Publication details
Dishevelled at the Crossroads of Pathways
| Authors | |
|---|---|
| Year of publication | 2014 |
| Type | Chapter of a book |
| MU Faculty or unit | |
| Citation | |
| Description | Dishevelled (Dvl) is a cytoplasmic phosphoprotein required for signal transduction in the Wnt/Beta-catenin pathway and in Beta-catenin-independent, collectively called the noncanonical, Wnt pathways. Early genetic experiments in flies demonstrated that Dvl has distinct molecular functions and plays a dual role in both PCP and Beta-catenin-mediated signaling. Dvl is a modular protein that contains three well-defined structural domains linked by the intrinsically disordered regions, which are predicted to have no secondary structure. Rescue analysis using Dvl deletion mutants in flies suggested that DIX and PDZ domains are necessary for Wnt/beta-catenin pathway, whereas PDZ and DEP domains are required for Wnt/PCP pathway Among the several kinases that phosphorylate Dvl proteins, the best described and the first one to mention is casein kinase (CK) 1 Delta/Epsilon. Ubiquitination does not only target proteins for degradation, but it also has a potential to regulate the signaling abilities of modified proteins by differential linkages. |