ArticlePloS one2014
Recombinant human melatonin receptor MT1 isolated in mixed detergents shows pharmacology similar to that in mammalian cell membranes.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Highly-Sensitive In Vitro Bioassays for FSH, TSH, PTH, Kp, and OT in Addition to LH in Mouse Leydig Tumor Cell.International journal of molecular sciences · 2023Article
- MT1 Melatonin Receptor Reconstitution in Nanodiscs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Characterization of the various functional pathways elicited by synthetic agonists or antagonists at the melatonin MTPharmacology research & perspectives · 2020Article
- The five dimensions of receptor pharmacology exemplified by melatonin receptors: An opinion.Pharmacology research & perspectives · 2020Review
- Importance of the Choice of a Recombinant System to Produce Large Amounts of Functional Membrane Protein hERG.International journal of molecular sciences · 2019Article
- Melatonin receptors: molecular pharmacology and signalling in the context of system bias.British journal of pharmacology · 2018Review
- Hamster Melatonin Receptors: Cloning and Binding Characterization of MT₁ and Attempt to Clone MT₂.International journal of molecular sciences · 2018Article
- New MT₂ Melatonin Receptor-Selective Ligands: Agonists and Partial Agonists.International journal of molecular sciences · 2017Article
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Authors and funding
11 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human melatonin MT1 receptor-belonging to the large family of G protein-coupled receptors (GPCRs)-plays a key role in circadian rhythm regulation and is notably involved in sleep disorders and depression. Structural and functional information at the molecular level are highly desired for fine characterization of this receptor; however, adequate techniques for isolating soluble MT1 material suitable for biochemical and biophysical studies remain lacking. Here we describe the evaluation of a panel of constructs and host systems for the production of recombinant human MT1 receptors, and the screening of different conditions for their solubilization and purification. Our findings resulted in the establishment of an original strategy using a mixture of Fos14 and CHAPS detergents to extract and purify a recombinant human MT1 from Pichia pastoris membranes. This procedure enabled the recovery of relatively pure, monomeric and ligand-binding active MT1 receptor in the near-milligram range. A comparative study based on extensive ligand-binding characterization highlighted a very close correlation between the pharmacological profiles of MT1 purified from yeast and the same receptor present in mammalian cell membranes. The high quality of the purified MT1 was further confirmed by its ability to activate its cognate Gαi protein partner when reconstituted in lipid discs, thus opening novel paths to investigate this receptor by biochemical and biophysical approaches.
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