Beta-2 adrenergic receptor

GWB-EEC334

Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.

Membrane; multi-pass membrane protein.

Phosphorylated by PKA and BARK; mediate homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.

Belongs to the G-protein coupled receptor 1 family [view classification]. Summary: This protein is beta-2-adrenergic receptor which is a member of the G protein-coupled receptor superfamily. This receptor is directly associated with one of its ultimate effectors the class C L-type calcium channel Ca(V)1. 2. This receptor-channel complex also contains a G protein an adenylyl cyclase cAMP-dependent kinase and the counterbalancing phosphatase PP2A. The assembly of the signaling complex provides a mechanism that ensures specific and rapid signaling by this G protein-coupled receptor. This protein contains no introns in either its coding or untranslated sequences. Different polymorphic forms point mutations and/or downregulation of this gene are associated with nocturnal asthma obesity and type 2 diabetes. [1] Zee R. Y. Cook N. R. Cheng S. Erlich H. A. Lindpaintner K. and Ridker P. M. Polymorphism in the beta2-adrenergic receptor and lipoprotein lipase genes as risk determinants for idiopathic venous thromboembolism: a multilocus population-based prospective genetic analysis[2] McGraw D. W. Mihlbachler K. A. Schwarb M. R. Rahman F. F. Small K. M. Almoosa K. F. and Liggett S. B. Airway smooth muscle prostaglandin-EP1 receptors directly modulate beta2-adrenergic receptors within a unique heterodimeric complex[3] Sotoodehnia N. Siscovick D. S. Vatta M. Psaty B. M. Tracy R. P. Towbin J. A. Lemaitre R. N. Rea T. D. Durda J. P. Chang J. M. et al. Beta2-adrenergic receptor genetic variants and risk of sudden cardiac death[4] Park J. S. Zhang S. Y. Jo S. H. Seo J. B. Li L. Park K. W. Oh B. H. Park Y. B. and Kim H. S. Common adrenergic receptor polymorphisms as novel risk factors for vasospastic angina[5] Spijker P. Vaidehi N. Freddolino P. L. Hilbers P. A. and Goddard W. A. III. Dynamic behavior of fully solvated beta2-adrenergic receptor embedded in the membrane with bound agonist or antagonist[6] Schofield P. R. Rhee L. M. Peralta E. G. Primary structure of the human beta-adrenergic receptor gene. [7] Kobilka B. K. Dixon R. A. F. Frielle T. Dohlman H. G. Bolanowski M. A. Sigal I. S. Yang-Feng T. L. Francke U. Caron M. G. Lefkowitz R. J. et al. cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor. [8] Chung F. -Z. Lentes K. -U. Gocayne J. D. M. G. Robinson D. A. Kerlavage A. R. Fraser C. M. Venter J. C. Cloning and sequence analysis of the human brain beta-adrenergic receptor. Evolutionary relationship to rodent and avian beta-receptors and porcine muscarinic receptors. [9] Emorine L. J. Marullo S. Delavier-Klutchko C. Kaveri S. V. Durieu-Trautmann O. Strosberg A. D. Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization. [10] Kobilka B. K. Frielle T. Dohlman H. G. Bolanowski M. A. Dixon R. A. F. Keller P. Caron M. G. Lefkowitz R. J. Delineation of the intronless nature of the genes for the human and hamster beta 2-adrenergic receptor and their putative promoter regions.