LIM proteins in actin cytoskeleton mechanoresponse
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作者:
Smith, M. A.
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Univ Utah, Dept Biol, Salt Lake City, UT 84112 USA
Univ Utah, Huntsman Canc Inst, Salt Lake City, UT 84112 USAUniv Utah, Dept Biol, Salt Lake City, UT 84112 USA
Smith, M. A.
[1
,2
]
Hoffman, L. M.
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机构:
Univ Utah, Dept Biol, Salt Lake City, UT 84112 USA
Univ Utah, Huntsman Canc Inst, Salt Lake City, UT 84112 USAUniv Utah, Dept Biol, Salt Lake City, UT 84112 USA
Hoffman, L. M.
[1
,2
]
Beckerle, M. C.
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机构:
Univ Utah, Dept Biol, Salt Lake City, UT 84112 USA
Univ Utah, Huntsman Canc Inst, Salt Lake City, UT 84112 USA
Univ Utah, Dept Oncol Sci, Salt Lake City, UT 84112 USAUniv Utah, Dept Biol, Salt Lake City, UT 84112 USA
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
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.