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First published online August 20, 2008

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Zyxin uses the force

Focal adhesions (FAs) – the integrin-rich sites that link the cell's actin cytoskeleton to the extracellular matrix – are strengthened by mechanical force. Filamentous actin (F-actin) accumulates at FAs when force is applied and helps to strengthen the integrin-cytoskeleton linkage – but which proteins control F-actin accumulation? On page 2795, Masahiro Sokabe and colleagues describe a role for the FA protein zyxin in this process. The authors show that fluorescently labelled actin polymerises at zyxin-rich FAs, which occur at the cell periphery. Moreover, cells that express a truncated, LIM-domain-only form of zyxin (which displaces endogenous zyxin from FAs) accumulate less F-actin at peripheral FAs. When cells are treated with blebbistatin (an inhibitor of myosin II), the authors show, actin polymerisation and zyxin accumulation at FAs are both diminished. When the cell substrate is subsequently stretched, however, both the localisation of zyxin and the polymerisation of actin at FAs are restored; notably, this restoration is suppressed in the presence of the LIM-domain-only zyxin deletion construct. Thus, zyxin accumulates at FAs in response to force and might, the authors propose, promote the polymerisation of actin.

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Related articles in JCS:

Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner

Hiroaki Hirata, Hitoshi Tatsumi, and Masahiro Sokabe
JCS 2008 121: 2795-2804. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?