Dishevelled-DEP domain interacting protein (DDIP) inhibits Wnt signaling by promoting TCF4 degradation and disrupting the TCF4/β-catenin complex

Haiwei Zhang, Hui Zhang, Yanquan Zhang, Ser Sur Ng, Fangli Ren, Yingying Wang, Yaqi Duan, Lin Chen, Yonggong Zhai, Qinglong Guo, Zhijie Chang

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The TCF4/β-catenin complex, the executor of canonical Wnt/β-catenin signaling, is regulated by a variety of factors. Among these, Dishevelled (Dvl) is a critical regulator that releases β-catenin from degradation and stabilizes TCF4/β-catenin complex. Here, we report that DDIP (Dishevelled- DEP domain Interacting Protein, also named as Spats1, spermatogenesis associated, serine-rich 1), a novel protein that interacts with Dvl, regulates Wnt signaling. We provide evidence that DDIP suppresses Lef-1 luciferase reporter activity stimulated by Wnt1, Dvl2 or β-catenin, interacts with the TCF4/β-catenin complex, and disrupts the interaction of TCF4 and β-catenin by promoting TCF4 degradation through the proteasome pathway. Our results indicate that DDIP is a negative regulator of the canonical Wnt signaling.

Original languageEnglish
Pages (from-to)1753-1760
Number of pages8
JournalCellular Signalling
Volume22
Issue number11
DOIs
StatePublished - Nov 2010

Keywords

  • DDIP
  • Dishevelled
  • Proteasome
  • TCF4/β-catenin complex

ASJC Scopus subject areas

  • Cell Biology

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