GTPase-Activating Protein and Phosphatidylinositol 3-Kinase Bind to Distinct Regions of the Platelet-Derived Growth Factor Receptor β Subunit

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
• Auger, K. R., S. A. Serunian, S. P. Soltoff, P. Libby, and L. C. Cantley. 1989. PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells. Cell 57:167–175.
   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
• Courtneidge, S. Α., R. M. Kypta, J. A. Cooper, and A. Kazlauskas. 1991. Platelet-derived growth factor receptor sequences important for binding of Src family tyrosine kinases. Cell Growth Differ. 2:483–486.
   PubMedGoogle Scholar
• Coughlin, S. R., J. A. Escobedo, and L. T. Williams. 1989. Role of phosphatidylinositol kinase in PDGF receptor signal transduction. Science 243:1191–1194.
   PubMed Web of Science ®Google 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
• Escobedo, J. Α., D. R. Kaplan, W. M. Kavanaugh, C. W. Turck, and L. T. Williams. 1991. A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine. Mol. Cell. Biol. 11:1125–1132.
   PubMed Web of Science ®Google Scholar
• Escobedo, J. Α., S. Navankasattusas, W. M. Kavanaugh, D. Milfay, V. A. Fried, and L. T. Williams. 1991. cDNA cloning of a novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor. Cell 65:75–82.
   PubMed Web of Science ®Google Scholar
• Escobedo, J. Α., and L. T. Williams. 1988. A PDGF receptor domain essential for mitogenesis but not for many other responses to PDGF. Nature (London) 335:85–87.
   PubMed Web of Science ®Google Scholar
• Fantl, W. J., J. A. Escobedo, and L. T. Williams. 1989. Mutations of the platelet-derived growth factor receptor that cause a loss of ligand-induced conformational change, subtle changes in kinase activity, and impaired ability to stimulate DNA synthesis. Mol. Cell. Biol. 9:4473–4478.
   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., and H. Hanafusa. 1991. Requirement of phosphatidylinositol-3 kinase modification for its association with p60src Mol. Cell. Biol. 11:1972–1979.
   Google Scholar
• Gibbs, J. Β., Μ. S. Marshall, Ε. Μ. Scolnick, R. A. F. Dixon, and U. S. Vogel. 1990. Modulation of guanine nucleotides bound to Ras in NIH 3T3 cells by oncogenes, growth factors, and the GTPase activating protein (GAP). J. Biol. Chem. 265:20437–20442.
   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
• Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual, p. 309–311. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Hart, C. E., J. W. Forstrom, J. D. Kelly, R. A. Seifert, R. A. Smith, R. Ross, M. J. Murray, and D. F. Bowen-Pope. 1988. Two classes of PDGF receptor recognize different isoforms of PDGF. Science 240:1529–1531.
   PubMed Web of Science ®Google Scholar
• Hart, C. E., R. A. Seifert, R. Ross, and D. F. Bowen-Pope. 1987. Synthesis, phosphorylation, and degradation of multiple forms of the platelet-derived growth factor receptor studies using a monoclonal antibody. J. Biol. Chem. 262:10780–10785.
   PubMedGoogle Scholar
• Heidaran, Μ. Α., J. H. Pierce, D. Lombardi, M. Ruggiero, J. S. Gutkind, T. Matsui, and S. A. Aaronson. 1991. Deletion or substitution within the α platelet-derived growth factor receptor kinase insert domain: effects on functional coupling with intracellular signaling pathways. Mol. Cell. Biol. 11:134–142.
   PubMedGoogle Scholar
• Heldin, C.-H., and B. Westermark. 1990. Platelet-derived growth factor: mechanism of action and possible in vivo function. Cell Regul. 1:555–566.
   PubMedGoogle Scholar
• Kaplan, D. R., D. K. Morrison, G. Wong, F. McCormick, and L. T. Williams. 1990. PDGF β-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex. Cell 61:125–133.
   PubMed Web of Science ®Google Scholar
• Kaplan, D. R., M. Whitman, B. Schaffhausen, D. C. Pallas, M. White, L. Cantley, and Τ. Μ. 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
• Kashishian, Α., A. Kazlauskas, and J. A. Cooper. 1992. Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo. EMBO J. 11:1373–1382.
   PubMed Web of Science ®Google Scholar
• Kazlauskas, Α., D. Bowen-Pope, R. Seifert, C. E. Hart, and J. A. Cooper. 1988. Different effects of homo- and heterodimers of platelet-derived growth factor A and Β chains on human and mouse fibroblasts. EMBO J. 7:3727–3735.
   PubMed Web of Science ®Google Scholar
• Kazlauskas, Α., and J. A. Cooper. 1988. Protein kinase C mediates platelet-derived growth factor-induced tyrosine phosphorylation of p42. J. Cell Biol. 106:1395–1402.
   PubMed Web of Science ®Google Scholar
• Kazlauskas, Α., and J. A. Cooper. 1989. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins. Cell 58:1121–1133.
   PubMedGoogle Scholar
• Kazlauskas, Α., and J. A. Cooper. 1990. Phosphorylation of the PDGF receptor β subunit creates a tight binding site for phosphatidylinositol 3 kinase. EMBO J. 9:3279–3266.
   PubMed Web of Science ®Google Scholar
• Kazlauskas, Α., D. L. Durden, and J. A. Cooper. 1991. Functions of the major tyrosine phosphorylation site of the PDGF receptor β subunit. Cell Regul. 2:413–425.
   PubMedGoogle Scholar
• Kazlauskas, Α., C. Ellis, T. Pawson, and J. A. Cooper. 1990. Binding of GAP to activated PDGF receptors. Science 247:1578–1581.
   PubMedGoogle Scholar
• Kelly, J. D., B. A. Haldeman, F. J. Grant, M. J. Murray, R. A. Seifert, D. F. Bowen-Pope, J. A. Cooper, and A. Kazlauskas. 1991. Platelet-derived growth factor (PDGF) stimulates receptor subunit dimerization and intersubunit trans-phosphorylation. J. Biol. Chem. 266:8987–8992.
   PubMedGoogle 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
• Koch, C. Α., 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
• Kumjian, D. Α., Μ. I. Wahl, S. G. Rhee, and T. O. Daniel. 1989. Platelet-derived growth factor (PDGF) binding promotes physical association of PDGF receptor with phospholipase C. Proc. Natl. Acad. Sci. USA 86:8232–8236.
   PubMed Web of Science ®Google Scholar
• Kypta, R. M., Y. Goldberg, E. T. Ulug, and S. A. Courtneidge. 1990. Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell 62:481–492.
   PubMed Web of Science ®Google Scholar
• Matsuda, M., B. J. Mayer, and H. Hanafusa. 1991. Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins. Mol. Cell. Biol. 11:1607–1613.
   PubMedGoogle Scholar
• Matsui, T., J. H. Pierce, T. P. Fleming, J. S. Greenberger, W. J. LaRochelle, M. Ruggiero, and S. A. Aaronson. 1989. Independent expression of human α or β platelet-derived growth factor cDNAs in a naive hematopoietic cell leads to functional coupling with mitogenic and chemotactic signaling pathways. Proc. Natl. Acad. Sci. USA 86:8314–8318.
   PubMed Web of Science ®Google Scholar
• Meisenhelder, J., P.-G. Suh, S. G. Rhee, and T. Hunter. 1989. Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro. Cell 57:1109–1122.
   PubMed Web of Science ®Google Scholar
• Miller, A. D., and G. J. Rosman. 1989. Improved retroviral vectors gene transfer and expression. BioTechniques 7:980–990.
   PubMed Web of Science ®Google Scholar
• Molloy, C. J., D. P. Bottaro, T. P. Fleming, M. S. Marshall, J. B. Gibbs, and S. A. Aaronson. 1989. PDGF induction of tyrosine phosphorylation of GTPase activating protein. Nature (London) 342:711–714.
   PubMed Web of Science ®Google Scholar
• Morrison, D. K., D. K. Kaplan, J. A. Escobedo, U. R. Τ. Μ. Roberts, and L. T. Williams. 1989. Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF β-receptor. Cell 58:649–657.
   PubMed Web of Science ®Google Scholar
• Morrison, D. K., D. R. Kaplan, S. G. Rhee, and L. T. Williams. 1990. Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-7 with the PDGF receptor signaling complex. Mol. Cell. Biol. 10:2359–2366.
   PubMedGoogle Scholar
• Nishibe, S., M. I. Wahl, S. Μ. Τ. Hernandez-Sotomayor, Ν. Κ. Tonks, S. G. Rhee, and G. Carpenter. 1990. Increase of the catalytic activity of phospholipase C-γ1 by tyrosine phosphorylation. Science 250:1253–1256.
   PubMed Web of Science ®Google Scholar
• Otsu, M., I. Hiles, I. Gout, M. J. Fry, F. Ruiz-Larrea, G. Panayotou, A. Thompson, R. Dhand, J. Hsuan, N. Totty, A. D. Smith, S. J. Morgan, S. A. Courtneidge, P. J. Parker, and M. D. Waterfield. 1991. Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/ppp60c-src complexes, and PI3-kinase. Cell 65:91–104.
   PubMed Web of Science ®Google Scholar
• Pendergast, A. M., A. J. Muller, M. H. Havlik, Y. Maru, and Ο. Ν. 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
• Reedijk, M., S. 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.
   PubMed Web of Science ®Google Scholar
• Rottapel, R., M. Reedyk, D. E. Williams, S. D. Lyman, D. M. Anderson, T. Pawson, and A. Bernstein. 1991. The Steel/W transduction pathway: Kit autophosphorylation and its association with a unique subset of cytoplasmic signaling proteins is induced by the steel factor. Mol. Cell. Biol. 11:3043–3051.
   PubMedGoogle Scholar
• Satoh, T., M. Endo, M. Nakafuku, S. Nakamura, and Y. Kaziro. 1990. Platelet-derived growth factor stimulated formation of active p21ras GTP complex in Swiss mouse 3T3 cells. Proc. Natl. Acad. Sci. USA 87:5993–5997.
   PubMed Web of Science ®Google Scholar
• Seifert, R. Α., C. E. Hart, P. E. Phillips, J. W. Forstrom, R. Ross, M. J. Murray, and D. F. Bowen-Pope. 1989. Two different subunits associate to create isoform-specific platelet-derived growth factor receptors. J. Biol. Chem. 264:8771–8778.
   PubMed Web of Science ®Google Scholar
• Skolnik, E. Y., B. Margolis, M. Mohammadi, E. Lowenstein, R. Fischer, A. Drepps, A. Ullrich, and J. Schlessinger. 1991. Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases. Cell 65:83–90.
   PubMed Web of Science ®Google Scholar
• Sultzman, L., C. Ellis, L.-L. Lin, T. Pawson, and J. Knopf. 1991. Platelet-derived growth factor increases the in vivo activity of phospholipase C-γ1 and phospholipase C-72. Mol. Cell. Biol. 11:2018–2025.
   PubMed Web of Science ®Google Scholar
• Ullrich, Α., and J. Schlessinger. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell 61:203–212.
   PubMed Web of Science ®Google Scholar
• Wahl, M. I., N. E. Olashaw, S. Nishibe, S. G. Rhee, W. J. Pledger, and G. Carpenter. 1989. Platelet-derived growth factor induces rapid and sustained tyrosine phosphorylation of phospholipase C-γ in quiescent BALB/c 3T3 cells. Mol. Cell. Biol. 9:2934–2943.
   PubMedGoogle Scholar
• Whitman, M., D. Kaplan, T. Roberts, and L. Cantley. 1987. Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Biochem. J. 247:165–174.
   PubMed Web of Science ®Google Scholar
• Williams, L. T. 1989. Signal transduction by the platelet-derived growth factor receptor. Science 243:1564–1570.
   PubMed Web of Science ®Google Scholar
• Williams, L. T. (University of California, San Francisco). Personal communication.
   Google Scholar
• Yeh, H.-J., K. G. Ruit, Y.-X. Wang, W. C. Parks, W. D. Snider, and T. F. Deuel. 1991. PDGF Α-chain gene is expressed by mammalian neurons during development and in maturity. Cell 64:209–216.
   PubMed Web of Science ®Google Scholar
• Yu, J.-C., M. A. Heidaran, J. H. Pierce, J. S. Gutkind, D. Lombardi, M. Ruggiero, and S. A. Aaronson. 1991. Tyrosine mutations within the α platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction. Mol. Cell. Biol. 11:3780–3785.
   PubMed Web of Science ®Google Scholar