Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha.
J Biol Chem
; 278(8): 6567-74, 2003 Feb 21.
Article
in En
| MEDLINE
| ID: mdl-12473654
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Carrier Proteins
/
Cell Adhesion
/
Focal Adhesions
/
Intracellular Signaling Peptides and Proteins
/
Membrane Proteins
Type of study:
Risk_factors_studies
Limits:
Animals
/
Humans
Language:
En
Journal:
J Biol Chem
Year:
2003
Document type:
Article
Affiliation country:
France
Country of publication:
United States