View source for Beta-2 adrenergic receptor

{{Infobox_gene}}
The '''beta-2 adrenergic receptor''' (β<sub>2</sub> adrenoreceptor), also known as '''ADRB2''', is a cell membrane-spanning [[beta-adrenergic receptor]] that interacts with ([[ligand binding|binds]]) [[epinephrine]], a hormone and [[neurotransmitter]] (ligand synonym, [[adrenaline]]) whose signaling, via [[adenylate cyclase]] stimulation through trimeric Gs proteins, increased [[Cyclic adenosine monophosphate|cAMP]], and downstream [[L-type calcium channel]] interaction, mediates physiologic responses such as [[Beta2-adrenergic agonist|smooth muscle relaxation and bronchodilation]].<ref name="pmid16387578">{{cite journal | vauthors = Johnson M | title = Molecular mechanisms of beta(2)-adrenergic receptor function, response, and regulation | journal = The Journal of Allergy and Clinical Immunology | volume = 117 | issue = 1 | pages = 18–24; quiz 25 | date = January 2006 | pmid = 16387578 | doi = 10.1016/j.jaci.2005.11.012 | doi-access = free }}</ref>

The official symbol for the human [[gene]] encoding the β<sub>2</sub> adrenoreceptor is ADRB2.<ref name="entrez">{{cite web | title = Entrez Gene: ADRB2 adrenoceptor beta 2, surface | url = https://www.ncbi.nlm.nih.gov/gene/154 | accessdate = 8 February 2015}}</ref>

==Gene==
The {{gene|ADRB2}} gene is [[intron]]less. Different polymorphic forms, [[point mutation]]s, and/or [[gene downregulation|downregulation]] of this gene are associated with nocturnal [[asthma]], [[obesity]] and [[type 2 diabetes]].<ref>{{cite web | title = Entrez Gene: ADRB2 adrenergic, beta-2-, receptor, surface| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=154| accessdate = }}</ref>

==Structure==
The 3D crystallographic structure (see figure and links to the right) of the β<sub>2</sub>-adrenergic receptor has been determined<ref name="Cherezov_2007">{{cite journal |vauthors=Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Kuhn P, Weis WI, Kobilka BK, Stevens RC | title = High-resolution crystal structure of an engineered human β<sub>2</sub>-adrenergic G protein-coupled receptor | journal = Science | volume = 318 | issue = 5854 | pages = 1258–65 | year = 2007 | pmid = 17962520 | doi = 10.1126/science.1150577 | issn = | pmc=2583103| bibcode = 2007Sci...318.1258C }}</ref><ref name="Rosenbaum_2007">{{cite journal |vauthors=Rosenbaum DM, Cherezov V, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Yao XJ, Weis WI, Stevens RC, Kobilka BK | title = GPCR engineering yields high-resolution structural insights into β<sub>2</sub>-adrenergic receptor function | journal = Science | volume = 318 | issue = 5854 | pages = 1266–73 | year = 2007 | pmid = 17962519 | doi = 10.1126/science.1150609 | issn = | bibcode = 2007Sci...318.1266R }}</ref><ref name="Rasmussen_2007">{{cite journal | vauthors = Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK | title = Crystal structure of the human beta2 adrenergic G-protein-coupled receptor | journal = Nature | volume = 450 | issue = 7168 | pages = 383–7  | date = Nov 2007 | pmid = 17952055 | doi = 10.1038/nature06325 | bibcode = 2007Natur.450..383R }}</ref> by making a [[fusion protein]] with [[lysozyme]] to increase the hydrophilic surface area of the protein for crystal contacts.  An alternative method, involving production of a fusion protein with an agonist, supported lipid-bilayer co-crystallization and generation of a 3.5 Å resolution structure.<ref>{{Cite journal|last=Liszewski|first=Kathy|date=1 October 2015|title=Dissecting the Structure of Membrane Proteins|url=http://www.genengnews.com/gen-articles/dissecting-the-structure-of-membrane-proteins/5583/|journal=[[Gen. Eng. Biotechnol. News|Genetic Engineering & Biotechnology News]]|volume=35|issue=17|page=16|type=paper}}{{subscription required}}</ref>

==Mechanism==
This receptor is directly associated with one of its ultimate effectors, the class C [[L-type calcium channel]] Ca<sub>V</sub>1.2. This receptor-channel complex is [[G protein-coupled receptor|coupled]] to the [[Gs alpha subunit|G<sub>s</sub>]] [[G protein]], which activates [[adenylyl cyclase]], catalysing the formation of [[cyclic adenosine monophosphate]] (cAMP) which then activates [[protein kinase A]], and counterbalancing [[phosphatase]] [[PP2A]]. Protein kinase A then goes on to phosphorylate (and thus inactivate) [[myosin light-chain kinase]], which causes smooth muscle relaxation, accounting for the vasodilatory effects of beta 2 stimulation. The assembly of the signaling complex provides a mechanism that ensures specific and rapid signaling. A two-state biophysical and molecular model has been proposed to account for the pH and REDOX sensitivity of this and other GPCRs.<ref name="pmid16574446">{{cite journal | vauthors = Rubenstein LA, Zauhar RJ, Lanzara RG | title = Molecular dynamics of a biophysical model for beta2-adrenergic and G protein-coupled receptor activation | journal = Journal of Molecular Graphics & Modelling | volume = 25 | issue = 4 | pages = 396–409  | date = Dec 2006 | pmid = 16574446 | doi = 10.1016/j.jmgm.2006.02.008 }}</ref>

Beta-2 adrenergic receptors have also been found to couple with [[Gi alpha subunit|G<sub>i</sub>]], possibly providing a mechanism by which response to ligand is highly localized within cells. In contrast, Beta-1 adrenergic receptors are coupled only to G<sub>s</sub>, and stimulation of these results in a more diffuse cellular response.<ref name="pmid11053129">{{cite journal | vauthors = Chen-Izu Y, Xiao RP, Izu LT, Cheng H, Kuschel M, Spurgeon H, Lakatta EG | title = G(i)-dependent localization of beta(2)-adrenergic receptor signaling to L-type Ca(2+) channels | journal = Biophysical Journal | volume = 79 | issue = 5 | pages = 2547–56 | date = Nov 2000 | pmid = 11053129 | pmc = 1301137 | doi = 10.1016/S0006-3495(00)76495-2 | bibcode = 2000BpJ....79.2547C }}</ref> This appears to be mediated by cAMP induced PKA phosphorylation of the receptor.<ref name="pmid12063255">{{cite journal | vauthors = Zamah AM, Delahunty M, Luttrell LM, Lefkowitz RJ | title = Protein kinase A-mediated phosphorylation of the beta 2-adrenergic receptor regulates its coupling to Gs and Gi. Demonstration in a reconstituted system | journal = The Journal of Biological Chemistry | volume = 277 | issue = 34 | pages = 31249–56 | date = Aug 2002 | pmid = 12063255 | doi = 10.1074/jbc.M202753200 }}</ref>

== Function ==
Actions of the β<sub>2</sub> receptor include:

===Muscular System===

{{clear|right}}
{|class="wikitable"
!Function
!Tissue
!Biological Role
|-
|rowspan=5|[[Smooth muscle]] relaxation in:
| [[GI tract]] (decreases motility)
| style="background: LemonChiffon"| Inhibition of [[digestion]]
|-
| [[Bronchi]]<ref name="purves">{{cite book | last1 = Fitzpatrick | first1 = David | last2 = Purves | first2 = Dale | last3 = Augustine | first3 = George | name-list-format = vanc | title = Neuroscience | publisher = Sinauer | location = Sunderland, Mass | year = 2004 | edition = Third | chapter =  Table 20:2 | pages = | isbn = 0-87893-725-0 | oclc = | doi = }}</ref> 
| style="background: LemonChiffon"|  Facilitation of [[respiration (physiology)|respiration]]. Hence, beta-2 agonists can be useful in treating [[asthma]].
|-
|[[Detrusor urinae muscle]] of [[Urinary bladder|bladder]] wall<ref name="pmid7540086">{{cite journal | vauthors = von Heyden B, Riemer RK, Nunes L, Brock GB, Lue TF, Tanagho EA | title = Response of guinea pig smooth and striated urethral sphincter to cromakalim, prazosin, nifedipine, nitroprusside, and electrical stimulation | journal = Neurourology and Urodynamics | volume = 14 | issue = 2 | pages = 153–68 | year = 1995 | pmid = 7540086 | doi = 10.1002/nau.1930140208 }}</ref><ref name="Moro et al. 2013">{{cite journal | vauthors = Moro C, Tajouri L, Chess-Williams R | title = Adrenoceptor function and expression in bladder urothelium and lamina propria | journal = Urology | volume = 81 | issue = 1 | pages = 211.e1–7 | date = January 2013 | pmid = 23200975 | doi = 10.1016/j.urology.2012.09.011 }}</ref> This effect is stronger than the [[alpha-1 receptor]] effect of contraction.
|Inhibition of need for [[micturition]]
|-
|[[Uterus]] 
|Inhibition of labor
|-
|[[Seminal tract]]<ref name=Rang163>{{cite book | vauthors = Rang HP |title=Pharmacology |publisher=Churchill Livingstone |location=Edinburgh |year=2003 |pages= |isbn=0-443-07145-4 |oclc= |doi=}} Page 163</ref>
|
|-
| Increased [[perfusion]] and [[vasodilation]]
|[[Blood vessels]] and [[arteries]] to [[skeletal muscle]] including the smaller [[Right coronary artery|coronary arteries]]<ref name=Rang270>{{cite book | vauthors = Rang HP |title=Pharmacology |publisher=Churchill Livingstone |location=Edinburgh |year=2003 |pages= |isbn=0-443-07145-4 |oclc= |doi=| page = 270}}</ref> and [[hepatic artery proper|hepatic artery]]
|rowspan=2 style="background: lemonchiffon"|Facilitation of muscle contraction and motility
|-
|Increased mass and contraction speed
|[[Striated muscle]]<ref name=Rang163/> 
|-
| [[Insulin]] and [[glucagon]] secretion
| Pancreas<ref>{{Cite journal|last=Philipson|first=L. H.|date=December 2002|title=beta-Agonists and metabolism|journal=The Journal of Allergy and Clinical Immunology|volume=110|issue=6 Suppl|pages=S313–317|issn=0091-6749|pmid=12464941|doi=10.1067/mai.2002.129702}}</ref>
|rowspan=2 style="background: LemonChiffon"| Increased blood [[glucose]] and uptake by skeletal muscle
|-
|[[Glycogenolysis]]<ref name=Rang163/>
|
|-
| Tremor
|Motor nerve terminals.<ref name=Rang163/> Tremor is mediated by [[Protein kinase A|PKA]] mediated facilitation of presynaptic [[Ca2+|Ca<sup>2+</sup>]] influx leading to acetylcholine release.
|| 
|-
|}
{|
|style="vertical-align:top;width:360px;"|'''Legend '''
{{legend|LemonChiffon|The function facilitates the [[fight-or-flight response]].
}}
|}

===Circulatory system===
* Heart muscle contraction
* increase [[cardiac output]] (minor degree compared to β<sub>1</sub>).
**Increases [[heart rate]] <ref name=purves/> in [[sinoatrial node]] (SA node) ([[chronotropic]] effect).
**Increases [[heart atrium|atrial]] [[cardiac muscle]] contractility. ([[inotropic]] effect).
**Increases contractility and [[cardiac muscle automaticity|automaticity]]<ref name=purves/> of [[heart ventricle|ventricular]] cardiac muscle.
*Dilate [[hepatic artery proper|hepatic artery]].
*Dilate [[arterioles]] to [[skeletal muscle]].

===Eye===
In the normal eye, beta-2 stimulation by [[salbutamol]] increases intraocular pressure via net:
* Increase in production of [[aqueous humour]] by the [[ciliary process]],
* Subsequent increased pressure-dependent uveoscleral outflow of humour, ''despite'' reduced drainage of humour via the [[Canal of Schlemm]].

In [[glaucoma]], drainage is reduced ( open-angle glaucoma) or blocked completely (closed-angle glaucoma). In such cases, beta-2 stimulation with its consequent increase in humour production is highly contra-indicated, and conversely, a topical beta-2 antagonist such as [[timolol]] may be employed.

===Digestive system===
* [[Glycogenolysis]] and [[gluconeogenesis]] in liver.<ref name=purves/>
* [[Glycogenolysis]] and [[lactic acid|lactate]] release in [[skeletal muscle]].<ref name=purves/>
* Contract [[sphincters]] of [[Gastrointestinal tract]].
* Thickened secretions from [[salivary gland]]s.<ref name=purves/>
*[[Insulin]] and [[glucagon]] secretion from pancreas. <ref>{{Cite journal|last=Philipson|first=L. H.|date=December 2002|title=beta-Agonists and metabolism|journal=The Journal of Allergy and Clinical Immunology|volume=110|issue=6 Suppl|pages=S313–317|issn=0091-6749|pmid=12464941|doi=10.1067/mai.2002.129702}}</ref>

===Other===
* Inhibit [[histamine]]-release from [[mast cells]].
* Increase protein content of secretions from [[lacrimal gland]]s.
* Receptor also present in [[cerebellum]].
* Bronchiole dilation (targeted while treating asthma attacks)
* Involved in brain - immune - communication <ref name="Elenkov">{{cite journal | vauthors = Elenkov IJ, Wilder RL, Chrousos GP, Vizi ES | title = The sympathetic nerve--an integrative interface between two supersystems: the brain and the immune system | journal = Pharmacological Reviews | volume = 52 | issue = 4 | pages = 595–638  | date = Dec 2000 | pmid = 11121511 | doi =  }}</ref>

==Agonists==
{{Infobox GPCR
| name                        = Beta-2 adrenergic receptor
| signal transduction         = Primary: [[Gs alpha subunit|G<sub>s</sub>]]<br />Secondary: [[Gi alpha subunit|G<sub>i/o</sub>]]
| primary endogenous agonists = [[epinephrine]], [[norepinephrine]]
| agonists                    = [[isoprenaline]], [[salbutamol]], [[salmeterol]], [[Beta2-adrenergic agonist#Types|others]]
| antagonists                 = [[carvedilol]], [[propranolol]], [[labetalol]], [[Beta blocker#Examples|others]]
| inverse agonists            = N/A
| PAMs                        = [[zinc|Zn<sup>2+</sup>]] (low concentrations)
| NAMs                        = [[zinc|Zn<sup>2+</sup>]] (high concentrations)
| IUPHAR Target ID            = 29
| DrugBank Polypeptides ID    = P07550
| HMDB Protein ID             = HMDBP01634
}}
{{Main|Beta2-adrenergic agonist|l1=Beta<sub>2</sub>-adrenergic agonist}}

===Spasmolytics used in [[asthma]] and [[Chronic obstructive pulmonary disease|COPD]]===
* Short-acting β<sub>2</sub> agonists (SABA)
** [[bitolterol]]
** [[fenoterol]]
** [[hexoprenaline]]
** [[isoprenaline]] <small>([[International Nonproprietary Name|INN]])</small> or isoproterenol <small>([[United States Adopted Name|USAN]])</small>
** [[levosalbutamol]] <small>([[International Nonproprietary Name|INN]])</small> or levalbuterol <small>([[United States Adopted Name|USAN]])</small>
** [[orciprenaline]] <small>([[International Nonproprietary Name|INN]])</small> or metaproterenol <small>([[United States Adopted Name|USAN]])</small>
** [[pirbuterol]]
** [[procaterol]]
** [[salbutamol]] <small>([[International Nonproprietary Name|INN]])</small> or albuterol <small>([[United States Adopted Name|USAN]])</small>
** [[terbutaline]]
* Long-acting β<sub>2</sub> agonists (LABA)
** [[arformoterol]] (some consider it to be an ultra-LABA)<ref>{{cite journal | vauthors = Matera MG, Cazzola M | title = ultra-long-acting beta2-adrenoceptor agonists: an emerging therapeutic option for asthma and COPD? | journal = Drugs | volume = 67 | issue = 4 | pages = 503–15 | date = 2007 | pmid = 17352511 | doi = 10.2165/00003495-200767040-00002 }}</ref>
** [[bambuterol]]
** [[clenbuterol]]
** [[formoterol]]
** [[salmeterol]]
* Ultra-long-acting β<sub>2</sub> agonists (ultra-LABA)
** [[carmoterol]]
** [[indacaterol]]
** [[milveterol]] (GSK 159797)
** [[olodaterol]]
** [[vilanterol]] (GSK 642444)

===[[Tocolytic]] agents===
* Short-acting β<sub>2</sub> agonists (SABA)
** [[fenoterol]]
** [[hexoprenaline]]
** [[isoxsuprine]]
** [[ritodrine]]
** [[salbutamol]] <small>([[International Nonproprietary Name|INN]])</small> or albuterol <small>([[United States Adopted Name|USAN]])</small>
** [[terbutaline]]

===β<sub>2</sub> agonists used for other purposes===
* [[zilpaterol]]

==Antagonists==
''([[Beta blocker]]s)''
*[[butoxamine]]*<ref name=Rang163/>
*[[Beta blocker#Nonselective agents|First generation (non-selective) β-blockers]]
*[[ICI-118,551]]*
*[[Propranolol]]

<nowiki>*</nowiki> denotes selective antagonist to the receptor.

== Interactions ==

Beta-2 adrenergic receptor has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[AKAP12]],<ref name = pmid11309381>{{cite journal | vauthors = Fan G, Shumay E, Wang H, Malbon CC | title = The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) binds the beta 2-adrenergic receptor via the receptor cytoplasmic Arg-329 to Leu-413 domain and provides a mobile scaffold during desensitization | journal = The Journal of Biological Chemistry | volume = 276 | issue = 26 | pages = 24005–14 | date = Jun 2001 | pmid = 11309381 | doi = 10.1074/jbc.M011199200 }}</ref><ref name = pmid9880537>{{cite journal | vauthors = Shih M, Lin F, Scott JD, Wang HY, Malbon CC | title = Dynamic complexes of beta2-adrenergic receptors with protein kinases and phosphatases and the role of gravin | journal = The Journal of Biological Chemistry | volume = 274 | issue = 3 | pages = 1588–95 | date = Jan 1999 | pmid = 9880537 | doi = 10.1074/jbc.274.3.1588 }}</ref> 
* [[Delta Opioid receptor|OPRD1]],<ref name = pmid11278447>{{cite journal | vauthors = McVey M, Ramsay D, Kellett E, Rees S, Wilson S, Pope AJ, Milligan G | title = Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy | journal = The Journal of Biological Chemistry | volume = 276 | issue = 17 | pages = 14092–9 | date = Apr 2001 | pmid = 11278447 | doi = 10.1074/jbc.M008902200 }}</ref> 
* [[Grb2]],<ref name = pmid9830057>{{cite journal | vauthors = Karoor V, Wang L, Wang HY, Malbon CC | title = Insulin stimulates sequestration of beta-adrenergic receptors and enhanced association of beta-adrenergic receptors with Grb2 via tyrosine 350 | journal = The Journal of Biological Chemistry | volume = 273 | issue = 49 | pages = 33035–41 | date = Dec 1998 | pmid = 9830057 | doi = 10.1074/jbc.273.49.33035 }}</ref>
* [[SNX27]]<ref name = pmid21602791>{{cite journal | vauthors = Temkin P, Lauffer B, Jäger S, Cimermancic P, Krogan NJ, von Zastrow M | title = SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors | journal = Nature Cell Biology | volume = 13 | issue = 6 | pages = 715–21 | date = Jun 2011 | pmid = 21602791 | pmc = 3113693 | doi = 10.1038/ncb2252 }}</ref>  and
* [[Sodium-hydrogen antiporter 3 regulator 1|SLC9A3R1]].<ref name = pmid11882663>{{cite journal | vauthors = Karthikeyan S, Leung T, Ladias JA | title = Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors | journal = The Journal of Biological Chemistry | volume = 277 | issue = 21 | pages = 18973–8 | date = May 2002 | pmid = 11882663 | doi = 10.1074/jbc.M201507200 }}</ref><ref name = pmid9671706>{{cite journal | vauthors = Hall RA, Ostedgaard LS, Premont RT, Blitzer JT, Rahman N, Welsh MJ, Lefkowitz RJ | title = A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 15 | pages = 8496–501 | date = Jul 1998 | pmid = 9671706 | pmc = 21104 | doi = 10.1073/pnas.95.15.8496 |bibcode = 1998PNAS...95.8496H }}</ref><ref name = pmid9560162>{{cite journal | vauthors = Hall RA, Premont RT, Chow CW, Blitzer JT, Pitcher JA, Claing A, Stoffel RH, Barak LS, Shenolikar S, Weinman EJ, Grinstein S, Lefkowitz RJ | title = The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange | journal = Nature | volume = 392 | issue = 6676 | pages = 626–30 | date = Apr 1998 | pmid = 9560162 | doi = 10.1038/33458 |bibcode = 1998Natur.392..626H }}</ref> 
{{Div col end}}

== See also ==
*Other [[adrenergic receptors]]
**[[Alpha-1 adrenergic receptor]]
**[[Alpha-2 adrenergic receptor]]
**[[Beta-1 adrenergic receptor]]
**[[Beta-3 adrenergic receptor]]
* [[Discovery and development of beta2 agonists]]

== References ==
{{Reflist|32em}}

== Further reading ==
{{refbegin|32em}}
* {{cite journal | vauthors = Frielle T, Caron MG, Lefkowitz RJ | title = Properties of the beta 1- and beta 2-adrenergic receptor subtypes revealed by molecular cloning | journal = Clinical Chemistry | volume = 35 | issue = 5 | pages = 721–5  | date = May 1989 | pmid = 2541947 | doi =  }}
* {{cite journal | vauthors = Taylor DR, Kennedy MA | title = Genetic variation of the beta(2)-adrenoceptor: its functional and clinical importance in bronchial asthma | journal = American Journal of Pharmacogenomics | volume = 1 | issue = 3 | pages = 165–74 | year = 2002 | pmid = 12083965 | doi = 10.2165/00129785-200101030-00002 }}
* {{cite journal | vauthors = Thibonnier M, Coles P, Thibonnier A, Shoham M | title = Molecular pharmacology and modeling of vasopressin receptors | journal = Progress in Brain Research | volume = 139 | issue =  | pages = 179–96 | year = 2002 | pmid = 12436935 | doi = 10.1016/S0079-6123(02)39016-2 }}
* {{cite journal | vauthors = Ge D, Huang J, He J, Li B, Duan X, Chen R, Gu D | title = beta2-Adrenergic receptor gene variations associated with stage-2 hypertension in northern Han Chinese | journal = Annals of Human Genetics | volume = 69 | issue = Pt 1 | pages = 36–44  | date = Jan 2005 | pmid = 15638826 | doi = 10.1046/j.1529-8817.2003.00093.x }}
* {{cite journal | vauthors = Muszkat M | title = Interethnic differences in drug response: the contribution of genetic variability in beta adrenergic receptor and cytochrome P4502C9 | journal = Clinical Pharmacology and Therapeutics | volume = 82 | issue = 2 | pages = 215–8  | date = Aug 2007 | pmid = 17329986 | doi = 10.1038/sj.clpt.6100142 }}
* {{cite journal | vauthors = von Zastrow M, Kobilka BK | title = Ligand-regulated internalization and recycling of human beta 2-adrenergic receptors between the plasma membrane and endosomes containing transferrin receptors | journal = The Journal of Biological Chemistry | volume = 267 | issue = 5 | pages = 3530–8  | date = Feb 1992 | pmid = 1371121 | doi =  }}
* {{cite journal | vauthors = Gope R, Gope ML, Thorson A, Christensen M, Smyrk T, Chun M, Alvarez L, Wildrick DM, Boman BM | title = Genetic changes at the beta-2-adrenergic receptor locus on chromosome 5 in human colorectal carcinomas | journal = Anticancer Research | volume = 11 | issue = 6 | pages = 2047–50 | year = 1992 | pmid = 1663718 | doi =  }}
* {{cite journal | vauthors = Bouvier M, Guilbault N, Bonin H | title = Phorbol-ester-induced phosphorylation of the beta 2-adrenergic receptor decreases its coupling to Gs | journal = FEBS Letters | volume = 279 | issue = 2 | pages = 243–8  | date = Feb 1991 | pmid = 1848190 | doi = 10.1016/0014-5793(91)80159-Z }}
* {{cite journal | vauthors = Yang-Feng TL, Xue FY, Zhong WW, Cotecchia S, Frielle T, Caron MG, Lefkowitz RJ, Francke U | title = Chromosomal organization of adrenergic receptor genes | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 87 | issue = 4 | pages = 1516–20  | date = Feb 1990 | pmid = 2154750 | pmc = 53506 | doi = 10.1073/pnas.87.4.1516 | bibcode = 1990PNAS...87.1516Y }}
* {{cite journal | vauthors = Hui KK, Yu JL | title = Effects of protein kinase inhibitor, 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine, on beta-2 adrenergic receptor activation and desensitization in intact human lymphocytes | journal = The Journal of Pharmacology and Experimental Therapeutics | volume = 249 | issue = 2 | pages = 492–8  | date = May 1989 | pmid = 2470898 | doi =  }}
* {{cite journal | vauthors = Hen R, Axel R, Obici S | title = Activation of the beta 2-adrenergic receptor promotes growth and differentiation in thyroid cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 12 | pages = 4785–8  | date = Jun 1989 | pmid = 2471981 | pmc = 287358 | doi = 10.1073/pnas.86.12.4785 | bibcode = 1989PNAS...86.4785H }}
* {{cite journal | vauthors = O'Dowd BF, Hnatowich M, Caron MG, Lefkowitz RJ, Bouvier M | title = Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor | journal = The Journal of Biological Chemistry | volume = 264 | issue = 13 | pages = 7564–9  | date = May 1989 | pmid = 2540197 | doi =  }}
* {{cite journal | vauthors = Bristow MR, Hershberger RE, Port JD, Minobe W, Rasmussen R | title = Beta 1- and beta 2-adrenergic receptor-mediated adenylate cyclase stimulation in nonfailing and failing human ventricular myocardium | journal = Molecular Pharmacology | volume = 35 | issue = 3 | pages = 295–303  | date = Mar 1989 | pmid = 2564629 | doi =  }}
* {{cite journal | vauthors = Emorine LJ, Marullo S, Delavier-Klutchko C, Kaveri SV, Durieu-Trautmann O, Strosberg AD | title = Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 20 | pages = 6995–9  | date = Oct 1987 | pmid = 2823249 | pmc = 299215 | doi = 10.1073/pnas.84.20.6995 | bibcode = 1987PNAS...84.6995E }}
* {{cite journal | vauthors = Chung FZ, Wang CD, Potter PC, Venter JC, Fraser CM | title = Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation | journal = The Journal of Biological Chemistry | volume = 263 | issue = 9 | pages = 4052–5  | date = Mar 1988 | pmid = 2831218 | doi =  }}
* {{cite journal | vauthors = Yang SD, Fong YL, Benovic JL, Sibley DR, Caron MG, Lefkowitz RJ | title = Dephosphorylation of the beta 2-adrenergic receptor and rhodopsin by latent phosphatase 2 | journal = The Journal of Biological Chemistry | volume = 263 | issue = 18 | pages = 8856–8  | date = Jun 1988 | pmid = 2837466 | doi =  }}
* {{cite journal | vauthors = Kobilka BK, Dixon RA, Frielle T, Dohlman HG, Bolanowski MA, Sigal IS, Yang-Feng TL, Francke U, Caron MG, Lefkowitz RJ | title = 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 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 1 | pages = 46–50  | date = Jan 1987 | pmid = 3025863 | pmc = 304138 | doi = 10.1073/pnas.84.1.46 | bibcode = 1987PNAS...84...46K }}
* {{cite journal | vauthors = Chung FZ, Lentes KU, Gocayne J, Fitzgerald M, Robinson D, Kerlavage AR, Fraser CM, Venter JC | title = Cloning and sequence analysis of the human brain beta-adrenergic receptor. Evolutionary relationship to rodent and avian beta-receptors and porcine muscarinic receptors | journal = FEBS Letters | volume = 211 | issue = 2 | pages = 200–6  | date = Jan 1987 | pmid = 3026848 | doi = 10.1016/0014-5793(87)81436-9 }}
{{refend}}

== External links ==
* {{cite web | url = http://www.iuphar-db.org/GPCR/ReceptorDisplayForward?receptorID=2189 | title = &beta;<sub>2</sub>-adrenoceptor  | accessdate = | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | pages = | archiveurl = | archivedate = }}
* {{UCSC gene info|ADRB2}}

{{G protein-coupled receptors|g1}}

[[Category:Adrenergic receptors]]