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Commun Integr Biol. 2008;1(2):192-5.

Zyxin emerges as a key player in the mechanotransduction at cell adhesive structures.

Author information

  • 1Cell Mechanosensing Project; ICORP/SORST; Japan Science and Technology Agency; Nagoya Japan; Department of Molecular Physiology; National Institute for Physiological Sciences; National Institutes of Natural Sciences; Okazaki Japan; Department of Physiology; Nagoya University Graduate School of Medicine; Nagoya Japan.

Abstract

Actin stress fiber (SF), focal adhesion (FA) and adherens junction (AJ) are known structures whose formation and development are mechanical force-dependent. At these structures, actin is actively polymerized, which in turn contributes the development of these structures. Recently, we reported that actin polymerization at FAs is facilitated by mechanical forces, which was critically dependent on the force-induced recruitment of the LIM protein zyxin to FAs. Zyxin enhances actin polymerization with the aid of Ena/VASP proteins. Both zyxin and Ena/VASP proteins are localized not only to FAs but also to AJs and SFs, facilitating actin polymerization at these structures. We discuss here the possibility that zyxin is a common mechanotransducer element regulating actin polymerization at FAs, AJs and SFs.

KEYWORDS:

Ena/VASP; actin polymerization; adherens junction; focal adhesion; mechanotransduction; stress fiber; zyxin

PMID:
19513257
[PubMed]
PMCID:
PMC2686020
Free PMC Article
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