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GPCR Oligomerization: Contribution to Receptor Biogenesis

Chapter
First Online:
Part of the Subcellular Biochemistry book series (SCBI, volume 63)

Abstract

G protein-coupled receptor (GPCR) export to the plasma membrane is considered to follow the default secretory pathway. Several observations indicate that trafficking from the endoplasmic reticulum to the plasma membrane is strictly regulated and involves interactions with specific proteins, such as resident ER chaperones. These interactions help with GPCR folding, but more importantly, they ensure that only properly folded proteins proceed from the ER to the trans-golgi network. The assembly of several GPCRs into a quaternary structure is started in the ER, before cell surface delivery, and helps in the correct expression of the GPCRs. This review will mainly focus on the role of GPCR oligomerization in receptor biogenesis.

Keywords

G protein-coupled receptors Oligomerization Endoplasmic reticulum Chaperone Serotonin GABA Dopamine Adenosine Co-immunoprecipitation BRET FRET PLA Bivalent ligand 

List of Abbreviations

BiFC

bimolecular fluorescence complementation

BRET

bioluminescence resonance energy transfer

ER

endoplasmic reticulum

ERAD

endoplasmic reticulum associated degradation

FRET

fluorescence resonance energy transfer

GPCR

G protein-coupled receptor

TM

transmembrane domain

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Notes

Acknowledgments

KVC has a postdoctoral fellowship from FWO (Fonds voor Wetenschappelijk Onderzoek). Figures 3.1a and 3.2a were made by Evelien Gellynck, Fig. 3.3 by Dasiel Borroto-Escuela.

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© Springer Science+Business Media Dordrecht 2012

Authors and Affiliations

  1. 1.Laboratory of Eukaryotic Gene Expression and Signal Transduction (LEGEST)Ghent University-UGentGhentBelgium

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