Biochemical and Structural Properties of the Integrin-Associated Cytoskeletal Protein Talin

被引:205
作者
Critchley, David R. [1 ]
机构
[1] Univ Leicester, Dept Biochem, Leicester LE1 9HN, Leics, England
基金
英国惠康基金;
关键词
vinculin; actin; PIP2; Rap1; focal adhesions; cytoskeleton; PHOSPHATIDYLINOSITOL PHOSPHATE KINASE; VINCULIN-BINDING-SITES; F-ACTIN-BINDING; CYTOPLASMIC DOMAIN; CELL-MIGRATION; I/LWEQ MODULE; FERM DOMAIN; FUNCTIONAL-SIGNIFICANCE; PLATELET-AGGREGATION; INDUCED ACTIVATION;
D O I
10.1146/annurev.biophys.050708.133744
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Interaction of cells with the extracellular matrix is fundamental to a wide variety of biological processes, such as cell proliferation, cell migration, embryogenesis, and organization of cells into tissues, and defects in cell-matrix interactions are an important element in many diseases. Cell-matrix interactions are frequently mediated by the integrin family of cell adhesion molecules, transmembrane alpha beta-heterodimers that are typically linked to the actin cytoskeleton by one of a number of adaptor proteins including talin, alpha-actinin, filamin, tensin, integrin-linked kinase, melusin, and skelemin. The focus of this review is talin, which appears unique among these proteins in that it also induces a conformational change in integrins that is propagated across the membrane, and increases the affinity of the extracellular domain for ligand. Particular emphasis is given to recent progress on the structure of talin, its interaction with binding partners, and its mode of regulation.
引用
收藏
页码:235 / 254
页数:20
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