Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation

The idea that G-protein-coupled receptors (GPCRs) can function as dimers is now generally accepted. Although an increasing amount of data suggests that dinners represent the basic signaling unit for most, if not all, members of this receptor family, GPCR dimerization might also be necessary to pass quality-control checkpoints of the biosynthetic pathway of GPCRs. To date, this hypothesis has been demonstrated unambiguously only for a small number of receptors that must form heterodimers to be exported properly to the plasma membrane (referred to as obligatory heterodimers). However, increasing evidence suggests that homodimerization might have a similar role in the receptor maturation process for many GPCRs.