LIM proteins in actin cytoskeleton mechanoresponse

被引:2
|
作者
Smith, M. A. [1 ,2 ]
Hoffman, L. M. [1 ,2 ]
Beckerle, M. C. [1 ,2 ,3 ]
机构
[1] Univ Utah, Dept Biol, Salt Lake City, UT 84112 USA
[2] Univ Utah, Huntsman Canc Inst, Salt Lake City, UT 84112 USA
[3] Univ Utah, Dept Oncol Sci, Salt Lake City, UT 84112 USA
基金
美国国家卫生研究院;
关键词
mechanotransduction; stress fiber; zyxin; LIM domain; focal adhesion; STRESS FIBERS; FOCAL ADHESIONS; MYOSIN-II; ZYXIN; FORCE; DOMAIN; GROWTH; LOCALIZATION; TENSION; MECHANOTRANSDUCTION;
D O I
10.1016/J.tcb.2014.04.009
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The actin cytoskeleton assembles into branched networks or bundles to generate mechanical force for critical cellular processes such as establishment of polarity, adhesion, and migration. Stress fibers (SFs) are contractile actomyosin structures that physically couple to the extracellular matrix through integrin-based focal adhesions (FAs), thereby transmitting force into and across the cell. Recently, LIN-11, Isl1 and MEC-3 (LIM) domain proteins have been implicated in mediating this cytoskeletal mechanotransduction. Among the more well-studied LIM domain adapter proteins is zyxin, a dynamic component of both FAs and SFs. Here we discuss recent research detailing the mechanisms by which SFs adjust their structure and composition to balance mechanical forces and suggest ways that zyxin and other LIM domain proteins mediate mechanoresponse.
引用
收藏
页码:575 / 583
页数:9
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