@article {cite-key, title = {Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex.}, journal = {Genes Dev}, volume = {13}, number = {14}, year = {1999}, month = {Jul}, pages = {1768{\textendash}1773}, address = {Howard Hughes Medical Institute (HHMI) and Department of Developmental Biology, Stanford University School of Medicine, Stanford, California 94305 USA.}, 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{\textquoteright}s affinity for beta-catenin, thereby disengaging beta-catenin from the degradation machinery.}, issn = {0890-9369 (Print); 0890-9369 (Linking)}, author = {Willert, K and Shibamoto, S and Nusse, R} }