J. Cell Biol., Volume 142, Number 3, August 10, 1998 847-857

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

Mitsuko Watabe-Uchida,^* Naoshige Uchida,^* Yuzo Imamura, Akira Nagafuchi, Kazushi Fujimoto,^§ Tadashi Uemura,^* Stefan Vermeulen, Frans van Roy,^¶ Eileen D. Adamson,^** and Masatoshi Takeichi^*

^* Department of Biophysics, Faculty of Science, Kyoto University, Kitashirakawa, Sakyo-ku, Kyoto 606-8502;  Department of Cell Biology and ^§ Department of Anatomy, Faculty of Medicine, Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8507, Japan;  University Hospital of Ghent and ^¶ Department of Molecular Biology, VIB-University of Ghent, B-9000 Ghent, Belgium; and ^** The Burnham Institute, La Jolla, California

E-catenin, a cadherin-associated protein, is required for tight junction (TJ) organization, but its role is poorly understood. We transfected an E-catenin-deficient colon carcinoma line with a series of E-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 E-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 E-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 E-catenin-vinculin interaction plays a role in the assembly of the apical junctional complex in epithelia.

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