Figure 1. The dimeric form of α-catenin interacts preferentially with PIP3 at the membrane of single cells and promotes the formation of long, extended filopodia that may establish attachment with neighboring cells. Monomeric α-catenin is the form that interacts with β-catenin in cadherin complexes at adhesion sites. Forcible dimerization of α-catenin mutants that do not bind PIP3 prevents filopodia formation and promotes faster wound closure of epithelial sheets. Strikingly, expression of these PIP3-binding defective mutants also interferes with the stability of cadherin-based adhesions.
Figure 1.

The dimeric form of α-catenin interacts preferentially with PIP3 at the membrane of single cells and promotes the formation of long, extended filopodia that may establish attachment with neighboring cells. Monomeric α-catenin is the form that interacts with β-catenin in cadherin complexes at adhesion sites. Forcible dimerization of α-catenin mutants that do not bind PIP3 prevents filopodia formation and promotes faster wound closure of epithelial sheets. Strikingly, expression of these PIP3-binding defective mutants also interferes with the stability of cadherin-based adhesions.

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