Afadin regulates actomyosin organization through αE-catenin at adherens junctions.
Afadin regulates actomyosin organization through αE-catenin at adherens junctions.
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Afadin 通过粘附连接处的 αE-连环蛋白调节肌动球蛋白组织。
DOI：
10.1083/jcb.201907079
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
Takai Y.
中科院分区：
文献类型：
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作者：
Sakakibara S;Mizutani K;Sugiura A;Sakane A;Sasaki T;Yonemura S;Takai Y.
肌动球蛋白包被的粘附素连接对上皮细胞的完整性和重塑至关重要。肌动球蛋白在体内通过αE-连环蛋白与β-连环蛋白和E-钙粘附素的络合作用与粘连连接结合；然而，体外溶液生化研究表明，αE-连环蛋白与β-连环蛋白的络合作用低于αE-连环蛋白与F-肌动蛋白的结合效率，而βE-连环蛋白与β-连环蛋白不结合。尽管“捕获键模型”部分解释了这种不一致，但体内和体外结果之间这种不一致的机制仍然难以捉摸。在这里，我们证明了afadin以一种新的机制与αE-catenin与β-catenin络合并增强其F-肌动蛋白结合活性，最终通过αE-catenin与β-catenin和E-钙粘附素在黏附连接处的络合诱导适当的肌球蛋白组织。
Actomyosin-undercoated adherens junctions are critical for epithelial cell integrity and remodeling. Actomyosin associates with adherens junctions through αE-catenin complexed with β-catenin and E-cadherin in vivo; however, in vitro biochemical studies in solution showed that αE-catenin complexed with β-catenin binds to F-actin less efficiently than αE-catenin that is not complexed with β-catenin. Although a “catch-bond model” partly explains this inconsistency, the mechanism for this inconsistency between the in vivo and in vitro results remains elusive. We herein demonstrate that afadin binds to αE-catenin complexed with β-catenin and enhances its F-actin–binding activity in a novel mechanism, eventually inducing the proper actomyosin organization through αE-catenin complexed with β-catenin and E-cadherin at adherens junctions.