title: The functional size of GPCRs - monomers, dimers or tetramers?
abstract: In almost 16 years since the word "dimer" was used in a publication to describe the organization of G protein-coupled receptors (GPCRs), a large number of studies have since weighed in on this notion. Are native, functional GPCRs monomers, dimers or as some would suggest even higher order structures? Here, we review some of the latest evidence regarding the organization of these receptors in both homo- and hetero-oligomeric formats, with a particular focus on β-adrenergic receptors. This is particularly important for understanding the allosteric nature of receptor/receptor interactions. It is likely that, over the course of evolution, mechanisms have come into play using all of the possible variations in receptor/receptor stoichiometry, depending on the cell and the physiological context in question. Finally, we provide some data that suggests that higher order structures of GPCRs, as with dimers themselves are probably assembled in the ER.
authors.affiliation: Department of Pharmacology and Therapeutics, McGill University, Room 1303 McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montréal, QC, H3G 1Y6, Canada.
authors.forename: Darlaine
authors.initials: D
authors.lastname: Pétrin
authors.forename: Terence E
authors.initials: TE
authors.lastname: Hébert
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D060066:Protein Interaction Maps; D055503:Protein Multimerization; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism*
chemical_list: D043562:Receptors, G-Protein-Coupled