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First published online September 19, 2007
doi: 10.1242/10.1242/jcs.013771

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Mechanistic insights from structural studies of -catenin and its binding partners

¹ Departments of Biological Structure
² Departments of Biochemistry, University of Washington, Seattle, WA 98195, USA

^* Author for correspondence (e-mail: wxu{at}u.washington.edu)

Accepted 19 July 2007

-catenin is both a crucial regulator of cell adhesion and the central effector of the canonical Wnt signaling pathway. It functions as a protein organizer by interacting with numerous partners at the membrane, in the cytosol, and in the nucleus. Recent structural and biochemical studies have revealed how -catenin engages in critical protein-protein interactions by using its armadillo repeat region and its N- and C-terminal domains. The groove in the armadillo repeat region is a particularly interesting feature of -catenin, since it serves as a common binding site for several -catenin-binding partners, with steric hindrance limiting which partners can be bound at a specific time. These studies provide important insights into -catenin-mediated mechanisms of cell adhesion and Wnt signaling and suggest potential approaches for the design of therapeutic agents to treat diseases caused by misregulated -catenin expression.

Key words: -catenin structure, Wnt signaling, Cell adhesion, Protein-protein interaction