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GPCR Oligomerization: Contribution to Receptor Biogenesis

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Part of the book series: Subcellular Biochemistry ((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.

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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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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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Correspondence to Kathleen Van Craenenbroeck .

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Van Craenenbroeck, K. (2012). GPCR Oligomerization: Contribution to Receptor Biogenesis. In: Dupré, D., Hébert, T., Jockers, R. (eds) GPCR Signalling Complexes – Synthesis, Assembly, Trafficking and Specificity. Subcellular Biochemistry, vol 63. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4765-4_3

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