The Drosophila dishevelled (Dsh) gene is a member of the segment polarity gene family which is involved in a variety of developmental patterning processes in the embryo and imaginal discs. Human homologs of Dsh (Dvl1, 2 and 3) have been identified.
Three isoforms of dishevelled (Dvl1, Dvl2, and Dvl3) functions in Wnt
Signaling. The DIX domain, the N-terminal region of Dvl-1 which shares 37% identity with the C-terminal region of Axin, is important for protein-protein interactions and the domain is necessary for the ability of Dvl-1 and Axin to regulate the stability of β-catenin in the Wnt signaling pathway.
The DIX domain enables the possible dimerization of Dvl with other members of the Dvl family as well as with Axin, which itself is a scaffold
protein functioning downstream of β-catenin to organize the
multiprotein complex responsible for degrading β-catenin.
1) Lee YN et al. 2008, Cell Signal. 20(2):443-452.
2) Kishida S et al. 1999, Mol Cell Biol. 19(6):4414-4422.
3) Bui TD et al. 1997, Biochem. Biophys. Res. Commun. 239 (2): 510–516.
