?-Catenin contributes to the strength of E-cadherin-p120 interactions.

ABSTRACT: Cadherin-catenin interactions play an important role in cadherin-mediated adhesion. Here we present strong evidence that in the cadherin-catenin complex ?-catenin contributes to the binding strength of another catenin, p120, to the same complex. Specifically, we found that a ?-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 ?-catenin-deficient MDA-MB-468 cells and their derivates in which ?-catenin was reintroduced showed that ?-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 ?-catenin. The six amino acid-long extension of this loop, caused by an alternative splicing, weakens p120 binding to cadherin. The data suggest that ?-catenin-p120 contact within the cadherin-catenin complex can regulate cadherin trafficking.

SUBMITTER: Troyanovsky RB 

PROVIDER: S-EPMC3216651 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature