Smad7 stabilizes β-catenin binding to E-cadherin complex and promotes cell-cell adhesion

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

Research output: Contribution to journalArticlepeer-review

49 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)23956-23963
Number of pages8
JournalJournal of Biological Chemistry
Issue number35
StatePublished - Aug 29 2008
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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