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Cell Growth and Development

Multiple Cytokines Stimulate the Binding of a Common 145-Kilodalton Protein to Shc at the Grb2 Recognition Site of Shc

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Pages 6926-6935 | Received 11 May 1994, Accepted 05 Jul 1994, Published online: 30 Mar 2023

REFERENCES

  • Alai, M., A. L. F. Mui, R. L. Cutler, X. R. Bustelo, M. Barbacid, and G. Krystal. 1992. Steel factor stimulates the tyrosine phosphorylation of the proto-oncogene product, p95vav, in human hemopoietic cells. J. Biol. Chem. 267:18021–18025.
  • Argetsinger, L. S., G. S. Campbell, X. Yang, B. A. Witthuhn, O. Silvennoinen, J. N. Ihle, and C. Carter-Su. 1993. Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell 74:237–244.
  • Baltensperger, K., L. M. Kozma, A. D. Cherniack, J. K. Klarlund, A. Chawla, U. Banerjee, and M. P. Czech. 1993. Binding of the Ras activator son of sevenless to insulin receptor substrate-1 signaling complexes. Science 260:1950–1952.
  • Buday, L., and J. Downward. 1993. Epidermal growth factor regulates p21 ras through the formation of a complex of receptor, Grb2 adapter 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 T lymphocytes. J. Biol. Chem. 268:17659–17661.
  • 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.
  • Chabot, B., D. A. Stephenson, V. M. Chapman, P. Besmer, and A. Bernstein. 1988. The proto-oncogene c-kit encoding a transmembrane tyrosine kinase receptor maps to the mouse W locus. Nature (London) 335:88–89.
  • Cutler, R. L., L. Liu, J. E. Damen, and G. Krystal. 1993. Multiple cytokines induce the tyrosine phosphorylation of Shc and its association with Grb2 in hemopoietic cells. J. Biol. Chem. 268:21463–21465.
  • Damen, J., A. L. F. Mui, P. Hughes, K. Humphries, and G. Krystal. 1992. Erythropoietin induced tyrosine phosphorylations in a high erythropoietin receptor expressing lymphoid cell line. Blood 80:1923–1932.
  • Damen, J. E., L. Liu, R. L. Cutler, and G. Krystal. 1993. Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein. Blood 82:2296–2303.
  • 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 Shc. Nature (London) 367:87–90.
  • 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.
  • Fazioli, F., L. Minichiello, B. Maoškovā, W. T. Wong, and P. P. Di Fiore. 1993. epsl5, a novel tyrosine kinase substrate, exhibits transforming activity. Mol. Cell. Biol. 13:5814–5828.
  • Feig, L. A. 1993. The many roads that lead to Ras. Science 260:767–768.
  • 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 Shc protein and Shc-Grb2/ASH association and retains mitogenic activity. Proc. Natl. Acad. Sci. USA 91:167–171.
  • Heldin, C. H. 1991. SH2 domains: elements that control protein interactions during signal transduction. Trends Biochem. Sci. 16:450–452.
  • Kitamura, T., N. Sato, K. Arai, and A. Miyajima. 1991. Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors. Cell 66:1165–1174.
  • 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 252:669–674.
  • Li, N., A. Batzer, R. Daly, V. Yajnik, E. Skolnik, P. Chardin, D. Bar-Sagi, B. Margolis, and J. Schlessinger. 1993. Guanine-nucleotide-releasing factor hSosl binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature (London) 363:85–88.
  • Li, W., R. Nishimura, A. Kashishian, A. G. Batzer, W. J. H. Kim, J. A. Cooper, and J. Schlessinger. 1994. A new function for a phosphotyrosine phosphatase: linking GRB2-Sos to a receptor tyrosine kinase. Mol. Cell. Biol. 14:509–517.
  • 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.
  • Lutticken, C., U. M. Wegenka, J. Yuan, J. Buschmann, C. Schindler, A. Ziemiecki, A. G. Harpur, A. F. Wilks, K. Yasukawa, T. Taga, T. Kishimoto, G. Barbieri, S. Pellegrini, M. Sendtner, P. C. Heinrich, and F. Horn. 1994. Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130. Science 263:89–92.
  • Margolis, B. 1992. Proteins with SH2 SH3 domains: transducers in the tyrosine kinase signaling pathway. Cell Growth Differ. 3:73–80.
  • Marx, J. 1993. Forging a path to the nucleus. Science 260:1588–1590.
  • Matuoka, K., F. Shibasaki, M. Shibata, and T. Takenawa. 1993. Ash/Grb-2, a SH2/SH3-containing protein, couples to signaling for mitogenesis and cytoskeletal reorganization by EGF and PDGF. EMBO J. 12:3467–3473.
  • McGlade, J., A. Cheng, G. Pelicci, P. G. Pelicci, and T. Pawson. 1992. Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases. Proc. Natl. Acad. Sci. USA 89:8869–8873.
  • McGlade, C. J., C. Ellis, M. Reedjik, D. Anderson, G. Mbamalu, A. Reith, G. Panayotou, P. End, A. Bernstein, A. Kazlauskas, M. Waterfield, and T. Pawson. 1992. SH2 domains of signaling proteins control specificity of binding to growth factor receptors. Mol. Cell. Biol. 12:991–997.
  • 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.
  • Mui, A. L. F., R. J. Kay, R. K. Humphries, and G. Krystal. 1992. Ligand-induced phosphorylation of the murine interleukin 3 receptor signals its cleavage. Proc. Natl. Acad. Sci. USA 89:10812–10816.
  • Murthy, S. C., P. Η. B. Sorensen, A. L. F. Mui, and G. Krystal. 1989. Interleukin-3 down-regulates its own receptor. Blood 73:1180–1187.
  • Oakley, B. R., D. R. Kirsch, and N. R. Morris. 1980. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 105:361–363.
  • Obermeier, A., R. Lammers, K.-H. Wiesmüller, 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.
  • O'Farrell, P. H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007–4021.
  • Ohmichi, M., K. Matuoka, T. Takenawa, and A. R. Saltiel. 1994. Growth factors differentially stimulate the phosphorylation of Shc proteins and their association with Grb-2 in PC-12 pheochromo-cytoma cells. J. Biol. Chem. 269:1143–1148.
  • 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 73:179–191.
  • 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.
  • Pronk, G. J., J. McGlade, G. Pelicci, T. Pawson, and J. L. Bos. 1993. Insulin-induced phosphorylation of the 46- and 52-kDa Shc proteins. J. Biol. Chem. 268:5748–5753.
  • Ravichandran, K. S., and S. J. Burakoff. 1994. The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation. J. Biol. Chem. 269:1599–1602.
  • Ravichandran, K. S., K. K. Lee, Z. Songyang, L. C. Cantley, P. Burn, and S. J. Burakoff. 1993. Interaction of Shc with the ζ chain of the T cell receptor upon T cell activation. Science 262:902–905.
  • Reedijk, M., X. Liu, P. van der Geer, K. Letwin, M. D. Waterfield, T. Hunter, and T. Pawson. 1992. Tyr721 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.
  • Rozakis-Adcock, M., R. Feraley, 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. Daly, W. Li, A. Batzer, S. Thomas, J. Brugge, P. G. Pelicci, J. Schlessinger, and T. Pawson. 1992. Association of the Shc and Grb/2Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature (London) 360:689–692.
  • Ruff-Jamison, S., J. McGlade, T. Pawson, K. Chen, and S. Cohen. 1993. Epidermal growth factor stimulates the tyrosine phosphorylation of SHC in the mouse. J. Biol. Chem. 268:7610–7612.
  • Sasaoka, T., B. Draznin, J. W. Leitner, W. J. Langlois, and J. M. Olefsky. 1994. Shc is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras-GTP formation. J. Biol. Chem. 269:10734–10738.
  • Sasaoka, T., D. W. Rose, B. H. Jhun, A. R. Saltiel, B. Draznin, and J. M. Olefsky. 1994. Evidence for a functional role of Shc proteins in mitogenic signaling induced by insulin, insulin-like growth factor-1, and epidermal growth factor. J. Biol. Chem. 269:13689–13694.
  • Silvennoinen, Ο., B. A. Witthuhn, F. W. Quelle, J. L. Cleveland, T. Yi, and J. N. Ihle. 1993. Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction. Proc. Natl. Acad. Sci. USA 90:8429–8433.
  • Skolnik, E. Y., A. Batzer, N. Li, C.-H. Lee, E. Lowenstein, M. Mohammadi, B. Margolis, and J. Schlessinger. 1993. The function of GRB2 in linking the insulin receptor to Ras signaling pathways. Science 260:1953–1955.
  • Skolnik, E. Y., C.-H. Lee, A. Batzer, L. M. Vicentini, 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 signalling. EMBO J. 12:1929–1936.
  • 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, H. Hanafusa, B. Schaffhausen, and L. C. Cantley. 1993. SH2 domains recognize specific phosphopeptide sequences. Cell 72:767–778.
  • Suen, K.-L., X. R. Bustelo, T. Pawson, and M. Barbacid. 1993. Molecular cloning of the mouse grb2 gene: differential interaction of the Grb2 adaptor protein with epidermal growth factor and nerve growth factor receptors. Mol. Cell. Biol. 13:5500–5512.
  • Tobe, K., K. Matuoka, H. Tamemoto, K. Ueki, Y. Kaburagi, S. Asai, T. Noguchi, M. Matsuda, S. Tanaka, S. Hattori, Y. Fukui, Y. Akanuma, Y. Yazaki, T. Takenawa, and T. Kadowaki. 1993. Insulin stimulates association of insulin receptor substrate-1 with the protein abundant Src homology/growth factor receptor-bound protein 2. J. Biol. Chem. 268:11167–11171.
  • Ullrich, A., and J. Schlessinger. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell 61:203–212.
  • Van der Geer, P., and T. Hunter. 1993. Mutation of Tyr697, a GRB2-binding site, and Tyr 721, 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.
  • Wang, J.-K., G. Gao, and M. Goldfarb. 1994. Fibroblast growth factor receptors have different signaling and mitogenic potentials. Mol. Cell. Biol. 14:181–188.
  • Witthuhn, B. A., F. W. Quelle, O. Silvennoinen, T. Yi, B. Tang, O. Miura, and J. N. Ihle. 1993. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell 74:227–236.
  • Wognum, A. W., P. M. Lansdorp, R. K. Humphries, and G. Krystal. 1990. Detection and isolation of the erythropoietin receptor using biotinylated erythropoietin. Blood 76:697–705.
  • Yi, T., and J. N. Ihle. 1993. Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand. Mol. Cell. Biol. 13:3350–3358.
  • Yi, T., A. L. F. Mui, G. Krystal, and J. N. Ihle. 1993. Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor β chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol. Cell. Biol. 13:7577–7586.

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