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First published online November 8, 2006
doi: 10.1242/10.1242/jcs.03267

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Cinderella no longer: -catenin steps out of cadherin's shadow

Division of Molecular Cell Biology, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Brisbane, Queensland, 4072, Australia

View larger version (20K): [in a new window]   Fig. 1. Possible mechanisms for -catenin-mediated cooperation between classical cadherins and the actin cytoskeleton. (A) A popular earlier model posited a quaternary complex comprising classical cadherins, ß-catenin, -catenin and cortical actin filaments. In this model, -catenin directly binds to both actin filaments and ß-catenin, thereby coupling stable actin filaments to the cadherin adhesion molecule. (B) The more complex current possibilities. -Catenin, acting in the cytosol or bound through ß-catenin to the cadherin molecular complex has the capacity to regulate the actin cytoskeleton by several mechanisms: binding directly to actin filaments, potentially thereby inhibiting Arp2/3-mediated actin nucleation; interacting with a range of actin regulators, including filament nucleators and binding proteins; and interacting with cell signalling pathways that can affect actin dynamics and organization. (C) The regions of -catenin responsible for association with some actin-binding proteins have been mapped.

View larger version (24K): [in a new window]   Fig. 2. Multiple cellular pools of -catenin. -Catenin exists in multiple cellular pools: incorporated into the cadherin complex at the plasma membrane; as monomers, homo- and hetero-dimers in the cytosol; and potentially also in the nucleus. Both in the cytosol and in the nucleus, cadherin-independent -catenin may regulate ß-catenin signalling in the canonical Wnt pathway by forming heterodimers with ß-catenin. , -catenin; ß, ß-catenin; Dsh, dishevelled; Pygo, Pygobus; TCF, T-cell factor.