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Originally published In Press as doi:10.1074/jbc.M211258200 on December 7, 2002

J. Biol. Chem., Vol. 278, Issue 8, 6567-6574, February 21, 2003
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Disruption of Focal Adhesions by Integrin Cytoplasmic Domain-associated Protein-1alpha *

Daniel BouvardDagger §, Lucile VignoudDagger , Sandra Dupé-ManetDagger , Nadia AbedDagger , Henri-Noël FournierDagger , Carole Vincent-MonegatDagger , Saverio Francesco Retta||, Reinhard Fässler§, and Marc R. BlockDagger **

From the Dagger  Laboratoire d'Etude de la Differenciation et de l'Adhérence Cellulaires, Unité Mixte de Recherche UJF/CNRS 5538, Institut Albert Bonniot, Faculte de Médecine de Grenoble, La Tronche F38706 cedex, France, the || Department of Genetics, Biology, and Biochemistry, University of Torino, Torino 10126, Italy, and the § Department of Molecular Medicine, Max Planck Institute for Biochemistry, Am Klopferspitz 18A, Martinsried D-82152, Germany

Regulation of integrin affinity and clustering plays a key role in the control of cell adhesion and migration. The protein ICAP-1alpha (integrin cytoplasmic domain-associated protein-1alpha ) binds to the cytoplasmic domain of the beta 1A integrin and controls cell spreading on fibronectin. Here, we demonstrate that, despite its ability to interact with beta 1A integrin, ICAP-1alpha is not recruited in focal adhesions, whereas it is colocalized with the integrin at the ruffling edges of the cells. ICAP-1alpha induced a rapid disruption of focal adhesions, which may result from the ability of ICAP-1alpha to inhibit the association of beta 1A integrin with talin, which is crucial for the assembly of these structures. ICAP-1alpha -mediated dispersion of beta 1A integrins is not observed with beta 1D integrins that do not bind ICAP. This strongly suggests that ICAP-1alpha action depends on a direct interaction between ICAP-1alpha and the cytoplasmic domain of the beta 1 chains. Altogether, these results suggest that ICAP-1alpha plays a key role in cell adhesion by acting as a negative regulator of beta 1 integrin avidity.

* This work was supported in part by the Fédération Nationale des Ligues Contre le Cancer, the CNRS (Program Biologie Cellulaire: du Normal au Pathologique), and the Association pour la Recherche contre le Cancer.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipient of a fellowship from the Ministère de la Recherche and the Association pour la Recherche contre le Cancer and presently supported by a Marie-Curie fellowship.

** To whom correspondence should be addressed. Tel.: 33-476-54-95-70; Fax: 33-476-54-94-25; E-mail: marc.block@ujf-grenoble.fr.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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