Identification of endoplasmic reticulum export motifs for G protein-coupled receptors

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Scopus citations


Coat protein complex II (COPII) vesicle-mediated protein export from the endoplasmic reticulum (ER) can be controlled by linear, independent motifs embedded within the cargo. ER export motifs directly interact with selective components of COPII vesicles and enhance cargo recruitment onto COPII vesicles. Moreover, ER export motifs are able to confer their transport abilities to other proteins. We have recently identified a novel ER export motif for α2B-adrenergic receptor (α2B-AR). This motif selectively interacts with Sec24C/D isoforms of COPII vesicles and facilitates α2B-AR export from the ER as well as transport to the cell surface. This motif can also mediate CD8 glycoprotein transport. These studies indicate that ER export of nascent G protein-coupled receptors (GPCRs) may be directed by specific codes that mediate receptor interaction with the ER-derived COPII vesicles. In this chapter, I discuss experimental approaches to identify ER export motifs for GPCRs by using α2B-AR as a model.

Original languageEnglish (US)
Title of host publicationG Protein Coupled ReceptorsTrafficking and Oligomerization
PublisherAcademic Press Inc.
Number of pages14
ISBN (Print)9780123918628
StatePublished - 2013

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


  • Anterograde transport
  • COPII vesicles
  • Cell surface expression
  • ER export motif
  • G protein-coupled receptor
  • Protein-protein interaction
  • Sec24

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Identification of endoplasmic reticulum export motifs for G protein-coupled receptors'. Together they form a unique fingerprint.

Cite this