Zyxin emerges as a key player in the mechanotransduction at cell adhesive structures
Zyxin emerges as a key player in the mechanotransduction at cell adhesive structures
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DOI：
10.4161/cib.1.2.7001
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发表时间：
2008-10
影响因子：
--
通讯作者：
H. Hirata;H. Tatsumi;M. Sokabe
中科院分区：
文献类型：
--
作者：
H. Hirata;H. Tatsumi;M. Sokabe
肌动蛋白应力纤维（SF）、黏着点（FA）和粘附结（AJ）是已知的与机械力有关的结构。在这些结构中，肌动蛋白被积极聚合，这反过来又促进了这些结构的发展。最近，我们报道了肌动蛋白在FAs的聚合是由机械力促进的，这主要依赖于力诱导的LIM蛋白zyxin向FAs的募集。Zyxin借助Ena/VASP蛋白促进肌动蛋白聚合。zyxin和Ena/VASP蛋白不仅定位于FAs，还定位于AJs和SFs，促进肌动蛋白在这些结构上的聚合。我们在这里讨论了酵素是一种共同的机械换能器元件的可能性，可以调节肌动蛋白在FAs， AJs和SFs的聚合。
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.