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Originally published In Press as doi:10.1074/jbc.M005984200 on August 15, 2000

J. Biol. Chem., Vol. 275, Issue 47, 37030-37037, November 24, 2000
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Inhibition of Wnt Signaling Pathway by a Novel Axin-binding Protein*

Takayuki KadoyaDagger §, Shosei KishidaDagger , Akimasa Fukui||, Takao HinoiDagger §, Tatsuo Michiue**, Makoto Asashima||**, and Akira KikuchiDagger Dagger Dagger

From the Department of Dagger  Biochemistry and § Second Department of Surgery, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551,  PRESTO, Japan Science and Technology Corporation, Hiroshima 734-8551, the || Department of Life Science (Biology), and ** CREST Project, University of Tokyo, 3-8-1, Komaba, Meguro-ku, Tokyo 153-8902, Japan

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.

* This work was supported by grants-in-aid for scientific research (B) and for scientific research on priority areas (A) from the Ministry of Education, Science, and Culture, Japan (1998 and 1999), by grants from the Yamanouchi Foundation for Research on Metabolic Disorders (1998 and 1999), the Uehara Memorial Foundation (1998), and in part by a grant-in-aid (Bio-Design Program) from the Ministry of Agriculture, Forestry, and Fisheries BDP-00-III-1.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number AF260129.

Dagger Dagger To whom correspondence should be addressed: Dept. of Biochemistry, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan. Tel.: 81-82-257-5130; Fax: 81-82-257-5134; E-mail: akikuchi@mcai.med.hiroshima-u.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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