G protein-coupled receptor (GPCR) export to the plasma membrane is considered to follow the default secretory pathway. Several observations indicate that traf ficking from the endoplasmic reticulum to the plasma membrane is strictly regulated and involves interactions with speci fic 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.
CITATION STYLE
Van Craenenbroeck, K. (2012). GPCR oligomerization: Contribution to receptor biogenesis. Subcellular Biochemistry, 63, 43–65. https://doi.org/10.1007/978-94-007-4765-4_3
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