Work

β-Arrestin 1 and Gαq/11 Coordinately Activate RhoA and Stress Fiber Formation following Receptor Stimulation

Year: 2004

Type: article

Abstract: 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. 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. This angiotensin II type 1A receptor-directed RhoA activation and stress fiber formation also require the activation of the heterotrimeric G protein G(alphaq/11). Whereas 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.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.m412924200

Authors: William G. Barnes, Eric Reiter, Jonathan D. Violin, Xiu-Rong Ren, Graeme Milligan, Robert J. Lefkowitz

Institutions: Duke Medical Center, Institut National de la Recherche Agronomique, University of Glasgow, Howard Hughes Medical Institute

Language: English

Topic: Receptor Mechanisms and Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430