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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.
