. B. Reynolds, W.-C. R. Wang, R. R. Vines, and J. T. Parsons. 1991. The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110. EMBO J. 10: 1889–1898.
   Google Scholar
• Kazlauskas, A., and J. Cooper. 1990. Phosphorylation of the PDGF receptor β subunit creates a tight binding site for phosphatidylinositol 3 kinase. EMBO J. 9: 3279–3286.
   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, D. Anderson, X. Liu, G. Mbamalu, and T. Pawson. 1992. Multiple SH2-mediated interactions in v-src-transformed cells. Mol. Cell. Biol. 12: 1366–1374.
   PubMedGoogle Scholar
• Ladner, M. B., G. A. Martin, J. A. Noble, V. P. Wittman, M. K. Warren, M. McGrogan, and E. R. Stanley. 1988. cDNA cloning and expression of murine CSF-1 from L929 cells. Proc. Natl. Acad. Sci. USA 85: 6706–6710.
   PubMed Web of Science ®Google Scholar
• Li, W., and E. R. Stanley. 1991. Role of dimerization and modification of the CSF-1 receptor in its activation and internalization during the CSF-1 response. EMBO J. 10: 277–288.
   PubMed Web of Science ®Google Scholar
• MacDonald, I., J. Levy, and T. Pawson. 1985. Expression of the mammalian c-fes protein in hematopoietic cells and identification of a distinc fes-related protein. Mol. Cell. Biol. 5: 2543–2551.
   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
• 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
• 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., P. 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
• McGlade, J., A. Cheng, G. Pelicci, P. G. Pelicci, and T. Pawson. 1992. She proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases. Proc. Natl. Acad. Sci. USA 89: 8869–8873.
   PubMed Web of Science ®Google Scholar
• Morgan, C., J. W. Pollard, and E. R. Stanley. 1987. Isolation and characterization of a cloned growth factor dependent macrophage cell line, BAC1.2F5. J. Cell. Physiol. 130: 420–427.
   PubMed Web of Science ®Google Scholar
• Noris, M., U. S. Vogel, J. B. Gibbs, and M. J. Weber. 1991. Inhibition of v-s/r-induced transformation by a GTPase-activating protein. Mol. Cell. Biol. 11: 2812–2818.
   PubMedGoogle Scholar
• Pawson, T., and G. D. Gish. 1992. SH2 and SH3 domains: from structure to function. Cell 71: 359–362.
   PubMed Web of Science ®Google Scholar
• Payne, D. M., A. J. Rossomando, P. Martino, A. K. Erikson, J.-H. Her, J. Shabanowitz, D. F. Hunt, M. J. Weber, and T. W. Sturgill. 1991. Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase). EMBO J. 10: 885–892.
   PubMed Web of Science ®Google Scholar
• Pelicci, G., L. Lanfrancone, F. Grignani, J. McGlade, F. Cavallo, G. Forni, I. Nicoletti, F. Grignani, T. Pawson, and P. G. Pelicci. 1992. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 70: 93–104.
   PubMed Web of Science ®Google Scholar
• Reedyk, M., X. Liu, and T. Pawson. 1990. Interactions of phosphatidylinositol kinase, GTPase-activating protein (GAP), and GAP-associated proteins with the colony-stimulating factor 1 receptor. Mol. Cell. Biol. 10: 5601–5608.
   PubMedGoogle Scholar
• Reedijk, M., X. Liu, P. van der Geer, K. Letwin, M. D. Waterfield, T. Hunter, and T. Pawson. 1992. Tyr 721 regulates specific binding of the CSF-1 receptor kinase insert to PI 3′-kinase SH2 domains: a model for SH2-mediated receptor-target interactions. EMBO J. 11: 1365–1372.
   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 p60src with two tyrosine-phosphorylated cellular proteins. Mol. Cell. Biol. 9: 629–638.
   PubMed Web of Science ®Google Scholar
• Rossomando, A. J., D. M. Payne, M. J. Weber, and T. W. Sturgill. 1989. Evidence that pp42, a major tyrosine kinase target protein, is a mitogen-activated serine/threonine protein kinase. Proc. Natl. Acad. Sci. USA 86: 6940–6943.
   PubMed Web of Science ®Google Scholar
• Rozakis-Adcock, M., J. McGlade, G. Mbamalu, G. Pellici, R. Daly, W. Li, A. Batzer, S. Thomas, J. Brugge, P. G. Pellici, J. Schlessinger, and T. Pawson. 1992. Association of the She and Grb2/ Sem5 SH2-containing proteins is implicated in activation of the ras pathway by tyrosine kinases. Nature (London) 360: 689–692.
   PubMed Web of Science ®Google Scholar
• Sadowski, I., J. 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
• Samarut, J., B. Mathey-Prevot, and H. Hanafusa. 1985. Preferential expression of the c-fps protein in chicken macrophages and granulocytic cells. Mol. Cell. Biol. 5: 1067–1072.
   PubMedGoogle Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
   Google Scholar
• Schaller, M. D., C. A. Borgman, B. C. Cobb, 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.
   PubMed Web of Science ®Google Scholar
• Sengupta, A., W.-K. Liu, Y. G. Yeung, D. C. Y. Yeung, A. R. FrackeltonJr., and E. R. Stanley. 1988. Identification and subcellular localization of proteins that are rapidly phosphorylated in tyrosine in response to colony-stimulating factor 1. Proc. Natl. Acad. Sci. USA 85: 8062–8067.
   PubMed Web of Science ®Google Scholar
• Sherr, C. J. 1991. Mitogenic response to colony-stimulating factor 1. Trends Genet. 7: 398–402.
   PubMedGoogle Scholar
• Sherr, C. J., C. W. Rettenmier, R. Sacca, M. F. Roussel, and E. R. Stanley. 1985. The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF-1. Cell 41: 665–676.
   PubMed Web of Science ®Google Scholar
• Shurtleff, S. A, J. R. Downing, C. O. Rock, S. A. Hawkins, M. F. Roussel, and C. J. Sherr. 1990. Structural features of the colony-stimulating factor 1 receptor that affect its association with phosphatidylinositol 3-kinase. EMBO J. 9: 2415–2421.
   PubMed Web of Science ®Google 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
• Songyang, Z., et al. Submitted for publication.
   Google Scholar
• Songyang, Z., S. E. Shoelson, M. Chaudhury, G. Gish, T. Pawson, W. G. Haser, F. King, T. Roberts, S. Ratnofsky, R. J. Lechleider, B. G. Neel, R. B. Birge, J. E. Fajardo, M. Chou, H. Hanafusa, B. Schaffhausen, and L. C. Cantley. 1993. SH2 domains recognize specific phosphopeptide sequences. Cell 72: 767–778.
   PubMed Web of Science ®Google Scholar
• Songyang, Z., S. E. Shoelson, J. McGlade, P. Olivier, T. Pawson, X. R. Bustelo, M. Barbacid, H. Sabe, H. Hanafusa, T. Yi, R. Ren, D. Baltimore, S. Ratnofsky, R. A. Feldman, and L. C. Cantley. 1994. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol. Cell. Biol. 14: 2777–2785.
   PubMed Web of Science ®Google Scholar
• Stanley, E. R. 1985. The macrophage colony stimulating factor, CSF-1. Methods Enzymol. 116: 564–587.
   PubMed Web of Science ®Google Scholar
• Stanley, E. R. CSF-1. In A. Thompson, and T. Picknett (ed.), The cytokine handbook, 2nd ed., in press. Academic Press Ltd., London.
   Google Scholar
• Thomas, S. M., M. DeMarco, G. D'Arcangelo, S. Halegoua, and J. Brugge. 1992. Ras is essential for nerve growth factor- and phorbol ester-induced tyrosine phosphorylation of MAP kinases. Cell 68: 1031–1040.
   PubMed Web of Science ®Google Scholar
• Ulrich, A., and J. Schlessinger. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell 61: 203–212.
   PubMed Web of Science ®Google Scholar
• Varticovski, L. B., D. Druker, D. Morrison, L. Cantley, and T. Roberts. 1989. The colony stimulating factor-1 receptor associates with and activates phosphatidylinositol-3 kinase. Nature (London) 342: 699–702.
   PubMed Web of Science ®Google Scholar
• Vojtek, A. B., S. Hollemberg, and J. Cooper. 1993. Mammalian ras interacts directly with the serine/threonine kinase raf. Cell 74: 205–214.
   PubMed Web of Science ®Google Scholar
• Warne, P. H., P. R. Viciana, and J. Downward. 1993. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature (London) 364: 352–355.
   PubMed Web of Science ®Google Scholar
• Wood, K. W., C. Sarnecki, T. Roberts, and J. Blenis. 1992. Ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK. Cell 68: 1041–1050.
   PubMed Web of Science ®Google Scholar
• Zachary, I., J. Sinnett-Smith, and E. Rozengurt. 1992. Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate. J. Biol. Chem. 267: 19031–19034.
   Google Scholar
• Zhang, X., J. Settleman, J. M. Kyriakis, E. Takeuchi-Suzuki, S. J. Elledge, M. S. Marshall, J. T. Binder, U. R. Rapp, and J. Avruch. 1993. Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1. Nature (London) 364: 308–313.
   PubMed Web of Science ®Google Scholar