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| ID:
41692.0,
MPI für Biochemie / Molecular Medicine (R. Fässler) |
| Disruption of focal adhesions by integrin cytoplasmic domain- associated protein-1 alpha |
| Authors: | Bouvard, D.; Vignoud, L.; Dupe-Manet, S.; Abed, N.; Fournier, H. N.; Vincent-Monegat, C.; Retta, S. F.; Fässler, R.; Block, M. R. | | Language: | English | | Date of Publication (YYYY-MM-DD): | 2003-02-21 | | Title of Journal: | Journal of Biological Chemistry | | Journal Abbrev.: | J. Biol. Chem. | | Volume: | 278 | | Issue / Number: | 8 | | Start Page: | 6567 | | End Page: | 6574 | | Review Status: | Peer-review | | Audience: | Not Specified | | Abstract / Description: | 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. | | Comment of the Author/Creator: | Date: 2003, FEB 21 | | External Publication Status: | published | | Document Type: | Article |
| Communicated by: | N.N. | | Affiliations: | MPI für Biochemie/Molecular Medicine (R. Fässler)
| | External Affiliations: | Fac Med Grenoble, Inst Albert Bonniot, UMR UJR CNRS 5538, Lab; Etud Differenciat & Adherence Cellulaires, F-38706 La Tronche,; France; Fac Med Grenoble, Inst Albert Bonniot, UMR UJR CNRS 5538, Lab Etud Differenciat & Adherence Cellulaires, F-38706 La Tronche, France; Univ Turin, Dept Genet Biol & Biochem, I-10126 Turin, Italy
| | Identifiers: | ISI:000181129400134 [ID No:1]
ISSN:0021-9258 [ID No:2] | |
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