Cellular Compartmentalization in Insulin Action: Altered Signaling by a Lipid-Modified IRS-1

REFERENCES

• Bagrodia, S., Taylor, S. J., and Shalloway, D.. 1993. Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c- src in mitosis. Mol. Cell. Biol. 13:1464–1470
   PubMed Web of Science ®Google Scholar
• Bos, J. L.. 1995. A target for phosphoinositide 3-kinase: Akt/PKB. Trends Biochem. Sci. 20:441–442
   PubMedGoogle Scholar
• Burgering, B. M., and Coffer, P. J.. 1995. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599–602
   PubMed Web of Science ®Google Scholar
• Buss, J. E., Solski, P. A., Schaeffer, J. P., MacDonald, M. J., and Der, C. J.. 1989. Activation of the cellular proto-oncogene product p21Ras by addition of a myristylation signal. Science 241:1600–1603
   Google Scholar
• Cheatham, B., Vlahos, C. J., Cheatham, L., Wang, L., Blenis, J., and Kahn, C. R.. 1994. Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation. Mol. Cell. Biol. 14:4902–4911
   PubMed Web of Science ®Google Scholar
• Chung, J., Grammer, T. C., Lemon, K. P., Kazlauskas, A., and Blenis, J.. 1994. PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase. Nature 370:71–75
   PubMed Web of Science ®Google Scholar
• Clarke, S.. 1992. Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem. 61:355–386
   PubMed Web of Science ®Google Scholar
• Cross, F. R., Garber, E. A., Pellman, D., and Hanafusa, H.. 1984. A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol. Cell. Biol. 4:1834–1842
   PubMed Web of Science ®Google Scholar
• Delahaye, L., Mothe-Satney, I., Myers, M. G.Jr., White, M. F., and Van Obberghen, E.. 1998. Interaction of insulin receptor substrate-1 (IRS-1) with phosphatidylinositol 3-kinase: effect of substitution of serine for alanine in potential IRS-1 serine phosphorylation sites. Endocrinology 139:4911–4919
   PubMedGoogle Scholar
• Fantl, W. J., Escobedo, J. A., Martin, G. A., Turck, C. W., del Rosario, M., McCormick, F., and Williams, L. T.. 1992. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signalling pathways. Cell 69:413–423
   PubMedGoogle Scholar
• Fantl, W. J., Johnson, D. E., and Williams, L. T.. 1993. Signalling by receptor tyrosine kinases. Annu. Rev. Biochem. 62:453–481
   PubMed Web of Science ®Google Scholar
• Franke, T. F., Kaplan, D. R., and Cantley, L. C.. 1997. PI3K: downstream AKTion blocks apoptosis. Cell 88:436–437
   Google Scholar
• Franke, T. F., Kaplan, D. R., Cantley, L. C., and Toker, A.. 1997. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275:665–668
   PubMed Web of Science ®Google Scholar
• Franke, T. F., Yang, S., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., and Tsichlis, P. N.. 1995. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81:727–736
   PubMed Web of Science ®Google Scholar
• Garcia, P., Gupta, R., Shah, S., Morris, A. J., Rudge, S. A., Scarlata, S., Petrova, V., McLaughlin, S., and Rebecchi, M. J.. 1995. The pleckstrin homology domain of phospholipase C-delta 1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes. Biochemistry 34:16228–16234
   PubMedGoogle Scholar
• Grammer, T. C., and Blenis, J.. 1996. The serine protease inhibitors, tosylphenylaline chloromethyl ketone and tosyllysine chloromethyl ketone, potently inhibit pp70s6k activation. J. Biol. Chem. 271:23650–23652
   PubMedGoogle Scholar
• Gustafson, T. A., He, W., Craparo, A., Schaub, C. D., and O'Neill, T. J.. 1995. Phosphotyrosine-dependent interaction of Shc and IRS-1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol. 15:2500–2508
   PubMed Web of Science ®Google Scholar
• Harlan, J. E., Hajduk, P. J., Yoon, H. S., and Fesik, S. W.. 1994. Pleckstrin homology domains bind to phosphatidylinositol 4,5-bisphosphate. Nature 371:168–170
   PubMed Web of Science ®Google Scholar
• Hotamisligil, G. S., Peraldi, P., Budvari, A., Ellis, R. W., White, M. F., and Spiegelman, B. M.. 1996. IRS-1 mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance. Science 271:665–668
   PubMed Web of Science ®Google Scholar
• Inoue, G., Cheatham, B., Emkey, R., and Kahn, C. R.. 1998. Dynamics of insulin signaling in 3T3-L1 adipocytes: differential compartmentalization and trafficking of insulin receptor substrate (IRS)-1 and IRS-2. J. Biol. Chem. 273:11548–11555
   PubMed Web of Science ®Google Scholar
• Kazlauskas, A., and Cooper, J. A.. 1989. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins. Cell 58:1121–1133
   PubMedGoogle Scholar
• Kazlauskas, A., and Cooper, J. A.. 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
• Klarlund, J. K., Guilherme, A., Holik, J. J., Virbasius, J. V., Chawla, A., and Czech, M. P.. 1997. Signaling by phosphoinositide-3,4,5-triphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275:1927–1930
   PubMed Web of Science ®Google Scholar
• Klippel, A., Kavanaugh, W. M., Pot, D., and Williams, L. T.. 1997. A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol. Cell. Biol. 17:338–344
   PubMed Web of Science ®Google Scholar
• Klippel, A., Reinhard, C., Kavanaugh, W. M., Apell, G., Escobedo, M.-A., and Williams, L. T.. 1996. Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways. Mol. Cell. Biol. 16:4117–4127
   PubMed Web of Science ®Google Scholar
• Koch, C. A., Anderson, D. J., Moran, M. F., Ellis, C. A., and Pawson, T.. 1991. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252:668–674
   PubMed Web of Science ®Google Scholar
• Kohn, A. D., Barthel, A., Kovacina, K. S., Boge, A., Wallach, B., Summers, S. A., Birnbaum, M. J., Scott, P. H., Lawrence, J. C. J., and Roth, R. A.. 1998. Construction and characterization of a conditionally active version of the serine/threonine kinase Akt. J. Biol. Chem. 273:11937–11943
   PubMedGoogle Scholar
• Kohn, A. D., Summers, S. A., Birnbaum, M. J., and Roth, R. A.. 1996. Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J. Biol. Chem. 271:31372–31378
   PubMed Web of Science ®Google Scholar
• Martin, S. S., Haruta, T., Morris, A. J., Klippel, A., Williams, L. T., and Olefsky, J. M.. 1996. Activated phosphatidylinositol 3-kinase in sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes. J. Biol. Chem. 271:17605–17608
   PubMed Web of Science ®Google Scholar
• Morris, A. J., Martin, S. S., Haruta, T., Nelson, J. G., Vollenweider, P., Gustafson, T. A., Mueckler, M., Rose, D. W., and Olefsky, J. M.. 1996. Evidence for an insulin receptor substrate 1 independent insulin signaling pathway that mediates insulin-responsive glucose transporter (GLUT4) translocation. Proc. Natl. Acad. Sci. USA 93:8401–8406
   PubMedGoogle Scholar
• Mothe, I., and Van Obberghen, E.. 1996. Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action. J. Biol. Chem. 271:11222–11227
   PubMed Web of Science ®Google Scholar
• Myers, M. G.Jr., Grammer, T. C., Brooks, J., Glasheen, E. M., Wang, L. M., Sun, X. J., Blenis, J., Pierce, J. H., and White, M. F.. 1995. The pleckstrin homology domain in IRS-1 sensitizes insulin signaling. J. Biol. Chem. 270:11715–11718
   PubMed Web of Science ®Google Scholar
• Myers, M. G.Jr., Grammer, T. C., Wang, L. M., Sun, X. J., Pierce, J. H., Blenis, J., and White, M. F.. 1994. IRS-1 mediates PI 3′-kinase and p70s6k signaling during insulin, IGF-1 and IL-4 stimulation. J. Biol. Chem. 269:28783–28789
   PubMed Web of Science ®Google Scholar
• Myers, M. G.Jr., Wang, L.-M., Sun, X. J., Zhang, Y., Yenush, L., Schlessinger, J., Pierce, J. H., and White, M. F.. 1994. The role of IRS-1–GRB-2 complexes in insulin signaling. Mol. Cell. Biol. 14:3577–3587
   PubMed Web of Science ®Google Scholar
• Myers, M. G.Jr., and White, M. F.. 1996. Insulin signal transduction and the IRS proteins. Annu. Rev. Pharmacol. Toxicol. 36:615–658
   PubMed Web of Science ®Google Scholar
• Myers, M. G.Jr., Zhang, Y., Aldaz, G. A. I., Grammer, T. C., Glasheen, E. M., Yenush, L., Wang, L. M., Sun, X. J., Blenis, J., Pierce, J. H., and White, M. F.. 1996. YMXM motifs and signaling by an insulin receptor substrate 1 molecule without tyrosine phosphorylation sites. Mol. Cell. Biol. 16:4147–4155
   PubMed Web of Science ®Google Scholar
• Natali, A., Bonadonna, R., Santoro, D., Galvan, A. Q., Baldi, S., Frascerra, S., Palombo, C., Ghione, S., and Ferrannini, E.. 1994. Insulin resistance and vasodilation in essential hypertension: studies with adenosine. J. Clin. Investig. 94:1570–1576
   PubMed Web of Science ®Google Scholar
• O'Neill, T. J., Craparo, A., and Gustafson, T. A.. 1994. Characterization of an interaction between insulin receptor substrate 1 and the insulin receptor by using the two-hybrid system. Mol. Cell. Biol. 14:6433–6442
   PubMedGoogle Scholar
• Paz, K., Hemi, R., LeRoith, D., Karasik, A., Elhanany, E., Kanety, H., and Zick, Y.. 1997. A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. J. Biol. Chem. 272:29911–29918
   PubMed Web of Science ®Google Scholar
• Peraldi, P., Hotamisligil, G. S., Buurman, W. A., White, M. F., and Spiegelman, B. M.. 1996. Tumor necrosis factor (TNF)-α inhibits insulin signaling through stimulation of the p55 TNF receptor and activation of sphingomyelinase. J. Biol. Chem. 271:13018–13022
   PubMed Web of Science ®Google Scholar
• Porfiri, E., Evans, T., Chardin, P., and Hancock, J. F.. 1994. Prenylation of Ras proteins is required for efficient hSOS1-promoted guanine nucleotide exchange. J. Biol. Chem. 269:22672–22677
   PubMedGoogle Scholar
• Ray, P., Higgins, K. M., Tan, J. C., Chu, T. Y., Yee, N. S., Nguyen, H., Lacy, E., and Besmer, P.. 1991. Ectopic expression of a c-kitW42 minigene in transgenic mice: recapitulation of W phenotypes and evidence for c-kit function in melanoblast progenitors. Genes Dev. 5:2265–2273
   PubMedGoogle Scholar
• Resh, M. D.. 1994. Myristylation and palmitylation of the Src family members: the fats of the matter. Cell 76:411–413
   PubMed Web of Science ®Google Scholar
• Rordorf-Nikolic, T., Van Horn, D. J., Chen, D., White, M. F., and Backer, J. M.. 1995. Regulation of phosphatidylinositol 3-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85 kDa regulatory subunit. J. Biol. Chem. 270:3662–3666
   PubMed Web of Science ®Google Scholar
• Ruderman, N., Kapeller, R., White, M. F., and Cantley, L. C.. 1990. Activation of phosphatidylinositol-3-kinase by insulin. Proc. Natl. Acad. Sci. USA 87:1411–1415
   PubMed Web of Science ®Google Scholar
• Salim, K., Bottomley, M. J., Querfurth, E., Zvelebil, M. J., Gout, I., Scaife, R., Margolis, R. L., Gigg, R., Smith, C. I. E., Driscoll, P. C., Waterfield, M. D., and Panayotou, G.. 1996. Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. EMBO J. 15:6241–6250
   PubMed Web of Science ®Google Scholar
• Sawyer, R. C., Rettenmier, C. W., and Hanafusa, H.. 1979. Formation of Rous-associated virus 60: origin of the polymerase gene. J. Virol. 29:856–862
   PubMedGoogle Scholar
• Sharma, P. M., Egawa, K., Huang, Y., Martin, J. L., Huvar, I., Boss, G. R., and Olefsky, J. M.. 1998. Inhibition of phosphatidylinositol 3-kinase activity by adenovirus-mediated gene transfer and its effect on insulin action. J. Biol. Chem. 273:18528–18537
   PubMedGoogle Scholar
• Stokoe, D., Stephens, L. R., Copeland, T., Gaffney, P. R., Reese, C. B., Painter, G. F., Holmes, A. B., McCormick, F., and Hawkins, P. T.. 1997. Dual role of phosphatidylinositol-3,4,5-triphosphate in the activation of protein kinase B. Science 277:567–570
   PubMed Web of Science ®Google Scholar
• Sun, X. J., Miralpeix, M., Myers, M. G.Jr., Glasheen, E. M., Backer, J. M., Kahn, C. R., and White, M. F.. 1992. The expression and function of IRS-1 in insulin signal transmission. J. Biol. Chem. 267:22662–22672
   PubMed Web of Science ®Google Scholar
• Sun, X. J., Rothenberg, P. L., Kahn, C. R., Backer, J. M., Araki, E., Wilden, P. A., Cahill, D. A., Goldstein, B. J., and White, M. F.. 1991. The structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature 352:73–77
   PubMed Web of Science ®Google Scholar
• Takayama, S., White, M. F., Lauris, V., and Kahn, C. R.. 1984. Phorbol esters modulate insulin receptor phosphorylation and insulin action in hepatoma cells. Proc. Natl. Acad. Sci. USA 81:7797–7801
   PubMedGoogle Scholar
• Tanti, J. F., Gremeaux, T., Van Obberghen, E., and Le Marchand-Brustel, Y.. 1994. Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling. J. Biol. Chem. 269:6051–6057
   PubMed Web of Science ®Google Scholar
• Tavare, J. M., Zhang, B., Ellis, L., and Roth, R. A.. 1991. Insulin-stimulated serine and threonine phosphorylation of the human insulin receptor. An assessment of the role of serines 1305/1306 and threonine 1348 by their replacement with neutral or negatively charged amino acids. J. Biol. Chem. 266:21804–21809
   PubMedGoogle Scholar
• Ullrich, A., and Schlessinger, J.. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell 61:203–212
   PubMed Web of Science ®Google Scholar
• Wang, C. C., Sonne, O., Hedo, J. A., Cushman, S. W., and Simpson, I. A.. 1983. Insulin-induced internalization of the insulin receptor in the isolated rat adipose cell. Detection of the internalized 130-kilodalton receptor subunit using a photoaffinity 125I insulin. J. Biol. Chem. 258:5129–5134
   PubMedGoogle Scholar
• Wang, L. M., Myers, M. G.Jr., Sun, X. J., Aaronson, S. A., White, M. F., and Pierce, J. H.. 1993. IRS-1: essential for insulin and IL-4-stimulated mitogenesis in hematopoietic cells. Science 261:1591–1594
   PubMedGoogle Scholar
• White, M. F.. 1991. Structure and function of tyrosine kinase receptors. J. Bioenerg. Biomembr. 23:63–82
   PubMed Web of Science ®Google Scholar
• Yenush, L., Fernandez, R., Myers, M. G.Jr., Grammer, T. C., Sun, X. J., Blenis, J., Pierce, J. H., Schlessinger, J., and White, M. F.. 1996. The Drosophila insulin receptor activates multiple signaling pathways but requires insulin receptor substrate proteins for DNA synthesis. Mol. Cell. Biol. 16:2509–2517
   PubMed Web of Science ®Google Scholar
• Yenush, L., Makati, K. J., Smith-Hall, J., Ishibashi, O., Myers, M. G.Jr., and White, M. F.. 1996. The pleckstrin homology domain is the principle link between the insulin receptor and IRS-1. J. Biol. Chem. 271:24300–24306
   PubMed Web of Science ®Google Scholar
• Yenush, L., Zanella, C., Uchida, T., Bernal, D., and White, M. F.. 1998. The pleckstrin homology and phosphotyrosine binding domains of insulin receptor substrate 1 mediate inhibition of apoptosis by insulin. Mol. Cell. Biol. 18:6784–6794
   PubMed Web of Science ®Google Scholar
• Zhang, F. L., and Casey, P. J.. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65:241–269
   PubMed Web of Science ®Google Scholar
• Zheng, Y., Zangrilli, D., Cerione, R. A., and Eva, A.. 1996. The pleckstrin homology domain mediates transformation by oncogenic dbl through specific intracellular targeting. J. Biol. Chem. 271:19017–19020
   PubMed Web of Science ®Google Scholar