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alpha-Catenin-vinculin interaction functions to organize the apical junctional complex in epithelial cells.

Authors
  • Watabe-Uchida, M
  • Uchida, N
  • Imamura, Y
  • Nagafuchi, A
  • Fujimoto, K
  • Uemura, T
  • Vermeulen, S
  • van Roy, F
  • Adamson, E D
  • Takeichi, M
Type
Published Article
Journal
The Journal of cell biology
Publication Date
Aug 10, 1998
Volume
142
Issue
3
Pages
847–857
Identifiers
PMID: 9700171
Source
Medline
License
Unknown

Abstract

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.

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