50
Views
49
CrossRef citations to date
0
Altmetric
Cell Growth and Development

Hierarchy of Binding Sites for Grb2 and Shc on the Epidermal Growth Factor Receptor

, , , &
Pages 5192-5201 | Received 01 Feb 1994, Accepted 05 May 1994, Published online: 30 Mar 2023

References

  • Backer, J. M., M. G. Myers, Jr., S. E. Shoelson, D. J. Chin, X. J. Sun, M. Miralpeix, P. Hu, B. J. Margolis, Ε. Υ. Skolnik, J. Schlessinger, and M. F. White. 1992. Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J. 11:3469–3479.
  • Bellot, F., W. Moolenar, R. Kris, B. Mirakhur, I. Verlaan, A. Ullrich, J. Schlessinger, and S. Felder. 1990. High-affinity epidermal growth factor binding is specifically reduced by a monoclonal antibody, and appears necessary for early responses. J. Cell Biol. 110:491–502.
  • Bertics, P. J., and G. N. Gill. 1985. Self-phosphorylation enhances the protein-tyrosine kinase activity of the epidermal growth factor receptor. J. Biol. Chem. 260:14642–14647.
  • Blenis, J. 1993. Signal transduction via the MAP kinases: proceed at your own RSK. Proc. Natl. Acad. Sci. USA 90:5889–5892.
  • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
  • Buday, L., and J. Downward. 1993. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adaptor protein, and Sos nucleotide exchange factor. Cell 73:611–620.
  • Burns, L. A., L. M. Karnitz, S. L. Sutor, and R. T. Abraham. 1993. Interleukin-2-induced tyrosine phosphorylation of p52shc in Τ lymphocytes. J. Biol. Chem. 268:17659–17661.
  • Chardin, P., J. Camonis, W. L. Gale, L. Van Aelst, J. Schlessinger, M. Η. Wigler, and D. Bar-Sagi. 1993. Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2. Science 260:1338–1343.
  • Cooper, J. A., and A. Kashishian. 1993. In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase. Mol. Cell. Biol. 13:1737–1745.
  • Decker, S. J. 1993. Transmembrane signaling by epidermal growth factor receptors lacking autophosphorylation sites. J. Biol. Chem. 268:9176–9179.
  • Dilworth, S. M., C. E. P. Brewster, M. D. Jones, L. Lanfrancone, G. Pelicci, and P. G. Pelicci. 1994. Transformation by polyoma virus middle T-antigen involves the binding and tyrosine phosphorylation of She. Nature (London) 367:87–90.
  • Downward, J., P. Parker, and M. D. Waterfield. 1984. Autophosphorylation sites on the epidermal growth factor receptor. Nature (London) 311:483–485.
  • Eck, M. J., S. E. Shoelson, and S. C. Harrison. 1993. Recognition of a high affinity phosphotyrosyl peptide by the Src homology 2 domain of p56lck. Nature (London) 362:87–91.
  • Egan, S. E., B. W. Giddings, M. W. Brooks, L. Buday, A. M. Sizeland, and R. A. Weinberg. 1993. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature (London) 363:45–51.
  • Fägerstam, L. 1991. A non-label technology for real time biospe-cific interaction analysis. Tech. Protein Chem. 2:65–71.
  • 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.
  • Felder, S., M. Zhou, P. Hu, J. M. Urena, A. Ullrich, M. Chaudhuri, M. F. White, S. E. Shoelson, and J. Schlessinger. 1993. SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol. 13:1449–1455.
  • Flores-Riveros, J. R., E. Sibley, T. Kastelic, and D. M. Lane. 1989. Substrate phosphorylation catalyzed by the insulin receptor tyrosine kinase. Kinetic correlation to autophosphorylation of specific sites in the β subunit. J. Biol. Chem. 264:21557–21572.
  • Gale, N. W., S. Kaplan, E. J. Lowenstein, J. Schlessinger, and D. Bar-Sagi. 1993. Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras. Nature (London) 363:88–92.
  • Gotoh, N., A. Tojo, K. Muroya, Y. Hashimoto, S. Hattori, S. Nakamura, T. Takenawa, Y. Yazaki, and M. Shibuya. 1994. Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphorylation of She protein and Shc-Grb2/ASH association and retains mitogenic activity. Proc. Natl. Acad. Sci. USA 91:167–171.
  • Honegger, A. M., T. J. Dull, F. Bellot, E. Van Obberghen, D. Szapary, A. Schmidt, A. Ullrich, and J. Schlessinger. 1988. Biological activities of EGF-receptor mutants with individually altered autophosphorylation sites. EMBO J. 7:3045–3052.
  • Honegger, A. M., T. J. Dull, D. Szapary, A. Komoriya, R. Kris, A. Ullrich, and J. Schlessinger. 1988. Kinetic parameters of the protein kinase activity of EGF-receptor mutants with individually altered autophosphorylation sites. EMBO J. 7:3053–3060.
  • 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.
  • Johnsson, B., S. Lofas, and G. Lindqvist. 1991. Immobilization of proteins to a carboxymethyldextran modified gold surface for biospecific interaction analysis in surface plasmon resonance. Anal. Biochem. 198:268–277.
  • Kamps, M. P., and Β. M. Sefton. 1988. Identification of multiple novel polypeptide substrates from v-src, v-yes, v-fps, v-ros, and v-erb-B oncogenic tyrosine kinases utilizing antisera against phos-photyrosine. Oncogene 2:305–315.
  • Kashishian, A., and J. A. Cooper. 1993. Phosphorylation sites at the C terminus of the platelet-derived growth factor receptor bind phospholipase Cγ1. Mol. Cell. Biol. 13:49–57.
  • Kashishian, A., A. Kazlauskaus, and J. A. Cooper. 1992. Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI 3-kinase in vivo. EMBO J. 11:1373–1382.
  • Kazlauskas, A., and J. A. Cooper. 1989. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins. Cell 58:1121–1133.
  • Kazlauskas, A., and J. A. Cooper. 1990. Phosphorylation of the PDGF receptor β subunit creates a tight binding site for phosphatidyl 3-kinase. EMBO J. 9:3279–3286.
  • Kazlauskas, A., C. Ellis, T. Pawson, and J. A. Cooper. 1990. Binding of GAP to activated PDGF receptors. Science 247:1578–1581.
  • Kazlauskas, A., G. S. Feng, T. Pawson, and M. Valius. 1993. The 64-kDa protein that associates with the platelet-derived growth factor receptor β subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp. Proc. Natl. Acad. Sci. USA 90:6939–6942.
  • Kazlauskas, A., A. Kashishian, J. A. Cooper, and M. Valius. 1992. GTPase-activating protein and phosphatidyl 3-kinase bind to distinct regions of the platelet-derived growth factor receptor β subunit. Mol. Cell. Biol. 12:2534–2544.
  • Kris, R., I. Lax, W. Gullick, D. M. Waterfield, A. Ullrich, M. Fridkin, and J. Schlessinger. 1985. Antibodies against a synthetic peptide as a probe for the kinase activity of the avian EGF-receptor and v-erbB protein. Cell 40:619–625.
  • Li, N., A. G. Batzer, R. J. Daly, V. Yajnik, Ε. Υ. Skolnik, P. Chardin, D. Bar-Sagi, B. Margolis, and J. Schlessinger. 1993. The guanine nucleotide releasing factor, hSOS1, binds to GRB2 linking receptor tyrosine kinases to Ras signaling. Nature (London) 363:85–88.
  • Li, N., J. Schlessinger, and B. Margolis. Autophosphorylation mutants of the EGF-receptor signal through auxiliary mechanisms involving SH2 domain proteins. Submitted for publication.
  • 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 SH2 and SH3 domain-containing protein Grb2 links receptor tyrosine kinases to ras signaling. Cell 70:431–442.
  • Margolis, B., F. Bellot, A. M. Honegger, A. Ullrich, J. Schlessinger, and A. Zilberstein. 1990. Tyrosine kinase activity is essential for the association of phospholipase C-7 with the epidermal growth factor receptor. Mol. Cell. Biol. 10:435–441.
  • Margolis, B., I. Lax, R. Kris, M. N. Dombalagian, A. M. Honegger, R. Howk, D. Givol, A. Ullrich, and J. Schlessinger. 1989. All autophosphorylation sites of the epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxy-terminal tails. J. Biol. Chem. 264:10667–10671.
  • 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.
  • Margolis, B., S. G. Rhee, S. Felder, M. Mervic, R. Lyall, A. Levitzki, A. Ullrich, A. Zilberstein, and J. Schlessinger. 1989. EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF-receptor signaling. Cell 57:1101–1107.
  • McGlade, J., A. Cheng, C. 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.
  • Mohammadi, M., C. A. Dionne, W. Li, N. Li, T. Spivak, A. M. Honegger, M. Jaye, and J. Schlessinger. 1992. A point mutation at Tyr 766 of FGF receptor eliminates FGF-induced tyrosine phosphorylation of PLC-γ and phosphatidylinositol hydrolysis without affecting mitogenesis. Nature (London) 358:681–684.
  • Mohammadi, M., A. M. Honegger, D. Rotin, R. Fischer, F. Bellot, W. Li, C. Dionne, M. Jaye, M. Rubinstein, and J. Schlessinger. 1991. A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Fig) is a binding site for the SH2 domain of phospholipase C-γ1 Mol. Cell. Biol. 11:5068–5078.
  • Mori, S., L. Rönnstrand, K. Yokote, A. Engstrom, S. A. Court-neidge, L. Claesson-Welsh, and C.-H. Heldin. 1993. Identification of two juxtamembrane autophosphorylation sites in the PDGF β-receptor; involvement in the interaction with Src family tyrosine kinases. EMBO J. 12:2257–2264.
  • Nishimura, R., W. Li, A. Kashishian, A. Mondino, M. Zhou, J. Cooper, and J. Schlessinger. 1993. Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor. Mol. Cell. Biol. 13:6889–6896.
  • Obermeier, A., R. Lammers, K. H. Wiesmuller, G. Jung, J. Schlessinger, and A. Ullrich. 1993. Identification of Trk binding sites for SHC and phosphatidylinositol 3′ kinase and formation of a multimeric signaling complex. J. Biol. Chem. 268:22963–22966.
  • Panayotou, G., G. Gish, P. End, O. Truong, I. Gout, R. Dhand, M. J. Fry, I. Hile, T. Pawson, and M. D. Waterfield. 1993. Interaction between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor β-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach. Mol. Cell. Biol. 13:3567–3576.
  • Pawson, T., and J. Schlessinger. 1993. SH2 and SH3 domains. Curr. Biol. 3:434–442.
  • 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.
  • Pendergast, A. M., L. A. Quilliam, L. D. Cripe, C. H. Bassing, Z. Dai, N. Li, A. G. Batzer, K. M. Rabun, C. J. Der, J. Schlessinger, and M. L. Gishizky. 1993. BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein. Cell 75:175–185.
  • Piccione, E., R. D. Case, S. M. Domchek, P. Hu, M. Chaudhuri, J. M. Backer, J. Schlessinger, and S. E. Shoelson. 1993. Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding. Biochemistry 32:3197–3202.
  • Pronk, G. J., J. McGlade, G. Pelicci, T. Pawson, and J. L. Bos. 1993. Insulin-induced phosphorylation of the 46- and 52 kDa She proteins. J. Biol. Chem. 268:5748–5753.
  • Rönnstrand, L., S. Mori, A.-K. Arridson, A. Eriksson, C. Wernstedt, U. Hellman, L. Claesson-Welsh, and C.-H. Heldin. 1992. Identification of two C-terminal autophosphorylation sites in the PDGF β-receptor: involvement in the interaction with phospho-lipase C-γ. EMBO J. 11:3911–3919.
  • Rosen, O. M., R. Hen-era, Y. Olowe, L. M. Petruzelli, and M. Η. Cobb. 1983. Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc. Natl. Acad. Sci. USA 80:3237–3240.
  • Rotin, D., B. Margolis, M. Mohammadi, R. D. Daly, G. Daum, N. Li, E. H. Fischer, W. H. Burgess, A. Ullrich, and J. Schlessinger. 1992. SH2 domains prevent tyrosine phosphorylation of the EGF-receptor: identification of Tyr 992 as the high affinity binding site for the SH2 domains of phospholipase C7. EMBO J. 11:559–567.
  • Rozakis-Adcock, M., R. Fernley, J. Wade, T. Pawson, and D. Bowtell. 1993. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature (London) 363:83–85.
  • Rozakis-Adcock, M., J. McGlade, G. Mbamalu, G. Pelicci, R. D. Daly, W. Li, A. G. Batzer, S. Thomas, J. Brugge, P. G. Pelicci, 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.
  • Schlessinger, J. 1993. How receptor tyrosine kinases activate Ras. Trends Biochem. Sci. 18:273–275.
  • Schlessinger, J., and A. Ullrich. 1992. Growth factor signaling by receptor tyrosine kinases. Neuron 9:383–391.
  • Skolnik, E. Y., A. G. Batzer, N. Li, E. Lowenstein, M. Mohammadi, B. Margolis, and J. Schlessinger. 1993. Function of GRB2 in linking the insulin receptor to Ras signaling pathway. Science 260:1953–1955.
  • Skolnik, E. Y., C. H. Lee, A. G. Batzer, L. M. Vincentini, M. Zhou, R. Daly, M. J. Myers, Jr., J. M. Backer, A. Ullrich, M. F. White, and J. Schlessinger. 1993. The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signaling. EMBO J. 12:1929–1936.
  • Skolnik, E. Y., B. Margolis, M. Mohammadi, E. Lowenstein, R. Fisher, 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.
  • Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with gluta-thione-S-transferase. Gene 67:31–40.
  • Soler, C., L. Beguinot, and G. Carpenter. 1994. Individual epidermal growth factor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins. J. Biol. Chem. 269:12320–12324.
  • 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. Fajardo, M. M. Chou, B. Schaff-hausen, and L. C. Cantley. 1993. SH2 domains recognize specific phosphopeptide sequences. Cell 72:767–778.
  • Tornqvist, H. E., and J. Avruch. 1988. Relationship of site-specific β subunit tyrosine autophosphorylation to insulin activation on the insulin receptor (tyrosine) protein kinase activity. J. Biol. Chem. 263:4593–4601.
  • Valius, M., C. Bazenet, and A. Kazlauskas. 1993. Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor β subunit and are required for binding of phospholipase Cγ and a 64-kilodalton protein, respectively. Mol. Cell. Biol. 13:133–143.
  • van der Geer, P., and T. Hunter. 1994. Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase binding site, abrogates signal transduction by the murine CSF-1 receptor expressed in Rat-2 fibroblasts. EMBO J. 12:5161–5172.
  • Waksman, G., D. Kominos, S. R. Robertson, N. Pant, D. Baltimore, R. B. Birge, D. Cowburn, H. Hanfusa, B. J. Mayer, M. Overduin, M. D. Resh, C. B. Rios, L. Silverman, and J. Kuriyan. 1992. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine phosphorylated peptides. Nature (London) 358:646–653.
  • Waksman, G., S. Shoelson, N. Pant, D. Cowburn, and J. Kuriyan. 1993. Binding of high affinity phosphotyrosyl peptide in the src SH2 domain: crystal structure of the complexed and peptide-free forms. Cell 72:779–790.
  • Walton, G. M., W. S. Chen, G. Rosenfeld, and G. Gill. 1990. Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrate. J. Biol. Chem. 265:1750–1754.
  • White, M. F., S. E. Shoelson, H. Keutmann, and C. R. Kahn. 1988. A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor. J. Biol. Chem. 263:2969–2980.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.