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XB-ART-10491
J Biol Chem 2000 Nov 24;27547:37030-7. doi: 10.1074/jbc.M005984200.
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Inhibition of Wnt signaling pathway by a novel axin-binding protein.

Kadoya T , Kishida S , Fukui A , Hinoi T , Michiue T , Asashima M , Kikuchi A .


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Axin forms a complex with adenomatous polyposis coli gene product, glycogen synthase kinase-3beta (GSK-3beta), beta-catenin, Dvl, and protein phosphatase 2A and functions as a scaffold protein in the Wnt signaling pathway. In the Axin complex, GSK-3beta efficiently phosphorylates beta-catenin, which is then ubiquitinated and degraded by proteasome. We isolated a novel protein that binds to Axin and named it Axam (for Axin associating molecule). Axam formed a complex with Axin in intact cells and bound directly to Axin. Axam inhibited the complex formation of Dvl with Axin and the activity of Dvl to suppress GSK-3beta-dependent phosphorylation of Axin. Furthermore, Axam induced the degradation of beta-catenin in SW480 cells and inhibited Wnt-dependent axis duplication in Xenopus embryos. These results suggest that Axam regulates the Wnt signaling pathway negatively by inhibiting the binding of Dvl to Axin.

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Species referenced: Xenopus
Genes referenced: dvl2 gys1 ptpa