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Papers In Press, published online ahead of print December 16, 2004
J. Biol. Chem, 10.1074/jbc.M412924200
Submitted on November 15, 2004
Revised on December 14, 2004
Accepted on December 16, 2004

beta -arrestin 1 and G(subalpha 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

Medicine Dept., HHMI/Duke University Medical Center, Durham, NC 27710

Corresponding Author: lefko001{at}receptor-biol.duke.edu

beta -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 (7TMs). Recently, beta -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 beta -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 (AT1AR). This AT1AR directed RhoA activation and stress fiber formation also requires the activation of the heterotrimeric G protein Galphaq/11}. While neither beta -arrestin 1 nor G {alphaq/11} activation alone is sufficient to robustly activate RhoA, the concurrent recruitment of beta -arrestin 1 and activation of G {alphaq/11} leads to full activation of RhoA and to the subsequent formation of stress fibers.


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