Deconstructing the cadherin-catenin-actin complex
Deconstructing the cadherin-catenin-actin complex
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DOI：
10.1016/j.cell.2005.09.020
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发表时间：
2005-12-02
期刊：
影响因子：
64.5
通讯作者：
Nelson, WJ
中科院分区：
文献类型：
--
作者：
Yamada, S;Pokutta, S;Nelson, WJ
组织中细胞的空间和功能组织是由细胞间的粘附决定的，细胞间的粘附被认为是通过粘附蛋白钙粘蛋白家族的细胞外结构域之间的相互作用启动的，并通过与肌动蛋白细胞骨架的连接而加强。普遍的观点认为，钙粘蛋白通过β -连环蛋白和α -连环蛋白与肌动蛋白细胞骨架相连，尽管四级复合物从未被证实。我们测试了这一假设，发现-连环蛋白不会同时与肌动蛋白丝和e -钙粘蛋白- β -连环蛋白复合物相互作用，即使在肌动蛋白结合蛋白和-肌动蛋白存在的情况下，无论是在溶液中还是在分离的钙粘蛋白含膜上。在极化细胞中直接分析表明，无论肌动蛋白组装的动态状态如何，E-cadherin、β -catenin和α -catenin的流动性是相似的，而肌动蛋白和几种肌动蛋白结合蛋白具有更高的流动性。这些结果表明，钙粘蛋白-连环蛋白复合物和肌动蛋白丝之间的联系比以前认为的更动态。
Spatial and functional organization of cells in tissues is determined by cell-cell adhesion, thought to be initiated through trans-interactions between extracellular domains of the cadherin family of adhesion proteins, and strengthened by linkage to the actin cytoskeleton. Prevailing dogma is that cadherins are linked to the actin cytoskeleton through beta-catenin and alpha-catenin, although the quaternary complex has never been demonstrated. We test this hypothesis and find that alpha-catenin does not interact with actin filaments and the E-cadherin-beta-catenin complex simultaneously, even in the presence of the actin binding proteins vinculin and alpha-actinin, either in solution or on isolated cadherin-containing membranes. Direct analysis in polarized cells shows that mobilities of E-cadherin, beta-catenin, and alpha-catenin are similar, regardless of the dynamic state of actin assembly, whereas actin and several actin binding proteins have higher mobilities. These results suggest that the linkage between the cadherin-catenin complex and actin filaments is more dynamic than previously appreciated.