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Originally published In Press as doi:10.1074/jbc.M201758200 on April 18, 2002

J. Biol. Chem., Vol. 277, Issue 25, 22581-22589, June 21, 2002
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RACK1 Is an Insulin-like Growth Factor 1 (IGF-1) Receptor-interacting Protein That Can Regulate IGF-1-mediated Akt Activation and Protection from Cell Death*

Patrick A. KielyDagger , Anagha Sant§, and Rosemary O'ConnorDagger

From the Dagger  Cell Biology Laboratory, Department of Biochemistry and Bioscience Institute, National University of Ireland, Lee Maltings Cork, Ireland and § ImmunoGen, Inc., Cambridge, Massachusetts 02139

The insulin receptor and insulin-like growth factor 1 receptor (IGF-1R), activated by their ligands, control metabolism, cell survival, and proliferation. Although the signaling pathways activated by these receptors are well characterized, regulation of their activity is poorly understood. To identify regulatory proteins we undertook a two-hybrid screen using the IGF-1R beta -chain as bait. This screen identified Receptor for Activated C Kinases (RACK1) as an IGF-1R-interacting protein. RACK1 also interacted with the IGF-1R in fibroblasts and MCF-7 cells and with endogenous insulin receptor in COS cells. Interaction with the IGF-1R did not require tyrosine kinase activity or receptor autophosphorylation but did require serine 1248 in the C terminus. Overexpression of RACK1 in either R+ fibroblasts or MCF-7 cells inhibited IGF-1-induced phosphorylation of Akt, whereas it enhanced phosphorylation of Erks and Jnks. Src, the p85 subunit of phosphatidylinositol 3-kinase, and SHP-2 were all associated with RACK1 in these cells. Interestingly, the proliferation of MCF-7 cells was enhanced by overexpression of RACK1, whereas IGF-1-mediated protection from etoposide killing was greatly reduced. Altogether the data indicate that RACK1 is an IGF-1R-interacting protein that can modulate receptor signaling and suggest that RACK1 has a particular role in regulating Akt activation and cell survival.

* This work was supported by research grants from Enterprise Ireland and the Irish Cancer Society.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. Tel.: 353-21- 4904212; Fax: 353-21-4904259; E-mail: r.oconnor@ucc.ie.

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