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Mol Cell Biol, May 1998, p. 2867-2875, Vol. 18, No. 5
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Axil, a Member of the Axin Family, Interacts with Both Glycogen Synthase Kinase 3beta and beta -Catenin and Inhibits Axis Formation of Xenopus Embryos

Hideki Yamamoto,1 Shosei Kishida,1 Takaaki Uochi,2 Satoshi Ikeda,1 Shinya Koyama,1 Makoto Asashima,2 and Akira Kikuchi1,*

Department of Biochemistry, Hiroshima University School of Medicine, Minami-ku, Hiroshima 734-8551,1 and Department of Life Science (Biology), University of Tokyo, Meguro-ku, Tokyo 153-8902,2 Japan

Received 17 November 1997/Returned for modification 19 December 1997/Accepted 13 February 1998

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.

* Corresponding author. Mailing address: Department of Biochemistry, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan. Phone: 81-82-257-5130. Fax: 81-82-257-5134. E-mail: akikuchi{at}mcai.med.hiroshima-u.ac.jp.

Mol Cell Biol, May 1998, p. 2867-2875, Vol. 18, No. 5
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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