Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Export

@article{citeulike:748015, abstract = {In the last four to five years, the view that G protein-coupled receptors (GPCRs) function as monomeric proteins has been challenged by numerous studies, which suggests that GPCRs exist as dimers or even higher-structure oligomers. Recently, biophysical methods based on luminescence and fluorescence energy transfer have confirmed the existence of such oligomeric complexes in living cells. Although no consensus exists on the role of receptor dimerization, converging evidence suggests potential roles in various aspects of receptor biogenesis and function. In several cases, receptors appear to fold as constitutive dimers early after biosynthesis, whereas ligand-promoted dimerization at the cell surface has been proposed for others. The reports of heterodimerization between receptor subtypes suggest a potential level of receptor complexity that could account for previously unexpected pharmacological diversities. In addition to fundamentally changing our views on the structure and activation processes of GPCRs, the concept of homo- and heterodimerization could have dramatic impacts on drug development and screening.}, address = {Department of Biochemistry and Groupe de Recherche sur le Syst\`{e}me Nerveux Autonome, Universit\'{e} de Montr\'{e}al, Montr\'{e}al, H3C 3J7, Canada. stephane.angers@umontreal.ca}, author = {Angers, S. and Salahpour, A. and Bouvier, M.}, citeulike-article-id = {748015}, citeulike-linkout-0 = {http://dx.doi.org/10.1146/annurev.pharmtox.42.091701.082314}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11807178}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11807178}, doi = {10.1146/annurev.pharmtox.42.091701.082314}, issn = {0362-1642}, journal = {Annu Rev Pharmacol Toxicol}, keywords = {bret, dimerization, fret, g-protein, gpcr, review}, pages = {409--435}, posted-at = {2006-07-08 18:30:45}, priority = {2}, title = {Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function.}, url = {http://dx.doi.org/10.1146/annurev.pharmtox.42.091701.082314}, volume = {42}, year = {2002} }

TY - JOUR ID - citeulike:748015 L3 - citeulike-article-id:748015 N2 - In the last four to five years, the view that G protein-coupled receptors (GPCRs) function as monomeric proteins has been challenged by numerous studies, which suggests that GPCRs exist as dimers or even higher-structure oligomers. Recently, biophysical methods based on luminescence and fluorescence energy transfer have confirmed the existence of such oligomeric complexes in living cells. Although no consensus exists on the role of receptor dimerization, converging evidence suggests potential roles in various aspects of receptor biogenesis and function. In several cases, receptors appear to fold as constitutive dimers early after biosynthesis, whereas ligand-promoted dimerization at the cell surface has been proposed for others. The reports of heterodimerization between receptor subtypes suggest a potential level of receptor complexity that could account for previously unexpected pharmacological diversities. In addition to fundamentally changing our views on the structure and activation processes of GPCRs, the concept of homo- and heterodimerization could have dramatic impacts on drug development and screening. JF - Annu Rev Pharmacol Toxicol SN - 0362-1642 AD - Department of Biochemistry and Groupe de Recherche sur le Système Nerveux Autonome, Université de Montréal, Montréal, H3C 3J7, Canada. stephane.angers@umontreal.ca EP - 435 TI - Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. VL - 42 SP - 409 KW - bret KW - dimerization KW - fret KW - g-protein KW - gpcr KW - review AU - Angers, S AU - Salahpour, A AU - Bouvier, M PY - 2002/// UR - http://dx.doi.org/10.1146/annurev.pharmtox.42.091701.082314 ER -