Unraveling the molecular architecture of a G protein-coupled receptor/ß-arrestin/Erk module complex.
Sci Rep
; 5: 10760, 2015 Jun 01.
Article
en En
| MEDLINE
| ID: mdl-26030356
ABSTRACT
ß-arrestins serve as signaling scaffolds downstream of G protein-coupled receptors, and thus play a crucial role in a plethora of cellular processes. Although it is largely accepted that the ability of ß-arrestins to interact simultaneously with many protein partners is key in G protein-independent signaling of GPCRs, only the precise knowledge of these multimeric arrangements will allow a full understanding of the dynamics of these interactions and their functional consequences. However, current experimental procedures for the determination of the three-dimensional structures of protein-protein complexes are not well adapted to analyze these short-lived, multi-component assemblies. We propose a model of the receptor/ß-arrestin/Erk1 signaling module, which is consistent with most of the available experimental data. Moreover, for the ß-arrestin/Raf1 and the ß-arrestin/ERK interactions, we have used the model to design interfering peptides and shown that they compete with both partners, hereby demonstrating the validity of the predicted interaction regions.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Modelos Moleculares
/
Arrestinas
/
Receptores Acoplados a Proteínas G
/
Quinasas MAP Reguladas por Señal Extracelular
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
Sci Rep
Año:
2015
Tipo del documento:
Article