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

http://www.ncbi.nlm.nih.gov/pubmed/9700171

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 RIS Download

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

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