Disruption of Focal Adhesions by Integrin Cytoplasmic Domain-associated Protein-1Î

Regulation of integrin affinity and clustering plays a key role in the control of cell adhesion and migration. The protein ICAP-1α (integrin cytoplasmic domain-associated protein-1α) binds to the cytoplasmic domain of the β 1A integrin and controls cell spreading on fibronectin. Here, we demonstr...

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Bibliographic Details
Published in:The Journal of biological chemistry 2003-02, Vol.278 (8), p.6567
Main Authors: Daniel Bouvard, Lucile Vignoud, Sandra Dupé-Manet, Nadia Abed, Henri-Noël Fournier, Carole Vincent-Monegat, Saverio Francesco Retta, Reinhard Fässler, Marc R. Block
Format: Article
Language:English
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Summary:Regulation of integrin affinity and clustering plays a key role in the control of cell adhesion and migration. The protein ICAP-1α (integrin cytoplasmic domain-associated protein-1α) binds to the cytoplasmic domain of the β 1A integrin and controls cell spreading on fibronectin. Here, we demonstrate that, despite its ability to interact with β 1A integrin, ICAP-1α is not recruited in focal adhesions, whereas it is colocalized with the integrin at the ruffling edges of the cells. ICAP-1α induced a rapid disruption of focal adhesions, which may result from the ability of ICAP-1α to inhibit the association of β 1A integrin with talin, which is crucial for the assembly of these structures. ICAP-1α-mediated dispersion of β 1A integrins is not observed with β 1D integrins that do not bind ICAP. This strongly suggests that ICAP-1α action depends on a direct interaction between ICAP-1α and the cytoplasmic domain of the β 1 chains. Altogether, these results suggest that ICAP-1α plays a key role in cell adhesion by acting as a negative regulator of β 1 integrin avidity.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M211258200