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首页> 外文期刊>Cell communication & adhesion >Direct Interaction fo the C-Terminal Domain of a-Catenin and F-Actin is Necessary for Stabilized Cell-Cell Adhesion
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Direct Interaction fo the C-Terminal Domain of a-Catenin and F-Actin is Necessary for Stabilized Cell-Cell Adhesion

机译：α-连环蛋白和F-肌动蛋白的C末端域的直接相互作用对于稳定的细胞间粘附是必需的

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摘要

Alpha-catenin functions to anchor adherens junctions to the filamentous action (F-actin) cyodkeleton, through direct andindirect binding mechanisms. When truncated at amino acid 865, alpha-catenin exhibited a markedly reducedF-actin binding affinity compared to wild-type. Expression of the truncated mutant in than a-catenin deficient colon carcinoma cell line, Clone A, could not restore an adhesive phenotype when compared. Furthermore, the truncated a-catenin fusion protein failed to concentrate at sitex of cell-cell contact, to promote morphological changes associated with epithelial monolayers, and to stimulate resistance to shearhing forces in a hanging drop aggregation assay. Subsequent attempts to isolate single residues governing the direct F-actin interaction, using neutralizing charge or reverse charge mutations of basic residues within a homology modeled alpha-catenin C-terminal 5-helix bundle. had no effect on F-actin cosedimentation. We conclude that direct attachment of alpha-catenin to F-actin is required to promote cadherin-mediated contact formation and strong cell-cell adhesive states.
机译：α-连环蛋白的功能是通过直接和间接结合机制，将粘附的连接锚定在丝状作用（F-actin）cykeketon上。当在氨基酸865处被截短时，与野生型相比，α-连环蛋白表现出明显降低的F-肌动蛋白结合亲和力。相比于a-catenin缺陷的结肠癌细胞系Clone A，截短的突变体的表达无法恢复粘附表型。此外，截短的α-连环蛋白融合蛋白不能集中在细胞与细胞接触的部位，从而不能促进与上皮单层相关的形态变化，并不能在悬滴聚集试验中刺激对剪切力的抵抗力。随后的尝试使用同源性建模的α-连环蛋白C末端5螺旋束中的碱性残基的中和电荷或反向电荷突变来分离支配直接F-肌动蛋白直接相互作用的单个残基。对F-肌动蛋白的沉淀没有影响。我们得出结论，α-catenin与F-actin的直接连接是促进钙粘蛋白介导的接触形成和强细胞-细胞粘附状态所必需的。

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