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, 22 (11), 1753-60

Dishevelled-DEP Domain Interacting Protein (DDIP) Inhibits Wnt Signaling by Promoting TCF4 Degradation and Disrupting the TCF4/beta-catenin Complex

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Dishevelled-DEP Domain Interacting Protein (DDIP) Inhibits Wnt Signaling by Promoting TCF4 Degradation and Disrupting the TCF4/beta-catenin Complex

Haiwei Zhang et al. Cell Signal.

Abstract

The TCF4/beta-catenin complex, the executor of canonical Wnt/beta-catenin signaling, is regulated by a variety of factors. Among these, Dishevelled (Dvl) is a critical regulator that releases beta-catenin from degradation and stabilizes TCF4/beta-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 beta-catenin, interacts with the TCF4/beta-catenin complex, and disrupts the interaction of TCF4 and beta-catenin by promoting TCF4 degradation through the proteasome pathway. Our results indicate that DDIP is a negative regulator of the canonical Wnt signaling.

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