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Curr Opin Cell Biol. 2012 Feb;24(1):116-24. doi: 10.1016/j.ceb.2011.11.001. Epub 2011 Dec 2.

Structure and function of focal adhesions.

Author information

1
University of Geneva, Department of Cell Physiology and Metabolism, Centre Médical Universitaire, 1. Rue Michel-Servet, 1211 Geneva 4, Switzerland. Bernhard.Wehrle-Haller@unige.ch

Abstract

Integrin-dependent cell adhesions come in different shapes and serve in different cell types for tasks ranging from cell-adhesion, migration, and the remodeling of the extracellular matrix to the formation and stabilization of immunological and chemical synapses. A major challenge consists in the identification of adhesion-specific as well as common regulatory mechanisms, motivating the need for a deeper analysis of protein-protein interactions in the context of intact focal adhesions. Specifically, it is critical to understand how small differences in binding of integrins to extracellular ligands and/or cytoplasmic adapter proteins affect the assembly and function of an entire focal adhesion. By using the talin-integrin pair as a starting point, I would like to discuss how specific protein-protein and protein-lipid interactions can control the behavior and function of focal adhesions. By responding to chemical and mechanical cues several allosterically regulated proteins create a dynamic multifunctional protein network that provides both adhesion to the extracellular matrix as well as intracellular signaling in response to mechanical changes in the cellular environment.

PMID:
22138388
DOI:
10.1016/j.ceb.2011.11.001
[Indexed for MEDLINE]

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