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Trends Cell Biol. 2014 Oct;24(10):575-83. doi: 10.1016/j.tcb.2014.04.009. Epub 2014 Jun 2.

LIM proteins in actin cytoskeleton mechanoresponse.

Author information

1
Department of Biology, University of Utah, Salt Lake City, UT 84112, USA; Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84112, USA.
2
Department of Biology, University of Utah, Salt Lake City, UT 84112, USA; Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84112, USA; Department of Oncological Sciences, University of Utah, Salt Lake City, UT 84112, USA. Electronic address: mary.beckerle@hci.utah.edu.

Abstract

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.

KEYWORDS:

LIM domain; focal adhesion; mechanotransduction; stress fiber; zyxin

PMID:
24933506
PMCID:
PMC4177944
DOI:
10.1016/j.tcb.2014.04.009
[Indexed for MEDLINE]
Free PMC Article

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