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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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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