Article

Rab1 interacts directly with the β2-adrenergic receptor to regulate receptor anterograde trafficking.

Department of Pharmacology, Faculty of Medicine, Dalhousie University, 5850 College Street, PO Box 15000, Halifax B3H 4R2, NS, Canada.
Biological Chemistry (impact factor: 2.96). 05/2012; 393(6):541-6. DOI:10.1515/hsz-2011-0284 pp.541-6
Source: PubMed

ABSTRACT 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 β2-adrenergic receptor (β2AR) 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 β2AR. Receptors lacking the interaction motif fail to traffic properly, suggesting that a direct interaction with Rab1 is required for β2AR anterograde trafficking.

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Keywords

anterograde pathway
 
direct interaction
 
endocytic pathway
 
endoplasmic reticulum
 
G protein-coupled receptors
 
GTP-bound Rab1 interacts
 
interaction motif
 
potential interaction
 
Rab guanosine triphosphatases
 
Rab1
 
Receptors
 
trafficking
 
β2-adrenergic receptor
 
β2AR anterograde trafficking