Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/112123
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Type: Journal article
Title: Characterization of the Mel1c melatoninergic receptor in platypus (Ornithorhynchus anatinus)
Author: Gautier, C.
Guenin, S.
Riest-Fery, I.
Perry, T.
Legros, C.
Nosjean, O.
Simonneaux, V.
Grützner, F.
Boutin, J.
Citation: PLoS ONE, 2018; 13(3):e0191904-1-e0191904-20
Publisher: Public Library Science
Issue Date: 2018
ISSN: 1932-6203
1932-6203
Statement of
Responsibility: 
Célia Gautier, Sophie-Penelope Guenin, Isabelle Riest-Fery, Tahlia Jade Perry, Céline Legros, Olivier Nosjean, Valerie Simonneaux, Frank Grützner, Jean A. Boutin
Abstract: Melatonin is a neurohormone produced in both animals and plants. It binds at least three G-protein-coupled receptors: MT1 and MT2, and Mel1cGPR. Mammalian GPR50 evolved from the reptilian/avian Mel1c and lost its capacity to bind melatonin in all the therian mammal species that have been tested. In order to determine if binding is lost in the oldest surviving mammalian lineage of monotremes we investigated whether the melatonin receptor has the ability to bind melatonin in the platypus (Ornithorhynchus anatinus), and evaluated its pharmacological profile. Sequence and phylogenetic analysis showed that platypus has in fact retained the ancestral Mel1c and has the capacity to bind melatonin similar to other mammalian melatonin receptors (MT1 and MT2), with an affinity in the 1 nM range. We also investigated the binding of a set of melatoninergic ligands used previously to characterize the molecular pharmacology of the melatonin receptors from sheep, rats, mice, and humans and found that the general profiles of these compounds make Mel1c resemble human MT1 more than MT2. This work shows that the loss of GPR50 binding evolved after the divergence of monotremes less than 190MYA in therian mammals.
Keywords: COS Cells; Animals; Platypus; Cercopithecus aethiops; Melatonin; Receptors, Melatonin; Receptor, Melatonin, MT1; Receptor, Melatonin, MT2; Cloning, Molecular; Phylogeny; Base Sequence; Protein Binding
Rights: © 2018 Gautier et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
RMID: 0030084151
DOI: 10.1371/journal.pone.0191904
Appears in Collections:Environment Institute publications

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