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α-Catenin homodimers are recruited to phosphoinositide-activated membranes to promote adhesion

Megan N Wood,N. Ishiyama,I. Singaram,Connie M. Chung,A. S. Flozak,A. Yemelyanov,M. Ikura,W. Cho,C. Gottardi

Published 2017 in Journal of Cell Biology

ABSTRACT

A unique feature of &agr;-catenin localized outside the cadherin–catenin complex is its capacity to form homodimers, but the subcellular localization and functions of this form of &agr;-catenin remain incompletely understood. We identified a cadherin-free form of &agr;-catenin that is recruited to the leading edge of migrating cells in a phosphatidylinositol 3-kinase–dependent manner. Surface plasmon resonance analysis shows that &agr;-catenin homodimers, but not monomers, selectively bind phosphatidylinositol-3,4,5-trisphosphate–containing lipid vesicles with high affinity, where three basic residues, K488, K493, and R496, contribute to binding. Chemical-induced dimerization of &agr;-catenin containing a synthetic dimerization domain promotes its accumulation within lamellipodia and elaboration of protrusions with extended filopodia, which are attenuated in the &agr;-cateninKKR<3A mutant. Cells restored with a full-length, natively homodimerizing form of &agr;-cateninKKR<3A display reduced membrane recruitment, altered epithelial sheet migrations, and weaker cell–cell adhesion compared with WT &agr;-catenin. These findings show that &agr;-catenin homodimers are recruited to phosphoinositide-activated membranes to promote adhesion and migration, suggesting that phosphoinositide binding may be a defining feature of &agr;-catenin function outside the cadherin–catenin complex.

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