@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}
}
