Dishevelled (DVL) proteins, three of which have been identified in humans, are 
highly conserved components of canonical and noncanonical Wnt signaling 
pathways. These multifunctional proteins, originally discovered in the fruit 
fly, through their different domains mediate complex signal transduction: DIX 
(dishevelled, axin) and PDZ (postsynaptic density 95, discs large, zonula 
occludens-1) domains serve for canonical beta-catenin signaling, while PDZ and 
DEP (dishevelled, Egl-10, pleckstrin) domains serve for non-canonical signaling. 
In canonical or beta-catenin signaling, DVL forms large molecular supercomplexes 
at the plasma membrane consisting of Wnt-Fz-LRP5/6-DVL-AXIN. This promotes the 
disassembly of the beta-catenin destruction machinery, beta-catenin 
accumulation, and consequent activation of Wnt signaling. Therefore, DVLs are 
considered to be key regulators that rescue cytoplasmic beta-catenin from 
degradation. The potential medical importance of DVLs is in both human 
degenerative disease and cancer. The overexpression of DVL has been shown to 
potentiate the activation of Wnt signaling and it is now apparent that 
up-regulation of DVLs is involved in several types of cancer.