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

Biol Chem. 2012 May;393(6):541-6. doi: 10.1515/hsz-2011-0284.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cyclic AMP / biosynthesis
  • Endoplasmic Reticulum / metabolism*
  • HEK293 Cells
  • Humans
  • Protein Binding
  • Protein Transport
  • Receptors, Adrenergic, beta-2 / metabolism*
  • rab1 GTP-Binding Proteins / metabolism*


  • Receptors, Adrenergic, beta-2
  • Cyclic AMP
  • rab1 GTP-Binding Proteins