Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex.
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| Title | Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex. |
| Publication Type | Journal Article |
| Year of Publication | 1999 |
| Authors | Willert K, Shibamoto S, Nusse R |
| Journal | Genes Dev |
| Volume | 13 |
| Pagination | 1768–1773 |
| Date Published | Jul |
| ISSN | 0890-9369 (Print); 0890-9369 (Linking) |
| 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. |
