Distinct functionality of dishevelled isoforms on Ca2+/calmodulin-dependent protein kinase 2 (CamKII) in Xenopus gastrulation.

ABSTRACT: Wnt ligands trigger the activation of a variety of β-catenin-dependent and β-catenin-independent intracellular signaling cascades. Despite the variations in intracellular signaling, Wnt pathways share the effector proteins frizzled, dishevelled, and β-arrestin. It is unclear how the specific activation of individual branches and the integration of multiple signals are achieved. We hypothesized that the composition of dishevelled-β-arrestin protein complexes contributes to signal specificity and identified CamKII as an interaction partner of the dishevelled-β-arrestin protein complex by quantitative functional proteomics. Specifically, we found that CamKII isoforms interact differentially with the three vertebrate dishevelled proteins. Dvl1 is required for the activation of CamKII and PKC i

SUBMITTER: Gentzel M 

PROVIDER: S-EPMC4342031 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature