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J. Biol. Chem., Vol. 280, Issue 9, 8041-8050, March 4, 2005

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-Arrestin 1 and G_q/11 Coordinately Activate RhoA and Stress Fiber Formation following Receptor Stimulation^*

William G. Barnes, Eric Reiter, Jonathan D. Violin, Xiu-Rong Ren, Graeme Milligan¶, and Robert J. Lefkowitz, An investigator with the Howard Hughes Medical Institute||**

From the ^||Howard Hughes Medical Institute and Departments of Biochemistry and Medicine, Duke University Medical Center, Durham, North Carolina 27710 and Institut National De La Recherche Agronomique and ^¶Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G128QQ, Scotland, United Kingdom

-Arrestins were initially shown, in conjunction with G protein-coupled receptor kinases, to be involved in the desensitization and internalization of activated seven-transmembrane receptors. Recently, -arrestin 2 has been shown to act as a signal mediator in mitogen-activated protein kinase cascades and to play a positive regulatory role in chemotaxis. We now show that -arrestin 1 is required to activate the small GTPase RhoA leading to the re-organization of stress fibers following the activation of the angiotensin II type 1A receptor. This angiotensin II type 1A receptor-directed RhoA activation and stress fiber formation also require the activation of the heterotrimeric G protein G_q/11. Whereas neither -arrestin 1 nor G_q/11 activation alone is sufficient to robustly activate RhoA, the concurrent recruitment of -arrestin 1 and activation of G_q/11 leads to full activation of RhoA and to the subsequent formation of stress fibers.

Received for publication, November 15, 2004 , and in revised form, December 14, 2004.

^* This work was supported by National Institutes of Health Grants HL 16037 and HL 70631 (to R. J. L.) supported this work. The costs of publication of this article were defrayed in part by the payment of page charges. This 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: Depts. of Medicine and Biochemistry, Howard Hughes Medical Institute, Box 3821, Duke University Medical Center, Durham, NC 27710. Tel.: 919-684-2974; Fax: 919-684-8875; E-mail: lefko001{at}receptor-biol.duke.edu.

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