Cancer Institute A national cancer institute
designated cancer center

Roeland Nusse

Publication Details

  • Wnt-induced dephosphorylation of Axin releases beta-catenin from the Axin complex GENES & DEVELOPMENT Willert, K., Shibamoto, S., Nusse, R. 1999; 13 (14): 1768-1773

    Abstract:

    The 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.

    View details for Web of Science ID 000081711100002

    View details for PubMedID 10421629

Stanford Medicine Resources:

Footer Links: