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Wnt-induced dephosphorylation of Axin releases β-catenin from the Axin complex

Authors
Publisher
Cold Spring Harbor Laboratory Press
Publication Date
Source
PMC
Keywords
  • Research Communication
Disciplines
  • Biology

Abstract

The stabilization of β-catenin is a key regulatory step during cell fate changes and transformations to tumor cells. Several interacting proteins, including Axin, APC, and the protein kinase GSK-3β are implicated in regulating β-catenin phosphorylation and its subsequent degradation. Wnt signaling stabilizes β-catenin, but it was not clear whether and how Wnt signaling regulates the β-catenin complex. Here we show that Axin is dephosphorylated in response to Wnt signaling. The dephosphorylated Axin binds β-catenin less efficiently than the phosphorylated form. Thus, Wnt signaling lowers Axin’s affinity for β-catenin, thereby disengaging β-catenin from the degradation machinery.

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