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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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

References

  1. Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha. Bouvard, D., Vignoud, L., Dupé-Manet, S., Abed, N., Fournier, H.N., Vincent-Monegat, C., Retta, S.F., Fassler, R., Block, M.R. J. Biol. Chem. (2003) [Pubmed]
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