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Am J Physiol Cell Physiol 289: C819-C825, 2005. First published May 18, 2005; doi:10.1152/ajpcell.00587.2004
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RECEPTORS AND SIGNAL TRANSDUCTION

Integrin {alpha}IIb{beta}3 signals lead cofilin to accelerate platelet actin dynamics

Hervé Falet,1 Gregory Chang,1,2 Brigitte Brohard-Bohn,2 Francine Rendu,2,3 and John H. Hartwig1

1Division of Hematology, Brigham and Women’s Hospital, Department of Medicine, Harvard Medical School, Boston, Massachusetts; and 2Institut National de la Santé et de la Recherche Médicale Unité 428, Unité de Formation et de Recherche des Sciences Pharmaceutiques et Biologiques, Université René Descartes, Paris, and 3Centre National de la Recherche Scientifique Unité Mixte de Recherche 7131, Hôpital Broussais, Paris, France

Submitted 1 December 2004 ; accepted in final form 10 May 2005

Cofilin, in its Ser3 dephosphorylated form, accelerates actin filament turnover in cells. We report here the role of cofilin in platelet actin assembly. Cofilin is primarily phosphorylated in the resting platelet as evidenced by a specific antibody directed against its Ser3 phosphorylated form. After stimulation with thrombin under nonstirring conditions, cofilin is reversibly dephosphorylated and transiently incorporates into the actin cytoskeleton. Its dephosphorylation is maximal 1–2 min after platelet stimulation, shortly after the peak of actin assembly occurs. Cofilin rephosphorylation begins 2 min after activation and exceeds resting levels by 5–10 min. Cofilin is dephosphorylated with identical kinetics but fails to become rephosphorylated when platelets are stimulated under stirring conditions. Cofilin is normally rephosphorylated when platelets are stimulated in the presence of Arg-Gly-Asp-Ser (RGDS) peptide or wortmannin to block {alpha}IIb{beta}3 cross-linking and signaling or in platelets isolated from a patient with Glanzmann thrombasthenia, which express only 2–3% of normal {alpha}IIb{beta}3 levels. Furthermore, actin assembly and Arp2/3 complex incorporation in the platelet actin cytoskeleton are decreased when {alpha}IIb{beta}3 is engaged. Our results suggest that cofilin is essential for actin dynamics mediated by outside-in signals in activated platelets.


Address for reprint requests and other correspondence: H. Falet, Div. of Hematology, Brigham and Women’s Hospital, One Blackfan Circle, Karp 6, Boston, MA 02115 (e-mail: hfalet{at}rics.bwh.harvard.edu)




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