Article abstract
Nature Cell Biology 7, 353 - 364 (2005)
Published online: 27 March 2005 | doi:10.1038/ncb1244
Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics
Thierry Dubois1, Olivia Paléotti2, Alexander A. Mironov, Jr3, Vincent Fraisier4, Theresia E. B. Stradal5, Maria Antonietta De Matteis3, Michel Franco2 & Philippe Chavrier1
Abstract
The small GTP-binding ADP-ribosylation factor 1 (ARF1) acts as a master regulator of Golgi structure and function through the recruitment and activation of various downstream effectors. It has been proposed that members of the Rho family of small GTPases also control Golgi function in coordination with ARF1, possibly through the regulation of Arp2/3 complex and actin polymerization on Golgi membranes. Here, we identify ARHGAP10 — a novel Rho GTPase-activating protein (Rho-GAP) that is recruited to Golgi membranes through binding to GTP-ARF1. We show that ARHGAP10 functions preferentially as a GAP for Cdc42 and regulates the Arp2/3 complex and F-actin dynamics at the Golgi through the control of Cdc42 activity. Our results establish a role for ARHGAP10 in Golgi structure and function at the crossroads between ARF1 and Cdc42 signalling pathways.
- Membrane and Cytoskeleton Dynamics Group, Institut Curie, CNRS-UMR144, 75248 Paris, France.
- Institut de Pharmacologie Moléculaire et Cellulaire, CNRS-UMR 6097, F-06560 Valbonne, France.
- Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (CH), Italy.
- Digital Imaging Platform, Institut Curie, CNRS-UMR144, 75248 Paris, France.
- German Research Centre for Biotechnology (GBF), Department of Cell Biology, Mascheroder Weg 1, D-38124 Braunschweig, Germany.
Correspondence to: Philippe Chavrier1 e-mail: philippe.chavrier@curie.fr
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