InterPro: IPR001158 DIX

Dishevelled (Dsh) protein is an important component of the Wnt signal-transduction pathway. It has three relatively conserved domains: DIX, PDZ and DEP. The DIX domain of Dvl-1 (a mammalian Dishevelled homologue) shares 37% identity with the C-terminal region of Axin. Dsh can interact with the Axin/APC/GSK3/beta-catenin complex, and may thus modulate its activity [1].

The Wnt signalling pathway is conserved in various species from Caenorhabditis elegans to mammals, and plays important roles in development, cellular proliferation, and differentiation. The molecular mechanisms by which the Wnt signal regulates cellular functions are becoming increasingly well understood. Wnt stabilises cytoplasmic beta-catenin, which stimulates the expression of genes including c-myc, c-jun, fra-1, and cyclin D1. Axin and its homologue Axil are components of the Wnt signalling pathway that negatively regulate this pathway. Other components of the Wnt signalling pathway, including Dvl, glycogen synthase kinase-3beta (GSK-3beta), beta-catenin, and adenomatous polyposis coli (APC), interact with Axin, and the phosphorylation and stability of beta-catenin are regulated in the Axin complex. Axil has similar functions to Axin. Thus, Axin and Axil act as scaffold proteins in the Wnt signalling pathway, thereby modulating the Wnt-dependent cellular functions [2].