Reactome | ADRB3 bind ADR,NAd

ADRB3 bind ADR,NAd

Stable Identifier

R-HSA-9611852

Type

Reaction [binding]

Species

Homo sapiens

Compartment

extracellular region, plasma membrane

Synonyms

Beta-3 adrenoceptors bind catecholamines

ReviewStatus

5/5

Locations in the PathwayBrowser

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Signal Transduction (Homo sapiens)

- Signaling by GPCR (Homo sapiens)
  - GPCR ligand binding (Homo sapiens)
    - Class A/1 (Rhodopsin-like receptors) (Homo sapiens)
      - Amine ligand-binding receptors (Homo sapiens)
        
        Adrenoceptors (Homo sapiens)
        
        ADRB3 bind ADR,NAd (Homo sapiens)

General

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β-adrenergic receptors couple with G protein alpha-s subtype (Wenzel-Seifert K et al, 2002), increasing cAMP activity resulting in heart muscle contraction, smooth muscle relaxation and glycogenolysis. There are three β subtypes in humans; β1 found mainly in the heart and kidneys (Frielle et al. 1987), β2 found mainly in the lungs, vascular smooth muscle and skeletal muscle (Kobilka et al. 1987) and β3 found mainly in fat cells (Emorine et al. 1989). The catecholamines adrenaline (ADR) and noradrenaline (NaAd) are natural endogenous ligands that bind to β-adrenergic receptors and cause general physiological changes (increases in heart rate, blood pressure and glucose levels) that prepare the body for physical activity ('fight-or-flight response') (Tank & Lee Wong 2015).

Literature References

PubMed ID	Title	Journal	Year
2570461	Molecular characterization of the human beta 3-adrenergic receptor Emorine, LJ, Marullo, S, Briend-Sutren, MM, Patey, G, Tate, K, Delavier-Klutchko, C, Strosberg, AD	Science	1989
12106601	Similarities and differences in the coupling of human beta1- and beta2-adrenoceptors to Gs(alpha) splice variants Wenzel-Seifert, K, Liu, HY, Seifert, R	Biochem Pharmacol	2002
2825170	Cloning of the cDNA for the human beta 1-adrenergic receptor Frielle, T, Collins, S, Daniel, KW, Caron, MG, Lefkowitz, RJ, Kobilka, BK	Proc Natl Acad Sci U S A	1987
3025863	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 Kobilka, BK, Dixon, RA, Frielle, T, Dohlman, HG, Bolanowski, MA, Sigal, IS, Yang-Feng, TL, Francke, U, Caron, MG, Lefkowitz, RJ	Proc Natl Acad Sci U S A	1987