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Molecular and Cellular Biology, June 1999, p. 4414-4422, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

DIX Domains of Dvl and Axin Are Necessary for Protein Interactions and Their Ability To Regulate beta -Catenin Stability

Shosei Kishida,1,2 Hideki Yamamoto,1 Shin-ichiro Hino,1 Satoshi Ikeda,1 Michiko Kishida,1 and Akira Kikuchi1,*

Department of Biochemistry, Hiroshima University School of Medicine, Minami-ku, Hiroshima 734-8551,1 and PRESTO, Japan Science and Technology Corporation, Hiroshima,2 Japan

Received 28 December 1998/Returned for modification 4 February 1999/Accepted 3 March 1999

The N-terminal region of Dvl-1 (a mammalian Dishevelled homolog) shares 37% identity with the C-terminal region of Axin, and this related region is named the DIX domain. The functions of the DIX domains of Dvl-1 and Axin were investigated. By yeast two-hybrid screening, the DIX domain of Dvl-1 was found to interact with Dvl-3, a second mammalian Dishevelled relative. The DIX domains of Dvl-1 and Dvl-3 directly bound one another. Furthermore, Dvl-1 formed a homo-oligomer. Axin also formed a homo-oligomer, and its DIX domain was necessary. The N-terminal region of Dvl-1, including its DIX domain, bound to Axin directly. Dvl-1 inhibited Axin-promoted glycogen synthase kinase 3beta -dependent phosphorylation of beta -catenin, and the DIX domain of Dvl-1 was required for this inhibitory activity. Expression of Dvl-1 in L cells induced the nuclear accumulation of beta -catenin, and deletion of the DIX domain abolished this activity. Although expression of Axin in SW480 cells caused the degradation of beta -catenin and reduced the cell growth rate, expression of an Axin mutant that lacks the DIX domain did not affect the level of beta -catenin or the growth rate. These results indicate that the DIX domains of Dvl-1 and Axin are important for protein-protein interactions and that they are necessary for the ability of Dvl-1 and Axin to regulate the stability of beta -catenin.

* 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.

Molecular and Cellular Biology, June 1999, p. 4414-4422, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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