Beta-arrestin is a necessary component of Wnt/beta-catenin signaling in vitro and in vivo.

ABSTRACT: The Wnt/beta-catenin signaling pathway is crucial for proper embryonic development and tissue homeostasis. The phosphoprotein dishevelled (Dvl) is an integral part of Wnt signaling and has recently been shown to interact with the multifunctional scaffolding protein beta-arrestin. Using Dvl deletion constructs, we found that beta-arrestin binds a region N-terminal of the PDZ domain of Dvl, which contains casein kinase 1 (CK1) phosphorylation sites. Inhibition of Wnt signaling by CK1 inhibitors reduced the binding of beta-arrestin to Dvl. Moreover, mouse embryonic fibroblasts lacking beta-arrestins were able to phosphorylate LRP6 in response to Wnt-3a but decreased the activation of Dvl and blocked beta-catenin signaling. In addition, we found that beta-arrestin can bind axin and forms a tri

SUBMITTER: Bryja V 

PROVIDER: S-EPMC1871847 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature