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A more recent version of this article appeared on February 1, 2004
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Submitted on June 16, 2003
Revised on September 16, 2003
Accepted on September 30, 2003
1 Centre National de la Recherche Scientifique Unité Propre de Recherche 2356, IFR 37, 5 rue Blaise Pascal, 67084 Strasbourg Cedex, France
2 Cancer Research UK, Lincoln’s Inn Fields laboratories, 44 Lincoln’s Inn Fields, London WC2A 3PX, England
* Corresponding author. E-mail address: gasman{at}neurochem.u-strasbg.fr.
In neuroendocrine cells, actin reorganisation is a prerequisite for regulated exocytosis. Small GTPases Rho proteins represent potential candidates coupling actin dynamics to membrane trafficking events. We previously reported that Cdc42 plays an active role in regulated exocytosis in chromaffin cells. The aim of the present work was to dissect the molecular effector pathway integrating Cdc42 to the actin architecture required for the secretory reaction in neuroendocrine cells. Using PC12 cells as a secretory model, we show that Cdc42 is activated at the plasma membrane during exocytosis. Expression of the constitutively active Cdc42L61 mutant increases the secretory response, recruits N-WASP and enhances actin polymerization in the subplasmalemmal region. Moreover, expression of N-WASP stimulates secretion by a mechanism dependent on its ability to induce actin polymerization at the cell periphery. Finally, we observed that Arp2/3 is associated with secretory granules and that it accompanies granules to the docking sites at the plasma membrane upon cell activation.
Our results demonstrate for the first time that secretagogue-evoked stimulation induces the sequential ordering of Cdc42, N-WASP and Arp2/3 at the interface between granules and the plasma membrane, thereby providing an actin structure that makes the exocytotic machinery more efficient.
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