α-Catenin contributes to the strength of E-cadherin-p120 interactions
Research output: Contribution to journal › Journal article › Research
Cadherin-catenin interactions play an important role in cadherin-mediated adhesion. Here we present strong evidence that in the cadherin-catenin complex α-catenin contributes to the binding strength of another catenin, p120, to the same complex. Specifically, we found that a β-catenin-uncoupled cadherin mutant interacts much more weakly with p120 than its full-size counterpart and that it is rapidly endocytosed from the surface of A-431 cells. We also showed that p120 overexpression stabilizes this mutant on the cell surface. Examination of the α-catenin-deficient MDA-MB-468 cells and their derivates in which α-catenin was reintroduced showed that α-catenin reinforces E-cadherin-p120 association. Finally, a cross-linking analysis of the cadherin-catenin complex indicated that a large loop located in the middle of the p120 arm-repeat domain is in close spatial vicinity to the amino-terminal VH1 domain of α-catenin. The six amino acid-long extension of this loop, caused by an alternative splicing, weakens p120 binding to cadherin. The data suggest that α-catenin-p120 contact within the cadherin-catenin complex can regulate cadherin trafficking.
Original language | English |
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Journal | Molecular Biology of the Cell |
Volume | 22 |
Issue number | 22 |
Pages (from-to) | 4247-55 |
Number of pages | 9 |
ISSN | 1059-1524 |
DOIs | |
Publication status | Published - Nov 2011 |
- Cadherins, Catenins, Cell Adhesion, Cell Adhesion Molecules, Cell Line, Tumor, Cell Membrane, Humans, Mutation, Protein Binding, Protein Transport, Signal Transduction, alpha Catenin, beta Catenin
Research areas
ID: 61726201