| Autor: |
Yamamoto, Hideki, Kishida, Shosei, Uochi, Takaaki, Ikeda, Satoshi, Koyama, Shinya, Asashima, Makoto, Kikuchi, Akira |
| Zdroj: |
Molecular and Cellular Biology; May 1998, Vol. 18 Issue: 5 p2867-2875, 9p |
| Abstrakt: |
ABSTRACTUsing a yeast two-hybrid method, we identified a novel protein which interacts with glycogen synthase kinase 3ß (GSK-3ß). 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 Xenopusembryos and inhibited Xwnt8-induced Xenopusaxis duplication. Axil was phosphorylated by GSK-3ß. Axil bound not only to GSK-3ß but also to ß-catenin, and the GSK-3ß-binding site of Axil was distinct from the ß-catenin-binding site. Furthermore, Axil enhanced GSK-3ß-dependent phosphorylation of ß-catenin. These results indicate that Axil negatively regulates the Wnt signaling pathway by mediating GSK-3ß-dependent phosphorylation of ß-catenin, thereby inhibiting axis formation. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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