α-Catenin-Vinculin Interaction Functions to Organize the Apical Junctional Complex in Epithelial Cells

作者：Mitsuko Watabe‐Uchida, Naoshige Uchida, Yuzo Imamura, Akira Nagafuchi, Kazushi Fujimoto, Tadashi Uemura, Stefan J. T. Vermeulen, Frans M. Van Roy, Eileen D. Adamson, Masatoshi Takeichi · 发表于：The Journal of Cell Biology · 年份：1998 · DOI：10.1083/jcb.142.3.847 · 被引用次数：346 · 研究领域：Wnt/β-catenin signaling in development and cancer、Barrier Structure and Function Studies、Hippo pathway signaling and YAP/TAZ

alphaE-catenin, a cadherin-associated protein, is required for tight junction (TJ) organization, but its role is poorly understood. We transfected an alphaE-catenin-deficient colon carcinoma line with a series of alphaE-catenin mutant constructs. The results showed that the amino acid 326-509 domain of this catenin was required to organize TJs, and its COOH-terminal domain was not essential for this process. The 326-509 internal domain was found to bind vinculin. When an NH2-terminal alphaE-catenin fragment, which is by itself unable to organize the TJ, was fused with the vinculin tail, this chimeric molecule could induce TJ assembly in the alphaE-catenin-deficient cells. In vinculin-null F9 cells, their apical junctional organization was impaired, and this phenotype was rescued by reexpression of vinculin. These results indicate that the alphaE-catenin-vinculin interaction plays a role in the assembly of the apical junctional complex in epithelia.