4
Views
6
CrossRef citations to date
0
Altmetric
Cell Growth and Development

Enhancement or Inhibition of Insulin Signaling by Insulin Receptor Substrate 1 Is Cell Context Dependent

&
Pages 4427-4434 | Received 03 Jan 1994, Accepted 13 Apr 1994, Published online: 30 Mar 2023

Refrences

  • Backer, J. M., M. G. MyersJr., S. E. Shoelson, D. J. Chin, X.-J. Sun, M. Miralpeix, P. Hu, B. Margolis, E. Y. Skolnik, J. Schles-singer, and M. F. White. 1992. Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J. 11: 3469–3479.
  • Backer, J. M., M. G. MyersJr., X.-J. Sun, D. J. Chin, S. E. Shoelson, M. Miralpeix, and M. F. White. 1993. Association of IRS-1 with the insulin receptor and the phosphatidylinositol 3′-kinase. J. Biol. Chem. 268: 8204–8212.
  • Baltensperger, K., L. M. Kozma, A. D. Cherniak, 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.
  • Blenis, J. 1993. Signal transduction via the MAP kinases: proceed at your own RSK. Proc. Natl. Acad. Sci. USA 90: 5889–5892.
  • Buday, L., and J. Downward. 1993. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell 73: 611–620.
  • Chardin, P., J. H. Camonis, N. W. Gale, L. Van Aelst, J. Schles-singer, M. H. Wigler, and D. Bar-Sagi. 1993. Human SOS1: a guanine nucleotide exchange factor for Ras that binds to GRB2. Science 260: 1338–1343.
  • Chuang, L.-E., M. G. MyersJr., J. M. Backer, S. E. Shoelson, M. F. White, M. J. Birnbaum, and C. R. Kahn. 1993. Insulin-stimulated oocyte maturation requires insulin receptor substrate 1 and interaction with the SH2 domains of phosphatidylinositol 3-kinase. Mol. Cell. Biol. 13: 6653–6660.
  • Chuang, L.-E., M. G. MyersJr., G. A. Siedner, M. J. Birnbaum, M. F. White, and C. R. Kahn. 1993. Insulin receptor substrate 1 mediates insulin and insulin-like growth factor I-stimulated maturation of Xenopus oocytes. Proc. Natl. Acad. Sci. USA 90: 5172–5175.
  • Davis, R. J. 1993. The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 268: 14553–14556.
  • de Vries-Smits, A. M. M., B. M. T. Burgering, S. J. Leevers, C. J. Marshall, and J. L. Bos. 1992. Involvement of p21ras in activation of extracellular signal-regulated kinase 2. Nature (London) 357: 602–604.
  • 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.
  • Frattali, A. L., J. L. Treadway, and J. E. Pessin. 1991. Evidence supporting a passive role for the insulin receptor transmembrane domain in insulin-dependent signal transduction. J. Biol. Chem. 266: 9829–9834.
  • Giorgetti, S., R. Balloti, A. Kowalski-Chauvel, S. Tartare, and E. Van Obberghen. 1993. The insulin and insulin-like growth factor-I receptor substrate IRS-1 associates with and activates phosphatidylinositol 3-kinase in vitro. J. Biol. Chem. 268: 7358–7364.
  • Goldfine, I. D. 1987. The insulin receptor; molecular biology and transmembrane signaling. Endocrinol. Rev. 8: 235–255.
  • Koide, H., T. Satoh, M. Nakafiiku, and Y. Kaziro. 1993. GTP-dependent association of Raf-1 with Ha-Ras: identification of Raf as a target downstream of Ras in mammalian cells. Proc. Natl. Acad. Sci. USA 90: 8683–8686.
  • Kuhne, M. R., T. Pawson, G. E. Lienhard, and G.-S. Feng. 1993. The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J. Biol. Chem. 268: 11479–11481.
  • Lavan, B. E., M. R. Kuhne, C. W. Garner, D. Anderson, M. Reedijk, T. Pawson, and G. E. Lienhard. 1992. The association of insulin-elicited phosphotyrosine proteins with src homology 2 domains. J. Biol. Chem. 267: 11631–11636.
  • Li, N., A. Batzer, R. Daly, V. Yajnik, E. Skolnik, P. Chardin, D. Bar-Sagi, B. Margolis, and J. Schlessinger. 1993. Guanine-nucle-otide-releasing factor hSOSl binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature (London) 363: 85–88.
  • 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.
  • MacDonald, S. G., C. M. Crews, L. Wu, J. Driller, R. Clark, R. L. Erikson, and F. McCormick. 1993. Reconstitution of the Raf-1-MEK-ERK signal transduction pathway in vitro. Mol. Cell. Biol. 13: 6615–6620.
  • Moodie, S. A., B. M. Willumsen, M. J. Weber, and A. Wolfman. 1993. Complexes of Ras GTP with Raf-1 and mitogen-activated protein kinase kinase. Science 260: 1658–1661.
  • Myers, M. G.Jr., J. M. Backer, X.-J. Sun, S. E. Shoelson, P. Hu, J. Schlessinger, M. Yoakim, B. Schaffhausen, and M. F. White. 1992. IRS-1 activates phosphatidylinositol 3′-kinase by associating with src homology 2 domains of p85. Proc. Natl. Acad. Sci. USA 89: 10350–10354.
  • Myers, M. G.Jr., and M. F. White. 1993. The new elements of insulin signaling: insulin receptor substrate-1 and proteins with SH2 domains. Diabetes 42: 643–650.
  • Ohmichi, M., K. Matuoka, T. Takenawa, and A. R. Saltiel. 1994. Growth factors differentially stimulate the phosphorylation of She proteins and their association with Grb2 in PC-12 pheochromocy-toma cells. J. Biol. Chem. 269: 1143–1148.
  • 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 a 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 She proteins. J. Biol. Chem. 268: 5748–5753.
  • Rice, K. M., G. E. Lienhard, and C. W. Garner. 1992. Regulation of the expression of ppl60, a putative insulin receptor signal protein, by insulin, dexamethasone, and l-methyl-3-isobutylxan-thine in 3T3-L1 adipocytes. J. Biol. Chem. 267: 10163–10167.
  • Rose, D. W., A. R. Saltiel, M. Majumdar, S. J. Decker, and J. M. Olefsky. 1994. Insulin receptor substrate 1 is required for insulinmediated mitogenic signal transduction. Proc. Natl. Acad. Sci. USA 91: 797–801.
  • 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 mSOSl. Nature (London) 363: 83–85.
  • 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.
  • 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. G. MyersJr., 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 She: implications for insulin control of ras signaling. EMBO J. 12: 1929–1936.
  • Stumpo, D. J., T. N. Stewart, M. Z. Gilman, and P. J. Blackshear. 1988. Identification of c-fos sequences involved in induction by insulin and phorbol esters. J. Biol. Chem. 263: 1611–1614.
  • Sun, X. J., D. L. Crimmins, M. G. MyersJr., M. Miralpeix, and M. F. White. 1993. Pleiotrophic insulin signals are engaged by multisite phosphorylation of IRS-1. Mol. Cell. Biol. 13: 7418–7428.
  • Sun, X.-J., M. Miralpeix, M. G. MyersJr., E. M. Glasheen, J. M. Backer, C. R. Kahn, and M. F. White. 1992. Expression and function of IRS-1 in insulin signal transmission. J. Biol. Chem. 267: 22662–22672.
  • Sun, X. J., P. Rothenberg, C. R. Kahn, J. M. Backer, E. Araki, P. A. Wilden, D. A. Cahill, B. J. Goldstein, and M. F. White. 1991. Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature (London) 352: 73–77.
  • Taylor, R. 1991. Insulin action. Clin. Endocrinol. 34: 159–171.
  • Taylor, S. I., A. Cama, D. Accili, F. Barbetti, M. J. Quon, M. De La Luz Sierra, Y. Suzuki, E. Roller, R. Levy-Toledano, E. Werthei-mer, V. Y. Moncada, H. Kadowaki, and T. Kadowaki. 1992. Mutations in the insulin receptor gene. Endocrinol. Rev. 13: 566–595.
  • 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 abundant Src homology/growth factor receptor-bound protein 2. J. Biol. Chem. 268: 11167–11171.
  • Van Aelst, L., M. Barr, S. Marcus, A. Polverino, and M. Wigler. 1993. Complex formation between RAS and RAF and other protein kinases. Proc. Natl. Acad. Sci. USA 90: 6213–6217.
  • van der Burg, B., R. P. de Groot, L. Isbrucker, W. Kruijer, and S. W. de Laat. 1990. Stimulation of TPA-responsive element activity by cooperative action of insulin and estrogen in human breast cancer cells. Mol. Endocrinol. 4: 1720–1726.
  • van der Burg, B., R. P. de Groot, L. Isbrucker, W. Kruijer, and S. W. de Laat. 1991. Oestrogen directly stimulates growth factor signal transduction pathways in human breast cancer cells. J. Steroid Biochem. Mol. Biol. 40: 215–221.
  • Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74: 205–214.
  • Wang, L.-M., A. D. Keegan, W. Li, G. E. Lienhard, S. Pacini, J. S. Gutkind, M. G. MyersJr., X.-J. Sun, M. F. White, S. A. Aaronson, W. E. Paul, and J. H. Pierce. 1993. Common elements in interleukin 4 and insulin signaling pathways in factor-dependent hematopoietic cells. Proc. Natl. Acad. Sci. USA 90: 4032–4036.
  • Wang, L.-M., M. G. MyersJr., X.-J. Sun, S. A. Aaronson, M. F. White, and J. H. Pierce. 1993. IRS-1: essential for insulin- and IL-4-stimulated mitogenesis in hematopoietic cells. Science 261: 1591–1594.
  • Waters, S. B., K. Yamauchi, and J. E. Pessin. 1993. Functional expression of insulin receptor substrate-1 is required for insulin-stimulated mitogenic signaling. J. Biol. Chem. 268: 22231–22234.
  • White, M. F., and C. R. Kahn. 1994. The insulin signaling system. J. Biol. Chem. 269: 1–4.
  • White, M. F., R. Maron, and C. R. Kahn. 1985. Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells. Nature (London) 318: 183–186.
  • Yamauchi, K., K. Holt, and J. E. Pessin. 1993. Phosphatidylinositol 3-kinase functions upstream of Ras and Raf in mediating insulin stimulation of c-fos transcription. J. Biol. Chem. 268: 14597–14600.
  • Yonezawa, K., H. Ueda, K. Hara, K. Nishida, A. Ando, A. Chavanieu, H. Matsuba, K. Shii, K. Yokono, F. Yasuhisa, B. Calas, F. Grigorescu, R. Dhand, I. Gout, M. Otsu, M. D. Water-field, and M. Kasuga. 1992. Insulin-dependent formation of a complex containing an 85-kDa subunit of phosphatidylinositol 3-kinase and tyrosine-phosphorylated insulin receptor substrate 1. J. Biol. Chem. 267: 25958–25966.
  • Zhang, X.-F., 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.

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.