title: Functional consequences of 7TM receptor dimerization.
abstract: 7TM receptors work as signaling platforms that activate multiple signalling systems at the intracellular face of the plasma membrane. It is an emerging concept that 7TM receptors form homo- and hetero-dimers or -oligomers in vitro and in vivo. Numerous studies suggest dimerization is important for receptor function including agonist/antagonist affinity, efficacy, trafficking, and specificity of signal transduction, yet it remains unknown whether dimerization is a prerequisite for 7TM receptor signaling. The current review provides an overview of the biochemical support for 7TM homodimerization, followed by a discussion of the characteristics of homodimerization, with focus on dimer organization, and the functional consequences of dimerization. Heterodimerization will not generally be discussed in this review although we have included a few examples to illustrate specific points, and a table that summarises the current literature on this subject.
authors.affiliation: Laboratory of Molecular Cardiology, The Heart Centre and Copenhagen Heart Arrhythmia Research Centre (CHARC), Copenhagen University Hospital, Faculty of Health, University of Copenhagen, 20 Juliane Mariesvej, Denmark. jlhansen@molheart.dk
authors.forename: Jakob Lerche
authors.initials: JL
authors.lastname: Hansen
authors.forename: Søren P
authors.initials: SP
authors.lastname: Sheikh
mesh_terms: D000818:Animals; D019281:Dimerization; D006801:Humans; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000502:physiology
chemical_list: D043562:Receptors, G-Protein-Coupled; C450520:seven-transmembrane G-protein-coupled receptor