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The Journal of Biological Chemistry
Year: 2008  |  Volume: 283  |  Issue: 35  |  Page No.: 23956 - 23963

Smad7 Stabilizes β-Catenin Binding to E-cadherin Complex and Promotes Cell-Cell Adhesion

Yi Tang, Zhongyu Liu, Ling Zhao, Thomas L. Clemens and Xu Cao    

Abstract: β-Catenin functions both as an adherens junction adhesion protein and as an essential mediator of the canonical Wnt signaling pathway. Wnts stabilize β-catenin and promote its accumulation in the nucleus, where it regulates transcription of the target genes. Here we show that Smad7 promotes cell-cell adhesion by stabilizing β-catenin and consequently increases the β-catenin-E-cadherin complex level at the plasma membrane. A Smad7-Axin interaction disassociates GSK-3β and β-catenin from Axin, as well as inhibits the recruitment of Smurf2, an E3 ligase, to β-catenin, thus protecting β-catenin from phosphorylation and degradation. Smad7 increases the stabilized β-catenin to form a complex with E-cadherin and stabilizes the E-cadherin-β-catenin complex. Thereby, rather than being translocated to the nucleus for regulating the target gene transcription, Smad7-stabilized-β-catenin is shunted to the E-cadherin complex to modulate cell-cell adhesion.

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