The structure and regulation of vinculin

被引:393
作者
Ziegler, Wolfgang H.
Liddington, Robert C.
Critchley, David R. [1 ]
机构
[1] Univ Leicester, Dept Biochem, Leicester LE2 7HD, Leics, England
[2] Univ Leipzig, Fac Med, IZKF Leipzig, D-04103 Leipzig, Germany
[3] Burnham Inst, Program Cell Adhes, La Jolla, CA 92037 USA
基金
英国惠康基金;
关键词
D O I
10.1016/j.tcb.2006.07.004
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Vinculin is a ubiquitously expressed actin-binding protein frequently used as a marker for both cell-cell and cell-extracellular matrix (focal adhesion) adherens-type junctions, but its function has remained elusive. Vinculin is made up of a globular head linked to a tail domain by a short proline-rich sequence, and an intramolecular interaction between the head and tail masks the numerous ligand-binding sites in the protein. Determination of the crystal structure of vinculin has shed new light on the way that these ligand-binding sites are regulated. The picture that emerges is one in which vinculin stabilizes focal adhesions and thereby suppresses cell migration, an effect that is relieved by transient changes in the local concentrations of inositol phospholipids. However, the finding that vinculin modulates the signalling pathways involved in apoptosis suggests that additional roles for vinculin remain to be discovered.
引用
收藏
页码:453 / 460
页数:8
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