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pubmed-article:10421629pubmed:abstractTextThe stabilization of beta-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-3beta are implicated in regulating beta-catenin phosphorylation and its subsequent degradation. Wnt signaling stabilizes beta-catenin, but it was not clear whether and how Wnt signaling regulates the beta-catenin complex. Here we show that Axin is dephosphorylated in response to Wnt signaling. The dephosphorylated Axin binds beta-catenin less efficiently than the phosphorylated form. Thus, Wnt signaling lowers Axin's affinity for beta-catenin, thereby disengaging beta-catenin from the degradation machinery.lld:pubmed
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pubmed-article:10421629pubmed:articleTitleWnt-induced dephosphorylation of axin releases beta-catenin from the axin complex.lld:pubmed
pubmed-article:10421629pubmed:affiliationHoward Hughes Medical Institute (HHMI) and Department of Developmental Biology, Stanford University School of Medicine, Stanford, California 94305 USA.lld:pubmed
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pubmed-article:10421629pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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