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

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.

Pubmed ID: 9700171

Authors

  • Watabe-Uchida M
  • Uchida N
  • Imamura Y
  • Nagafuchi A
  • Fujimoto K
  • Uemura T
  • Vermeulen S
  • van Roy F
  • Adamson ED
  • Takeichi M

Journal

The Journal of cell biology

Publication Data

August 10, 1998

Associated Grants

None

Mesh Terms

  • Binding Sites
  • Cell Communication
  • Cytoskeletal Proteins
  • Epithelial Cells
  • Humans
  • Intercellular Junctions
  • Membrane Proteins
  • Phosphoproteins
  • Recombinant Fusion Proteins
  • Tumor Cells, Cultured
  • Vinculin
  • Zonula Occludens-1 Protein
  • alpha Catenin