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J. Biol. Chem., Vol. 281, Issue 18, 12352-12361, May 5, 2006

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Role of the Arf6 GDP/GTP Cycle and Arf6 GTPase-activating Proteins in Actin Remodeling and Intracellular Transport^*

From the Institut de Pharmacologie Moléculaire et Cellulaire, CNRS UMR 6097, 660, route des Lucioles, 06560 Valbonne, France

We have analyzed both biochemically and functionally a series of Arf6 mutants, providing new insights into the molecular mode of action of the small G protein Arf6. First, by comparing a fast-cycling mutant (Arf6(T157N)) and a GTPase-deficient mutant (Arf6(Q67L)), we established the necessity for completion of the Arf6 GDP/GTP cycle for recycling of major histocompatibility complex molecules to the plasma membrane. Second, we found that aluminum fluoride (AlF), known for inducing membrane protrusion in cells expressing exogenous wild-type Arf6, stabilized a functional wild-type Arf6·AlF_x · GTPase-activating protein (GAP) complex in vitro and in vivo. We also found that the tandem mutation Q37E/S38I prevented the binding of two Arf GAPs, but not the effector ARHGAP10, and blocked the formation of membrane protrusion and actin reorganization. Together, our results with AlF_x and Arf6(Q37E/S38I) demonstrate the critical role of the Arf6 GAPs as effectors for Arf6-regulated actin cytoskeleton remodeling. Finally, competition experiments conducted in vivo suggest the existence of a membrane receptor for GDP-bound Arf6.

Received for publication, February 2, 2006 , and in revised form, March 2, 2006.

^* This work was supported in part by a grant from the Association pour la Recherche sur le Cancer (to F. L. and M. F.) and by Cancéropole Provence-Alp-Côte d'Azur Projet AxeIII (to P. C.). 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.

¹ Recipient of a fellowship from the Ministère de la Recherche et de l'Education.

² To whom correspondence should be addressed. Tel.: 33-4-9395-7770; Fax: 33-4-9395-7710; E-mail: luton{at}ipmc.cnrs.fr.

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