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Originally published In Press as doi:10.1074/jbc.M111838200 on March 23, 2002

J. Biol. Chem., Vol. 277, Issue 22, 19439-19447, May 31, 2002
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Insulin Receptor Substrate 4 Associates with the Protein IRAS*

Hiroyuki SanoDagger , Simon C. H. LiuDagger , William S. Lane§, John E. Piletz, and Gustav E. LienhardDagger ||

From the Dagger  Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, the § Microchemistry and Proteomics Analysis Facility, Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, and the  Departments of Psychiatry, Pharmacology, and Physiology, University of Mississippi Medical Center, Jackson, Mississippi 39216

The insulin receptor substrates (IRSs) are key components in signaling from the insulin receptor, and consequently any proteins that interact with them are expected to participate in insulin signaling. In this study we have searched for proteins that interact with IRS-4 by identifying the proteins that coimmunoprecipitated with IRS-4 from human embryonic kidney 293 cells by microsequencing through mass spectrometry. A group of proteins was found. These included phosphatidylinositol 3-kinase, a protein previously identified as an IRS-4 interactor, and several proteins for which there was no previous evidence of IRS-4 association. One of these proteins, named IRAS, that had been found earlier in another context was examined in detail. The results from the overexpression of IRAS, where its amount was about the same as that of IRS-4, indicated that IRAS associated directly with IRS-4 and showed that the increased complexation of IRS-4 with IRAS did not alter the insulin-stimulated tyrosine phosphorylation of IRS-4 or the association of IRS-4 with phosphatidylinositol 3-kinase or Grb2. On the other hand, overexpression of IRAS enhanced IRS-4-dependent insulin stimulation of the extracellularly regulated kinase. The domains of IRAS and IRS-4 responsible for the association of these two proteins were identified, and it was shown that IRAS also associates with IRS-1, IRS-2, and IRS-3.

* This work was supported by National Institutes of Health Grants DK42816 (to G. E. L.) and MH49248 (to J. E. P.), a grant from the Uehara Memorial Foundation (to H. S.), and a grant from Solvay Pharmaceuticals Company (to J. E. P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Biochemistry, Vail Bldg., Dartmouth Medical School, Hanover, NH 03755. Tel.: 603-650-1627; Fax: 603-650-1128; E-mail: gustav.e.lienhard@dartmouth.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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