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J. Biol. Chem., Vol. 283, Issue 35, 23956-23963, August 29, 2008

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

From the Department of Pathology, University of Alabama at Birmingham, Birmingham, Alabama 35294

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.

Received for publication, January 14, 2008 , and in revised form, June 24, 2008.

^* This work was supported, in whole or in part, by National Institutes of Health Grant DK57501 (to X. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported in part by a Career Scientist Award from the Veterans Affairs Administration.

² To whom correspondence should be addressed: 1670 University Blvd., Birmingham, AL 35294-0019. Tel.: 205-934-0162; Fax: 205-934-1775; E-mail: cao{at}uab.edu.

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