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Axil, a member of the Axin family, interacts with both glycogen synthase kinase 3beta and beta-catenin and inhibits axis formation of Xenopus embryos.

Authors: Yamamoto, H  Kishida, S  Uochi, T  Ikeda, S  Koyama, S  Asashima, M  Kikuchi, A 
Citation: Yamamoto H, etal., Mol Cell Biol 1998 May;18(5):2867-75.
Pubmed: (View Article at PubMed) PMID:9566905

Using a yeast two-hybrid method, we identified a novel protein which interacts with glycogen synthase kinase 3beta (GSK-3beta). This protein had 44% amino acid identity with Axin, a negative regulator of the Wnt signaling pathway.We designated this protein Axil for Axin like. Like Axin, Axil ventralized Xenopus embryos and inhibited Xwnt8-induced Xenopus axis duplication. Axil was phosphorylated by GSK-3beta. Axil bound not only to GSK-3beta but also to beta-catenin, and the GSK-3beta-binding site of Axil was distinct from the beta-catenin-binding site. Furthermore, Axil enhanced GSK-3beta-dependent phosphorylation of beta-catenin. These results indicate that Axil negatively regulates the Wnt signaling pathway by mediating GSK-3beta-dependent phosphorylation of beta-catenin, thereby inhibiting axis formation.

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CRRD Object Information
CRRD ID: 68736
Created: 2001-10-10
Species: All species
Last Modified: 2001-10-10
Status: ACTIVE



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