Ezrin directly interacts with the alpha1b-adrenergic receptor and plays a role in receptor recycling.

Détails

ID Serval
serval:BIB_6DF656D98E4E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Ezrin directly interacts with the alpha1b-adrenergic receptor and plays a role in receptor recycling.
Périodique
Journal of Biological Chemistry
Auteur(s)
Stanasila L., Abuin L., Diviani D., Cotecchia S.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
2006
Peer-reviewed
Oui
Volume
281
Numéro
7
Pages
4354-4363
Langue
anglais
Résumé
Using the yeast two-hybrid system, we identified ezrin as a protein interacting with the C-tail of the alpha1b-adrenergic receptor (AR). The interaction was shown to occur in vitro between the receptor C-tail and the N-terminal portion of ezrin, or Four-point-one ERM (FERM) domain. The alpha1b-AR/ezrin interaction occurred inside the cells as shown by the finding that the transfected alpha1b-AR and FERM domain or ezrin could be coimmunoprecipitated from human embryonic kidney 293 cell extracts. Mutational analysis of the alpha1b-AR revealed that the binding site for ezrin involves a stretch of at least four arginines on the receptor C-tail. The results from both receptor biotinylation and immunofluorescence experiments indicated that the FERM domain impaired alpha1b-AR recycling to the plasma membrane without affecting receptor internalization. The dominant negative effect of the FERM domain, which relies on its ability to mask the ezrin binding site for actin, was mimicked by treatment of cells with cytochalasin D, an actin depolymerizing agent. A receptor mutant (DeltaR8) lacking its binding site in the C-tail for ezrin displayed delayed receptor recycling. These findings identify ezrin as a new protein directly interacting with a G protein-coupled receptor and demonstrate the direct implication of ezrin in GPCR trafficking via an actin-dependent mechanism.
Mots-clé
Actins/physiology, Binding Sites, Cell Line, Cytochalasin D/pharmacology, Cytoskeletal Proteins/chemistry, Cytoskeletal Proteins/physiology, Humans, Microscopy, Confocal, Protein Structure, Tertiary, Protein Transport, Receptors, Adrenergic, alpha-1/chemistry, Receptors, Adrenergic, alpha-1/metabolism, Receptors, G-Protein-Coupled/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 11:05
Dernière modification de la notice
20/08/2019 14:27
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