期刊
BIOLOGICAL CHEMISTRY
卷 393, 期 6, 页码 541-546出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2011-0284
关键词
beta 2-adrenergic receptor; ER export; G protein-coupled receptor; Rab GTPase; trafficking
资金
- Heart and Stroke Foundation of Nova Scotia [G-08-DU-3267]
- NSERC [EQPEQ-3591097-2008, RGPIN/355310-2008]
- Canada Foundation for Innovation
- Nova Scotia Health Research Foundation
- Canadian Institutes of Health Research
- Dalhousie Medical Research Foundation
Very little is understood about the trafficking of G protein-coupled receptors (GPCRs) from the endoplasmic reticulum (ER) to the plasma membrane. Rab guanosine triphosphatases (GTPases) are known to participate in the trafficking of various GPCRs via a direct interaction during the endocytic pathway, but whether this occurs in the anterograde pathway is unknown. We evaluated the potential interaction of Rab1, a GTPase known to regulate beta 2-adrenergic receptor (beta 2AR) trafficking, and its effect on export from the ER. Our results show that GTP-bound Rab1 interacts with the F(x)(6)LL motif of beta 2AR. Receptors lacking the interaction motif fail to traffic properly, suggesting that a direct interaction with Rab1 is required for beta 2AR anterograde trafficking.
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