The IRS‐signalling system during insulin and cytokine action

BioEssays - Tập 19 Số 6 - Trang 491-500 - 1997
Lynne Yenush1, Morris F. White2
1Research Division, Joslin Diabetes Center, Boston, MA, USA.
2Research Division, Joslin Diabetes Center and the Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, MA 02215, USA

Tóm tắt

AbstractThe discovery of the first intracellular substrate for insulin, IRS‐1, redirected the field of diabetes research and has led to many important advances in our understanding of insulin action. Detailed analysis of IRS‐1 demonstrates structure/function relationships for this modular docking molecule, including mechanisms of substrate recognition and signal propagation. Recent work has also identified other structurally similar molecules, including IRS‐2, the Drosophila protein, DOS, and the Grb2‐binding protein, Gab1, suggesting that this intracellular signalling strategy is conserved evolutionarily and is utilized by an expanding number of receptor systems. In fact, IRS‐1 itself has been shown to be important in other growth factor and cytokine signalling systems, including growth hormone and several interleukins. Analysis of mice lacking IRS‐1 confirms an important physiological role for this protein in glucose metabolism and general cell growth in the intact animal. Disregulation of the signalling pathways integrated by the IRS proteins may contribute to the pathophysiology of non‐insulin‐dependent diabetes mellitus or other diseases.

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Tài liệu tham khảo

10.1002/mrd.1080350406

10.1016/S0092-8674(05)80085-6

10.1038/377173a0

10.1038/352073a0

Johnson J., 1995, Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of insulin receptor substrates 1 and 2 in T cells, J. Biol. Chem., 270, 1

10.1074/jbc.270.24.14685

10.1074/jbc.270.27.15938

10.1074/jbc.271.1.278

10.1038/372746a0

10.1016/S0092-8674(88)80008-4

10.1021/bi00152a046

10.1073/pnas.90.9.4032

10.1038/372186a0

10.1074/jbc.270.11.5698

10.2337/diabetes.42.7.1041

10.1210/mend.11.2.9885

10.1016/S0092-8674(00)81273-8

10.1038/379560a0

10.1128/MCB.14.6.3577

10.1126/science.8316835

10.1074/jbc.271.18.10583

10.1016/S0021-9258(19)50220-4

Beitner‐Johnson D., 1996, The proto‐oncogene product c‐Crk associates with insulin receptor substrate‐1 and 4PS, J. Biol. Chem., 271, 287, 10.1074/jbc.271.16.9287

10.1073/pnas.90.24.11713

10.1074/jbc.271.17.10200

10.1128/MCB.14.10.6433

10.1074/jbc.270.46.27407

10.1016/S0092-8674(00)81022-3

10.1016/0092-8674(94)90356-5

10.1016/S0092-8674(00)81236-2

10.1074/jbc.271.39.24300

Pitcher J. A., 1995, Pleckstrin homology domain‐mediated membrane assocaition and activation of the beta‐adrenergic receptor kinase requires coordinate interaction with G‐beta/gamma subunits and lipid, J. Biol. Chem., 270, 11707, 10.1074/jbc.270.20.11707

10.1074/jbc.271.32.19017

10.1074/jbc.271.11.5980

10.1074/jbc.271.20.11641

10.1038/384173a0

10.1016/S0092-8674(00)81274-X

10.1016/0968-0004(94)90140-6

10.1128/MCB.16.5.2509

10.1126/science.7527156

10.1128/MCB.15.8.4232

Backer J. M., 1992, Insulin stimulation of phosphatidylinositol 3‐kinase activity maps to insulin receptor regions required for endogenous substrate phosphorylation, J. Biol. Chem., 267, 1367, 10.1016/S0021-9258(18)48440-2

10.1074/jbc.270.8.3662

Lam K., 1994, The phosphatidylinositol 3‐kinase serine kinase phosphorylates IRS‐1 stimulation by insulin and inhibition by wortmannin, J. Biol. Chem., 269, 20648, 10.1016/S0021-9258(17)32042-2

10.1128/MCB.16.8.4147

10.1016/0092-8674(95)90534-0

Diaz‐Meco M. T., 1994, Evidence for the in vitro and in vivo interaction of Ras with protein kinase C zeta, J. Biol. Chem., 269, 31706, 10.1016/S0021-9258(18)31753-8

10.1038/379277a0

10.1074/jbc.271.21.12595

10.1002/j.1460-2075.1993.tb05842.x

10.1128/MCB.16.6.3074

10.1038/373536a0

10.1074/jbc.270.8.3471

10.1074/jbc.270.35.20497

Wang L. M., 1995, The insulin related substrate‐1‐related 4PS substrate but not the interleukin‐2R gamma chain is involved in interleukin‐13 mediated signal transduction, Blood, 86, 4218, 10.1182/blood.V86.11.4218.bloodjournal86114218

10.1042/bj3100741

10.1073/pnas.93.22.12490

Tranisijevik M., 1993, Phosphorylation of the insulin receptor substrate IRS‐1 by casein kinase II, J. Biol. Chem., 268, 18157, 10.1016/S0021-9258(17)46824-4

10.1016/S0021-9258(17)37568-3

10.1074/jbc.271.19.11222

10.1126/science.271.5249.665

10.1098/rstb.1996.0011

10.2337/diab.43.11.1271

10.1172/JCI117936

10.1038/scientificamerican0192-86

Fingar D. C., 1994, A role for raf‐1 in the divergent signaling pathways mediating insulin‐stimulated glucose transport, J. Biol. Chem., 269, 10127, 10.1016/S0021-9258(17)36999-5

10.1073/pnas.91.16.7415

Okada T., 1994, Essential role of phsophatidylinositol 3‐kinase in insulin‐induced glucose transport and antilipolysis in rat adipocytes – Studies with a selective inhibitor wortmannin, J. Biol. Chem., 269, 3568, 10.1016/S0021-9258(17)41901-6

10.1038/378785a0

10.1038/348302a0

10.1128/MCB.15.9.4711

10.1128/MCB.16.6.2857

10.1016/S0092-8674(00)81896-6

10.1074/jbc.270.42.24670

10.1172/JCI118705

10.1016/S0140-6736(95)92779-4

10.1016/S0092-8674(05)80084-4

10.1038/ng0196-106

10.1006/excr.1995.1168

Sell C., 1995, Insulin‐like growth factor I (IGF‐I) and the IGF‐I receptor prevent etoposide‐induced apoptosis, Cancer Res., 55, 303

D'Ambrosio C., 1995, Transforming potential of the insulin receptor substrate 1, Cell Growth Differ., 6, 557

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BioEssays

Tập 19 Số 6

491-500

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