MT<sub>2</sub> receptor | Melatonin receptors | IUPHAR/BPS Guide to PHARMACOLOGY

MT2 receptor

Target id: 288

Nomenclature: MT2 receptor

Family: Melatonin receptors

Annotation status:  image of a green circle Annotated and expert reviewed. Please contact us if you can help with updates.  » Email us

   GtoImmuPdb view: OFF :     Currently no data for MT2 receptor in GtoImmuPdb

Gene and Protein Information
class A G protein-coupled receptor
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human 7 362 11q21-q22 MTNR1B melatonin receptor 1B 49-50
Mouse 7 364 9 A2 Mtnr1b melatonin receptor 1B 30
Rat 7 364 8q12 Mtnr1b melatonin receptor 1B 3
Gene and Protein Information Comments
The ovine MT2 receptor has been shown to present 72% identity with the human receptor [13].
Previous and Unofficial Names
mel1b receptor
Database Links
Specialist databases
GPCRDB mtr1b_human (Hs), mtr1b_mouse (Mm)
Other databases
ChEMBL Target
DrugBank Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Gene
OMIM
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Associated Proteins
Interacting Proteins
Name Effect References
MT1 receptor 5-6
GPR50 36
Natural/Endogenous Ligands
melatonin

Download all structure-activity data for this target as a CSV file

Agonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
[125I]SD6 Hs Full agonist 10.2 pKd 35
pKd 10.2 (Kd 6.6x10-11 M) [35]
2-[125I]melatonin Hs Full agonist 9.7 – 10.0 pKd 4,22
pKd 9.7 – 10.0 (Kd 1.86x10-10 – 1.07x10-10 M) [4,22]
[125I]DIV880 Hs Partial agonist 9.7 pKd 35
pKd 9.7 (Kd 2.24x10-10 M) [35]
[125I]S70254 Hs Partial agonist 9.6 pKd 35
pKd 9.6 [35]
[3H]melatonin Hs Full agonist 9.0 – 9.6 pKd 10
pKd 9.0 – 9.6 (Kd 9.12x10-10 – 2.8x10-10 M) [10]
UCM1014 Hs Full agonist 12.0 pKi 59
pKi 12.0 (Ki 1x10-12 M) [59]
isoamyl-agomelatine Hs Partial agonist 11.0 pKi 26
pKi 11.0 [26]
CIFEA Hs Full agonist 10.9 pKi 32
pKi 10.9 [32]
LY 156735 Hs Full agonist 10.4 pKi 42
pKi 10.4 [42]
IIK7 Hs Full agonist 10.3 pKi 27,60
pKi 10.3 (Ki 5x10-11 M) [27,60]
IIK7 Mm Full agonist 10.3 pKi 7
pKi 10.3 (Ki 5.2x10-11 M) [7]
agomelatine Hs Full agonist 9.9 – 10.5 pKi 4,8
pKi 9.9 – 10.5 [4,8]
tasimelteon Hs Full agonist 10.2 pKi 64
pKi 10.2 (Ki 6.92x10-11 M) [64]
UCM 765 Hs Full agonist 10.2 pKi 51
pKi 10.2 [51]
2-iodo-melatonin Hs Full agonist 9.7 – 10.3 pKi 4,8,19,22
pKi 9.7 – 10.3 [4,8,19,22]
ramelteon Hs Full agonist 10.0 pKi 31,48
pKi 10.0 [31,48]
GR 196429 Hs Full agonist 9.7 – 9.8 pKi 8,10
pKi 9.7 – 9.8 [8,10]
melatonin Hs Full agonist 9.4 – 9.8 pKi 4,19,22
pKi 9.4 – 9.8 [4,19,22]
6-Cl-MLT Hs Full agonist 9.4 – 9.8 pKi 4,8,19,22
pKi 9.4 – 9.8 [4,8,19,22]
S24014 Hs Partial agonist 9.6 pKi 4
pKi 9.6 [4]
5-methoxy-luzindole Hs Partial agonist 9.6 pKi 22
pKi 9.6 (Ki 2.5x10-10 M) [22]
BOMPPA Hs Full agonist 9.5 pKi 28
pKi 9.5 [28]
S24773 Hs Partial agonist 9.3 – 9.6 pKi 4
pKi 9.3 – 9.6 [4]
EFPPEA Hs Full agonist 9.4 pKi 33
pKi 9.4 [33]
UCM 793 Hs Full agonist 9.2 pKi 51
pKi 9.2 [51]
GR 128107 Hs Partial agonist 8.6 – 9.1 pKi 22,63
pKi 8.6 – 9.1 [22,63]
6-hydroxymelatonin Hs Full agonist 8.3 – 8.8 pKi 10,19,22
pKi 8.3 – 8.8 [10,19,22]
S22153 Hs Partial agonist 8.1 – 8.2 pKi 4
pKi 8.1 – 8.2 [4]
S26284 Hs Partial agonist 6.8 – 7.2 pKi 4
pKi 6.8 – 7.2 [4]
View species-specific agonist tables
Agonist Comments
The partial agonists DIV880 and S70254 are the first reported selective ligands for the MT2 receptor subtype [35]. The partial antagonist GR 128107 has also been classed as an antagonist.
Antagonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
(hydroxymethylphenyl)agomelatine Hs Antagonist 9.4 pKi 47
pKi 9.4 (Ki 3.6x10-10 M) [47]
K185 Hs Antagonist 9.3 pKi 27,60
pKi 9.3 (Ki 5.1x10-10 M) [27,60]
4P-PDOT Hs Antagonist 8.8 – 9.4 pKi 4,22,24
pKi 8.8 – 9.4 (Ki 1.58x10-9 – 3.9x10-10 M) [4,22,24]
UCM 549 Hs Antagonist 8.9 – 9.2 pKi 38,58
pKi 8.9 – 9.2 [38,58]
2-(indolin-1yl)-melatonin Hs Antagonist 8.9 pKi 66
pKi 8.9 [66]
UCM 454 Hs Antagonist 8.1 pKi 52
pKi 8.1 [52]
DH97 Hs Antagonist 8.0 pKi 62
pKi 8.0 (Ki 1x10-8 M) [62]
UCM 724 Hs Antagonist 8.0 pKi 38
pKi 8.0 [38]
luzindole Hs Antagonist 7.6 – 8.1 pKi 4,10,20,22,24
pKi 7.6 – 8.1 [4,10,20,22,24]
S20928 Hs Antagonist 7.1 – 7.2 pKi 4
pKi 7.1 – 7.2 [4]
5-HEAT Hs Antagonist 7.1 pKi 45
pKi 7.1 [45]
S26131 Hs Antagonist 6.8 – 7.0 pKi 4
pKi 6.8 – 7.0 [4]
Primary Transduction Mechanisms
Transducer Effector/Response
Gi/Go family Adenylate cyclase inhibition
Phospholipase C stimulation
References:  23,29,39,41,49
Secondary Transduction Mechanisms
Transducer Effector/Response
Other - See Comments
Comments:  Guanylate cyclase inhibition.
References:  46
Tissue Distribution
Hippocampus.
Species:  Human
Technique:  immunocytochemistry.
References:  55
Fetal kidney.
Species:  Human
Technique:  RT-PCR.
References:  18
Uveal melanocytes and melanoma cells.
Species:  Human
Technique:  RT-PCR.
References:  53
Cerebellum.
Species:  Human
Technique:  in situ hybridisation.
References:  1
Brown and white adipose tissue, PAZ6 adipocytes.
Species:  Human
Technique:  RT-PCR.
References:  11
Granulosa cells.
Species:  Human
Technique:  RT-PCR.
References:  44,57
Placental tissues and choriocarcinoma cell lines.
Species:  Human
Technique:  RT-PCR, Western blotting and confocal microscopy.
References:  34
Retina.
Species:  Human
Technique:  RT-PCR.
References:  49
Brain, lung.
Species:  Mouse
Technique:  RT-PCR.
References:  43
Retina.
Species:  Mouse
Technique:  In situ hybridisation
References:  14
Hypothalamus, retina, small intestine > liver, heart SA node.
Species:  Rat
Technique:  RT-PCR.
References:  54
Expression Datasets

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Log average relative transcript abundance in mouse tissues measured by qPCR from Regard, J.B., Sato, I.T., and Coughlin, S.R. (2008). Anatomical profiling of G protein-coupled receptor expression. Cell, 135(3): 561-71. [PMID:18984166] [Raw data: website]

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Functional Assays
Measurement of cAMP levels in CHO cells transfected with the human MT2 receptor.
Species:  Human
Tissue:  CHO cells.
Response measured:  Inhibition of cAMP accumulation.
References:  10,31
Measurement of cAMP levels in NIH 3T3 cells transfected with the human MT2 receptor.
Species:  Human
Tissue:  NIH 3T3 cells.
Response measured:  Inhibition of cAMP accumulation.
References:  27
Measurement of [35S]GTPγS binding in CHO cells transfected with the human MT2 receptor.
Species:  Human
Tissue:  CHO cells.
Response measured:  [35S]GTPγS binding.
References:  4
Measurement of [35S]GTPγS binding in NIH 3T3 cells transfected with the human MT2 receptor.
Species:  Human
Tissue:  NIH 3T3 cells.
Response measured:  [35S]GTPγS binding.
References:  45
Measurement of melatonin-mediated vasodilation in rat caudal arteries.
Species:  Rat
Tissue:  Caudal artery.
Response measured:  Vasodilation.
References:  15,40
Measurement of phase advance circadian rhythm neuronal firing in the mouse suprachiasmatic nucleus.
Species:  Mouse
Tissue:  Suprachiasmatic nucleus slice.
Response measured:  Phase shift of peak neuronal activity.
References:  21,37,48
Physiological Functions
Increase in splenic lymphocyte proliferation.
Species:  Mouse
Tissue:  Splenocytes.
References:  16-17
Inhibition of proliferation.
Species:  Human
Tissue:  Choriocarcinoma JAr Cells.
References:  56
Physiological Consequences of Altering Gene Expression
MT2 receptor knockout mice do not exhibit melatonin-mediated hippocampal LTP, as seen in wild-type mice.
Species:  Mouse
Tissue: 
Technique:  Transgenesis.
References:  65
MT2 receptor knockout mice do not exhibit luzindole-mediated antidepressant-like actions, as seen in wild-type mice.
Species:  Mouse
Tissue: 
Technique:  Transgenesis.
References:  61
Phenotypes, Alleles and Disease Models Mouse data from MGI

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Allele Composition & genetic background Accession Phenotype Id Phenotype Reference
Mtnr1btm1Drw Mtnr1btm1Drw/Mtnr1btm1Drw
C3.129S4-Mtnr1b
MGI:2181726  MP:0002169 no abnormal phenotype detected PMID: 12529409 
Clinically-Relevant Mutations and Pathophysiology
Disease:  Diabetes mellitus, noninsulin-dependent; NIDDM
Synonyms: Diabetes mellitus, Type II; T2D [OMIM: 125853]
Maturity onset diabetes
Type 2 diabetes mellitus [Disease Ontology: DOID:9352]
Disease Ontology: DOID:9352
OMIM: 125853
Role: 
Click column headers to sort
Type Species Amino acid change Nucleotide change Description Reference
Missense Human A42P Very rare variant identified in type 2 diabetes patients, associated with type 2 diabetes risk, no melatonin binding and signaling 9
Missense Human L60R Very rare variant identified in control population and type 2 diabetes patients, associated with type 2 diabetes risk, no melatonin binding and signaling 2,9
Missense Human P95L Very rare variant identified in type 2 diabetes patients, associated with type 2 diabetes risk, no melatonin binding and signaling 9
Missense Human Y308S Very rare variant identified in type 2 diabetes patients, associated with type 2 diabetes risk, no melatonin binding and signaling 9
Biologically Significant Variants
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  R330W
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, without obvious functional defect
Amino acid change:  A342V
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  A359E
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients and control population, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  I353T
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  L166I
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in population with impaired fasting glucose and control population without obvious functional defect
Amino acid change:  M120I
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  R316H
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, without obvious functional defect
Amino acid change:  S238G
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Common variant, not associated with type 2 diabetes risk
Amino acid change:  K243R
Nucleotide accession: 
Protein accession: 
References:  2,9,12
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  A234T
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  E237K
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, without obvious functional defect
Amino acid change:  D246N
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, without obvious functional defect
Amino acid change:  P36S
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  A8S
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients with impaired ERK1/2 activation
Amino acid change:  F250V
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  R330Q
Nucleotide accession: 
Protein accession: 
References:  12
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  R138H
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  W22L
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  G21S
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  A13V
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  A25T
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Common variant, not associated with type 2 diabetes risk but associated with prevalence of obesity and increased BMI shown in one study but not in another
Amino acid change:  G24E
Nucleotide accession: 
Protein accession: 
References:  2,9,12,25
Type:  Missense mutation
Species:  Human
Description:  Rare variant, not associated with type 2 diabetes risk
Amino acid change:  R231H
Nucleotide accession: 
Protein accession: 
References:  2,9,12
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  M146V
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  M120V
Nucleotide accession: 
Protein accession: 
References:  9,12
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in population with impaired fasting glucose and control population without obvious functional defect
Amino acid change:  S123R
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  R222H
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, without obvious functional defect
Amino acid change:  I223T
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, without obvious functional defect
Amino acid change:  Y141F
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, without obvious functional defect
Amino acid change:  T201M
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in type 2 diabetes patients, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  A52T
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population and type 2 diabetes patients without obvious functional defect
Amino acid change:  R154H
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  R138L
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Rare variant, not associated with type 2 diabetes risk, no Gi and ERK1/2 activation
Amino acid change:  R138C
Nucleotide accession: 
Protein accession: 
References:  2,9,12
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in several populations including type 2 diabetes and ADSD without obvious functional defect in one study and impaired ERK1/2 activation in another
Amino acid change:  V124I
Nucleotide accession: 
Protein accession: 
References:  2,9,12
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  G109A
Nucleotide accession: 
Protein accession: 
References:  9
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population without obvious functional defect
Amino acid change:  L66F
Nucleotide accession: 
Protein accession: 
References:  25
Type:  Missense mutation
Species:  Human
Description:  Very rare variant identified in control population and type 2 diabetes patients, associated with type 2 diabetes risk, impaired Gi protein activation
Amino acid change:  A74T
Nucleotide accession: 
Protein accession: 
References:  9

References

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1. Al-Ghoul WM, Herman MD, Dubocovich ML. (1998) Melatonin receptor subtype expression in human cerebellum. Neuroreport, 9: 4063-4068. [PMID:9926848]

2. Andersson EA, Holst B, Sparsø T, Grarup N, Banasik K, Holmkvist J, Jørgensen T, Borch-Johnsen K, Egerod KL, Lauritzen T et al.. (2010) MTNR1B G24E variant associates With BMI and fasting plasma glucose in the general population in studies of 22,142 Europeans. Diabetes, 59 (6): 1539-48. [PMID:20200315]

3. Audinot V, Bonnaud A, Grandcolas L, Rodriguez M, Nagel N, Galizzi JP, Balik A, Messager S, Hazlerigg DG, Barrett P et al.. (2008) Molecular cloning and pharmacological characterization of rat melatonin MT1 and MT2 receptors. Biochem. Pharmacol., 75 (10): 2007-19. [PMID:18384758]

4. Audinot V, Mailliet F, Lahaye-Brasseur C, Bonnaud A, Le Gall A, Amossé C, Dromaint S, Rodriguez M, Nagel N, Galizzi JP, Malpaux B, Guillaumet G, Lesieur D, Lefoulon F, Renard P, Delagrange P, Boutin JA. (2003) New selective ligands of human cloned melatonin MT1 and MT2 receptors. Naunyn Schmiedebergs Arch Pharmacol, 367: 553-561. [PMID:12764576]

5. Ayoub MA, Couturier C, Lucas-Meunier E, Angers S, Fossier P, Bouvier M, Jockers R. (2002) Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J. Biol. Chem., 277 (24): 21522-8. [PMID:11940583]

6. Ayoub MA, Levoye A, Delagrange P, Jockers R. (2004) Preferential formation of MT1/MT2 melatonin receptor heterodimers with distinct ligand interaction properties compared with MT2 homodimers. Mol. Pharmacol., 66 (2): 312-21. [PMID:15266022]

7. Baba K, Benleulmi-Chaachoua A, Journé AS, Kamal M, Guillaume JL, Dussaud S, Gbahou F, Yettou K, Liu C, Contreras-Alcantara S et al.. (2013) Heteromeric MT1/MT2 melatonin receptors modulate photoreceptor function. Sci Signal, 6 (296): ra89. [PMID:24106342]

8. Beresford IJ, Browning C, Starkey SJ, Brown J, Foord SM, Coughlan J, North PC, Dubocovich ML, Hagan RM. (1998) GR196429: a nonindolic agonist at high-affinity melatonin receptors. J Pharmacol Exp Ther, 285: 1239-1245. [PMID:9618428]

9. Bonnefond A, Clément N, Fawcett K, Yengo L, Vaillant E, Guillaume JL, Dechaume A, Payne F, Roussel R, Czernichow S et al.. (2012) Rare MTNR1B variants impairing melatonin receptor 1B function contribute to type 2 diabetes. Nat. Genet., 44 (3): 297-301. [PMID:22286214]

10. Browning C, Beresford I, Fraser N, Giles H. (2000) Pharmacological characterization of human recombinant melatonin mt(1) and MT(2) receptors. Br. J. Pharmacol., 129: 877-886. [PMID:10696085]

11. Brydon L, Petit L, Delagrange P, Strosberg AD, Jockers R. (2001) Functional expression of MT2 (Mel1b) melatonin receptors in human PAZ6 adipocytes. Endocrinology, 142: 4264-4271. [PMID:11564683]

12. Chaste P, Clement N, Mercati O, Guillaume JL, Delorme R, Botros HG, Pagan C, Périvier S, Scheid I, Nygren G, Anckarsäter H, Rastam M, Ståhlberg O, Gillberg C, Serrano E, Lemière N, Launay JM, Mouren-Simeoni MC, Leboyer M, Gillberg C, Jockers R, Bourgeron T. (2010) Identification of pathway-biased and deleterious melatonin receptor mutants in autism spectrum disorders and in the general population. PLoS ONE, 5 (7): e11495. [PMID:20657642]

13. Cogé F, Guenin SP, Fery I, Migaud M, Devavry S, Slugocki C, Legros C, Ouvry C, Cohen W, Renault N et al.. (2009) The end of a myth: cloning and characterization of the ovine melatonin MT(2) receptor. Br. J. Pharmacol., 158 (5): 1248-62. [PMID:19814723]

14. Contreras-Alcantara S, Baba K, Tosini G. (2010) Removal of melatonin receptor type 1 induces insulin resistance in the mouse. Obesity (Silver Spring), 18 (9): 1861-3. [PMID:20168308]

15. Doolen S, Krause DN, Dubocovich ML, Duckles SP. (1998) Melatonin mediates two distinct responses in vascular smooth muscle. Eur J Pharmacol, 345: 67-69. [PMID:9593596]

16. Drazen DL, Bilu D, Bilbo SD, Nelson RJ. (2001) Melatonin enhancement of splenocyte proliferation is attenuated by luzindole, a melatonin receptor antagonist. Am J Physiol Regul Integr Comp Physiol, 280: R1476-R1482. [PMID:11294771]

17. Drazen DL, Nelson RJ. (2001) Melatonin receptor subtype MT2 (Mel 1b) and not mt1 (Mel 1a) is associated with melatonin-induced enhancement of cell-mediated and humoral immunity. Neuroendocrinology, 74: 178-184. [PMID:11528219]

18. Drew JE, Williams LM, Hannah LT, Barrett P, Abramovich DR. (1998) Melatonin receptors in the human fetal kidney: 2-[125I]iodomelatonin binding sites correlated with expression of Mel1a and Mel1b receptor genes. J Endocrinol, 156: 261-267. [PMID:9518871]

19. Dubocovich ML. (1985) Characterization of a retinal melatonin receptor. J. Pharmacol. Exp. Ther., 234 (2): 395-401. [PMID:2991499]

20. Dubocovich ML. (1988) Luzindole (N-0774): a novel melatonin receptor antagonist. J. Pharmacol. Exp. Ther., 246 (3): 902-10. [PMID:2843633]

21. Dubocovich ML, Hudson RL, Sumaya IC, Masana MI, Manna E. (2005) Effect of MT1 melatonin receptor deletion on melatonin-mediated phase shift of circadian rhythms in the C57BL/6 mouse. J Pineal Res, 39: 113-120. [PMID:16098087]

22. Dubocovich ML, Masana MI, Iacob S, Sauri DM. (1997) Melatonin receptor antagonists that differentiate between the human Mel1aand Mel1b recombinant subtypes are used to assess the pharmacological profile of the rabbit retina ML1 presynaptic heteroreceptor. Naunyn Schmiedebergs Arch. Pharmacol., 355: 365-375. [PMID:9089668]

23. Dubocovich ML, Rivera-Bermudez MA, Gerdin MJ, Masana MI. (2003) Molecular pharmacology, regulation and function of mammalian melatonin receptors. Front Biosci, 8: d1093-d1108. [PMID:12957828]

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Ralf Jockers, Philippe Delagrange, Margarita L. Dubocovich, Regina Pekelmann Markus, Nicolas Renault, Gianluca Tosini, Darius Paul Zlotos, Daniel P. Cardinali, Diana N. Krause, James Olcese, David Sugden.
Melatonin receptors: MT2 receptor. Last modified on 20/02/2018. Accessed on 15/11/2018. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=288.