An octapeptide in the juxtamembrane domain of VE-cadherin is important for p120ctn binding and cell proliferation.
The cadherins are a family of adhesive proteins involved in cell-cell homophilic interactions. VE-cadherin, expressed in endothelial cells, is involved in morphogenesis, regulation of permeability, and cellular proliferation. The cytoplasmic tails of cadherins contain two major domains, the juxtamembrane domain that plays a role in the intercellular localization of the ... protein and also serves for binding of p120ctn, and a C-terminal domain that associates with beta- or gamma-catenin. A highly conserved region present in the juxtamembrane domain of the cadherins has been shown to be necessary for p120ctn binding in E-cadherin. Using a mutant VE-cadherin lacking a highly conserved octapeptide, we demonstrated that it is required for p120ctn binding to VE-cadherin as determined by immunoprecipitation and colocalization studies. By immunofluorescence, this mutant protein has a topographical distribution similar to that of the wild-type VE-cadherin and, therefore, we conclude that the topographical distribution of VE-cadherin is independent of this motif. In addition, although cell-cell association is present in cells expressing this mutant form of VE-cadherin, we found that the strength of adhesion is decreased. Finally, our results for the first time demonstrate that the interaction of VE-cadherin with p120 catenin plays an important role in cellular growth, suggesting that the binding of p120 catenin to cadherins may regulate cell proliferation.
Mesh Terms:
Amino Acid Sequence, Animals, Antigens, CD, CHO Cells, Cadherins, Cell Adhesion, Cell Adhesion Molecules, Cell Division, Conserved Sequence, Cricetinae, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Peptide Fragments, Phosphoproteins, Protein Binding, Protein Structure, Tertiary, Sequence Deletion, Transfection
Amino Acid Sequence, Animals, Antigens, CD, CHO Cells, Cadherins, Cell Adhesion, Cell Adhesion Molecules, Cell Division, Conserved Sequence, Cricetinae, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Peptide Fragments, Phosphoproteins, Protein Binding, Protein Structure, Tertiary, Sequence Deletion, Transfection
Exp. Cell Res.
Date: Mar. 10, 2002
PubMed ID: 11855855
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