Distinct functionality of dishevelled isoforms on Ca2+/calmodulin-dependent protein kinase 2 (CamKII) in Xenopus gastrulation.
Mol Biol Cell
; 26(5): 966-77, 2015 Mar 01.
Article
em En
| MEDLINE
| ID: mdl-25568338
ABSTRACT
Wnt ligands trigger the activation of a variety of ß-catenin-dependent and ß-catenin-independent intracellular signaling cascades. Despite the variations in intracellular signaling, Wnt pathways share the effector proteins frizzled, dishevelled, and ß-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-ß-arrestin protein complexes contributes to signal specificity and identified CamKII as an interaction partner of the dishevelled-ß-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 in the Wnt/Ca(2+) pathway. However, CamKII interacts with Dvl2 but not with Dvl1, and Dvl2 is necessary to mediate CamKII function downstream of Dvl1 in convergent extension movements in Xenopus gastrulation. Our findings indicate that the different Dvl proteins and the composition of dishevelled-ß-arrestin protein complexes contribute to the specific activation of individual branches of Wnt signaling.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfoproteínas
/
Proteínas de Xenopus
/
Proteínas Adaptadoras de Transdução de Sinal
/
Proteína Quinase Tipo 2 Dependente de Cálcio-Calmodulina
/
Gastrulação
Tipo de estudo:
Prognostic_studies
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Mol Biol Cell
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
Alemanha