α-Catenin cytomechanics - role in cadherin-dependent adhesion and mechanotransduction
α-Catenin cytomechanics - role in cadherin-dependent adhesion and mechanotransduction
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DOI：
10.1242/jcs.139014
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发表时间：
2014-04-15
影响因子：
4
通讯作者：
Leckband, Deborah E.
中科院分区：
文献类型：
--
作者：
Barry, Adrienne K.;Tabdili, Hamid;Leckband, Deborah E.
本文的研究结果证实了α-连环蛋白在不同力学环境中基于钙粘蛋白的粘附和力学转导中的作用。珠扭转测量结合成像，并使用不同的细胞系和α-连环蛋白突变体揭示，急性局部机械操作的钙粘蛋白债券触发黏着斑蛋白和肌动蛋白招聘钙粘蛋白粘附在肌动蛋白和α-连环蛋白依赖的方式。α-连环蛋白对细胞表面钙粘蛋白的二维结合亲和力的适度影响进一步表明，力激活的粘附加强是由于增强的钙粘蛋白与细胞骨架的相互作用，而不是α-连环蛋白依赖的亲和力调节。基于钙粘蛋白的刚性传感的补充调查也表明，虽然α-连环蛋白改变牵引力的产生，它不是唯一的调节顺应性钙粘蛋白涂层基质上的细胞收缩性。
The findings presented here demonstrate the role of alpha-catenin in cadherin-based adhesion and mechanotransduction in different mechanical contexts. Bead-twisting measurements in conjunction with imaging, and the use of different cell lines and alpha-catenin mutants reveal that the acute local mechanical manipulation of cadherin bonds triggers vinculin and actin recruitment to cadherin adhesions in an actin-and alpha-catenin-dependent manner. The modest effect of alpha-catenin on the two-dimensional binding affinities of cell surface cadherins further suggests that forceactivated adhesion strengthening is due to enhanced cadherincytoskeletal interactions rather than to alpha-catenin-dependent affinity modulation. Complementary investigations of cadherin-based rigidity sensing also suggest that, although alpha-catenin alters traction force generation, it is not the sole regulator of cell contractility on compliant cadherin-coated substrata.