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) 6LL 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.
Original language | English |
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Pages (from-to) | 541-546 |
Number of pages | 6 |
Journal | Biological Chemistry |
Volume | 393 |
Issue number | 6 |
DOIs | |
Publication status | Published - 1 May 2012 |
Keywords
- β2-adrenergic receptor
- ER export
- G protein-coupled receptor
- Rab GTPase
- trafficking