Interaction of dishevelled and Xenopus axin-related protein is required for Wnt signal transduction

Signaling by the Wnt family of secreted proteins plays an important role in animal development and is often misregulated in carcinogenesis. Wnt signal transduction is controlled by the rate of degradation of beta-catenin by a complex of proteins including glycogen synthase kinase 3 (GSK3), adenomato us polyposis coli, and Axin, Dishevelled is required for Wnt signal transdu ction, and its activation results in stabilization of beta-catenin. However , the biochemical events underlying this process remain largely unclear. He re we show that Xenopus Dishevelled (Xdsh) interacts with a Xenopus Axin-re lated protein (XARP). This interaction depends on the presence of the Dishe velled-Axin (DIX) domains in both XARP and Xdsh. Moreover, the same domains are essential for signal transduction through Xdsh, Finally, our data poin t to a possible mechanism for signal transduction, in which Xdsh prevents b eta-catenin degradation by displacing GSK3 from its complex with XARP.