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Originally published as MBC in Press, 10.1091/mbc.E06-06-0567 on November 22, 2006

Vol. 18, Issue 2, 501-511, February 2007

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Endogenous ARF6 Interacts with Rac1 upon Angiotensin II Stimulation to Regulate Membrane Ruffling and Cell MigrationFormula

Mathieu Cotton*, Pierre-Luc Boulay*, Tanguy Houndolo*, Nicolas Vitale{dagger}, Julie A. Pitcher{ddagger}, and Audrey Claing*

*Department of Pharmacology, School of Medicine, University of Montréal, Montréal, Canada H3C 3J7; {dagger}Institut des Neurosciences Cellulaires et Intégratives Unité Mixte de Recherche-7168 Centre National de la Recherche Scientifique/Université Louis Pasteur 67084, Strasbourg, France; and {ddagger}Medical Research Council Laboratory for Molecular and Cellular Biology and Department of Pharmacology, University College London, London, England, WC1E 6BT

Submitted June 30, 2006; Revised November 13, 2006; Accepted November 15, 2006
Monitoring Editor: Carole Parent

ARF6 and Rac1 are small GTPases known to regulate remodelling of the actin cytoskeleton. Here, we demonstrate that these monomeric G proteins are sequentially activated when HEK 293 cells expressing the angiotensin type 1 receptor (AT1R) are stimulated with angiotensin II (Ang II). After receptor activation, ARF6 and Rac1 transiently form a complex. Their association is, at least in part, direct and dependent on the nature of the nucleotide bound to both small G proteins. ARF6-GTP preferentially interacts with Rac1-GDP. AT1R expressing HEK293 cells ruffle, form membrane protrusions, and migrate in response to agonist treatment. ARF6, but not ARF1, depletion using small interfering RNAs recapitulates the ruffling and migratory phenotype observed after Ang II treatment. These results suggest that ARF6 depletion or Ang II treatment are functionally equivalent and point to a role for endogenous ARF6 as an inhibitor of Rac1 activity. Taken together, our findings reveal a novel function of endogenously expressed ARF6 and demonstrate that by interacting with Rac1, this small GTPase is a central regulator of the signaling pathways leading to actin remodeling.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-06-0567) on November 22, 2006.

Formula The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Audrey Claing (audrey.claing{at}umontreal.ca)

Abbreviations used: ARF, ADP-ribosylation factor; Ang II, angiotensin II; AT1R, angiotensin II type 1 receptor; GPCR, angiotensin II type 1 receptor; GEF, guanine-nucleotide exchange factor; GAP, GTPase-activating protein; PIX, p21-activated kinases [PAK]-interacting exchange factor; siRNA, small interfering RNA.




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