title: Rab1 interacts directly with the β2-adrenergic receptor to regulate receptor anterograde trafficking.
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.
authors.affiliation: Department of Pharmacology, Faculty of Medicine, Dalhousie University, 5850 College Street, PO Box 15000, Halifax B3H 4R2, NS, Canada.
authors.forename: Maha M
authors.initials: MM
authors.lastname: Hammad
authors.forename: Yi-Qun
authors.initials: YQ
authors.lastname: Kuang
authors.forename: Alexa
authors.initials: A
authors.lastname: Morse
authors.forename: Denis J
authors.initials: DJ
authors.lastname: Dupré
mesh_terms: D000242:Cyclic AMP / Q000096:biosynthesis; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D057809:HEK293 Cells; D006801:Humans; D011485:Protein Binding; D021381:Protein Transport; D018343:Receptors, Adrenergic, beta-2 / Q000378:metabolism*; D020761:rab1 GTP-Binding Proteins / Q000378:metabolism*
chemical_list: D018343:Receptors, Adrenergic, beta-2; D000242:Cyclic AMP; D020761:rab1 GTP-Binding Proteins