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First published online 26 April 2005
doi: 10.1242/jcs.02351

Journal of Cell Science 118, 2201-2210 (2005)
Published by The Company of Biologists 2005
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Research Article

ARF6 GTPase controls bacterial invasion by actin remodelling

María Eugenia Balañá1, Florence Niedergang2,*, Agathe Subtil1,*, Andrés Alcover1, Philippe Chavrier2 and Alice Dautry-Varsat1,{ddagger}

1 Unité de Biologie des Interactions Cellulaires, Institut Pasteur, CNRS URA 2582, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France
2 CNRS UMR 144 Institut Curie, 12 rue Lhomond, 75005 Paris, France

{ddagger} Author for correspondence (e-mail: adautry{at}pasteur.fr)

Accepted 24 February 2005

The obligate intracellular bacterium Chlamydia penetrates the host epithelial cell by inducing cytoskeleton and membrane rearrangements reminiscent of phagocytosis. Here we report that Chlamydia induces a sharp and transient activation of the endogenous small GTP-binding protein ARF6, which is required for efficient uptake. We also show that a downstream effector of ARF6, phosphatidylinositol 4-phosphate 5-kinase and its product, phosphatidylinositol 4,5-bisphosphate were instrumental for bacterial entry. By contrast, ARF6 activation of phospholipase D was not required for Chlamydia uptake. ARF6 activation was necessary for extensive actin reorganization at the invasion sites. Remarkably, these signalling players gathered with F-actin in a highly organized three-dimensional concentric calyx-like protrusion around invasive bacteria. These results indicate that ARF6, which controls membrane delivery during phagocytosis of red blood cells in macrophages, has a different role in the entry of this small bacterium, controlling cytoskeletal reorganization.

Key words: Chlamydia, Phagocytosis, Intracellular bacteria, PIP 5-kinase, PIP2




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