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Disruption of focal adhesions by integrin cytoplasmic domain- associated protein-1 alpha

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Bouvard,  D.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

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Fässler,  R.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Bouvard, D., Vignoud, L., Dupe-Manet, S., Abed, N., Fournier, H. N., Vincent-Monegat, C., et al. (2003). Disruption of focal adhesions by integrin cytoplasmic domain- associated protein-1 alpha. Journal of Biological Chemistry, 278(8), 6567-6574.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6C99-8
Abstract
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.