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

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.

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Genre: Journal Article
Alternative Title : J. Biol. Chem.

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 Creators:
Bouvard, D.1, Author              
Vignoud, L., Author
Dupe-Manet, S., Author
Abed, N., Author
Fournier, H. N., Author
Vincent-Monegat, C., Author
Retta, S. F., Author
Fässler, R.1, Author              
Block, M. R., Author
Affiliations:
1Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              

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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.

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Language(s): eng - English
 Dates: 2003-02-21
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41692
ISI: 000181129400134
 Degree: -

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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 278 (8) Sequence Number: - Start / End Page: 6567 - 6574 Identifier: ISSN: 0021-9258