Wnt Regulation: Exploring Axin-Disheveled interactions and defining mechanisms by which the SCF E3 ubiquitin ligase is recruited to the destruction complex

Wnt signaling plays key roles in development and disease, by regulating the stability of its key effector βcat. In the absence of Wnt signals, βcat is phosphorylated by the Wnt-regulatory destruction complex, ubiquitinated by an SCF-class E3 ubiquitin ligase, and destroyed by the proteasome. Binding of Wnt ligands to their Frizzled/LRP receptors stabilizes βcat, via the cytoplasmic effector Dsh. Here we explore two important questions in the field: Is there a direct transfer of βcat from the destruction complex to the E3 ligase, and how does Dsh interaction with the destruction complex protein Axin regulate destruction complex function?