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DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability.

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.

Pubmed ID: 10330181

Authors

  • Kishida S
  • Yamamoto H
  • Hino S
  • Ikeda S
  • Kishida M
  • Kikuchi A

Journal

Molecular and cellular biology

Publication Data

June 17, 1999

Associated Grants

None

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Axin Protein
  • Cell Line
  • Chromatography, Gel
  • Cytoskeletal Proteins
  • Dose-Response Relationship, Drug
  • Escherichia coli
  • Fluorescent Antibody Technique
  • Microinjections
  • Microscopy, Confocal
  • Models, Genetic
  • Phosphoproteins
  • Phosphorylation
  • Plasmids
  • Proteins
  • Proto-Oncogene Proteins c-myc
  • Repressor Proteins
  • Saccharomyces cerevisiae
  • Time Factors
  • Trans-Activators
  • Transfection
  • beta Catenin