MT1 Melatonin Receptor Reconstitution in Nanodiscs.


Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2022
Historique:
entrez: 30 9 2022
pubmed: 1 10 2022
medline: 5 10 2022
Statut: ppublish

Résumé

A way to study G protein-coupled receptors in a minimal system is to reconstruct artificial membrane mimics, made of detergent and/or of lipids in which the purified receptor is maintained. In particular, it is now possible to generate lipid nanoparticles, such as nanodiscs, in which a single receptor molecule is included. Such objects offer the invaluable potential of studying an isolated receptor stabilized in a finely controlled membrane-like environment to evaluate its pharmacology, its function, and its structure at the molecular level. In this chapter, we detail the different steps from the extraction and isolation of a recombinant MT1 melatonin receptor in detergent, down to its reconstitution into nanodiscs. A G protein activation test is further described in order to exemplify how the functionality of such particles may be investigated.

Identifiants

pubmed: 36180690
doi: 10.1007/978-1-0716-2593-4_21
doi:

Substances chimiques

Detergents 0
Lipid Nanoparticles 0
Lipids 0
Liposomes 0
Membranes, Artificial 0
Receptor, Melatonin, MT1 0
GTP-Binding Proteins EC 3.6.1.-
Melatonin JL5DK93RCL

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

171-178

Informations de copyright

© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Lagerström MC, Schiöth HB (2008) Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 7:339–357. https://doi.org/10.1038/nrd2518
doi: 10.1038/nrd2518 pubmed: 18382464
Jockers R, Maurice P, Boutin JA et al (2008) Melatonin receptors, heterodimerization, signal transduction and binding sites: what’s new? Br J Pharmacol 154:1182–1195. https://doi.org/10.1038/bjp.2008.184
doi: 10.1038/bjp.2008.184 pubmed: 18493248 pmcid: 2483381
Katritch V, Cherezov V, Stevens RC (2013) Structure-function of the G protein-coupled receptor superfamily. Annu Rev Pharmacol Toxicol 53:531–556. https://doi.org/10.1146/annurev-pharmtox-032112-135923
doi: 10.1146/annurev-pharmtox-032112-135923 pubmed: 23140243
Stauch B, Johansson LC, McCorvy JD et al (2019) Structural basis of ligand recognition at the human MT1 melatonin receptor. Nature 569:284–288. https://doi.org/10.1038/s41586-019-1141-3
doi: 10.1038/s41586-019-1141-3 pubmed: 31019306
Johansson LC, Stauch B, McCorvy JD et al (2019) XFEL structures of the human MT2 melatonin receptor reveal the basis of subtype selectivity. Nature 569:289–292. https://doi.org/10.1038/s41586-019-1144-0
doi: 10.1038/s41586-019-1144-0 pubmed: 31019305 pmcid: 6589158
Stein RM, Kang HJ, McCorvy JD et al (2020) Virtual discovery of melatonin receptor ligands to modulate circadian rhythms. Nature 579:609–614. https://doi.org/10.1038/s41586-020-2027-0
doi: 10.1038/s41586-020-2027-0 pubmed: 32040955 pmcid: 7134359
Glatfelter GC, Jones AJ, Rajnarayanan RV et al (2021) Pharmacological actions of carbamate insecticides at mammalian melatonin receptors. J Pharmacol Exp Ther 376:306–321. https://doi.org/10.1124/jpet.120.000065
doi: 10.1124/jpet.120.000065 pubmed: 33203660 pmcid: 7841424
Chattopadhyay A (2014) GPCRs: lipid-dependent membrane receptors that act as drug targets. Adv Biol 2014:1–12. https://doi.org/10.1155/2014/143023
doi: 10.1155/2014/143023
Bayburt TH, Sligar SG (2010) Membrane protein assembly into Nanodiscs. FEBS Lett 584:1721–1727. https://doi.org/10.1016/j.febslet.2009.10.024
doi: 10.1016/j.febslet.2009.10.024 pubmed: 19836392
Oldham WM, van Eps N, Preininger AM et al (2006) Mechanism of the receptor-catalyzed activation of heterotrimeric G proteins. Nat Struct Mol Biol 13:772–777. https://doi.org/10.1038/nsmb1129
doi: 10.1038/nsmb1129 pubmed: 16892066
Logez C, Berger S, Legros C et al (2014) Recombinant human melatonin receptor MT1 isolated in mixed detergents shows pharmacology similar to that in mammalian cell membranes. PLoS One 9:e100616. https://doi.org/10.1371/journal.pone.0100616
doi: 10.1371/journal.pone.0100616 pubmed: 24959712 pmcid: 4069108
Guyot L, Hartmann L, Mohammed-Bouteben S et al (2020) Preparation of recombinant membrane proteins from Pichia pastoris for molecular investigations. Curr Protoc Protein Sci 100:e104. https://doi.org/10.1002/cpps.104
doi: 10.1002/cpps.104 pubmed: 32289210
Byrne B (2015) Pichia pastoris as an expression host for membrane protein structural biology. Curr Opin Struct Biol 32:9–17. https://doi.org/10.1016/j.sbi.2015.01.005
doi: 10.1016/j.sbi.2015.01.005 pubmed: 25658849
André N, Cherouati N, Prual C et al (2006) Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen. Protein Sci 15:1115–1126. https://doi.org/10.1110/ps.062098206
doi: 10.1110/ps.062098206 pubmed: 16597836 pmcid: 2242496
Denisov IG, Grinkova YV, Lazarides AA et al (2004) Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size. J Am Chem Soc 126:3477–3487. https://doi.org/10.1021/ja0393574
doi: 10.1021/ja0393574 pubmed: 15025475
Kozasa T (2004) Purification of G protein subunits from Sf9 insect cells using hexahistidine-tagged alpha and beta gamma subunits. Methods Mol Biol 237:21–38. https://doi.org/10.1385/1-59259-430-1:21
doi: 10.1385/1-59259-430-1:21 pubmed: 14501036
Sligar SG, Denisov IG (2021) Nanodiscs: a toolkit for membrane protein science. Protein Sci 30:297–315. https://doi.org/10.1002/pro.3994
doi: 10.1002/pro.3994 pubmed: 33165998
Efremov RG, Gatsogiannis C, Raunser S (2017) Lipid nanodiscs as a tool for high-resolution structure determination of membrane proteins by single-particle cryo-EM. Methods Enzymol 594:1–30. https://doi.org/10.1016/bs.mie.2017.05.007
doi: 10.1016/bs.mie.2017.05.007 pubmed: 28779836

Auteurs

Jean A Boutin (JA)

Pole d'expertise Biotechnologie, Chimie & Biologie, Institut de Recherches Servier, Croissy-sur-Seine, France. ja.boutin.pro@gmail.com.
PHARMADEV (Pharmacochimie et biologie pour le développement), Faculté de Pharmacie, Toulouse, France. ja.boutin.pro@gmail.com.

Christel Logez (C)

Pole d'expertise Biotechnologie, Chimie & Biologie, Institut de Recherches Servier, Croissy-sur-Seine, France.
Plateforme IMPReSs, Laboratoire de Biotechnologie et Signalisation Cellulaire, CNRS, Université de Strasbourg, Illkirch, France.
Bioprocess Research & Development, SANOFI PASTEUR, Marcy l'Etoile, France.

Marjorie Damian (M)

IBMM, Université de Montpellier, CNRS, ENSCM, Montpellier, France.

Renaud Wagner (R)

Plateforme IMPReSs, Laboratoire de Biotechnologie et Signalisation Cellulaire, CNRS, Université de Strasbourg, Illkirch, France.

Jean-Louis Banères (JL)

IBMM, Université de Montpellier, CNRS, ENSCM, Montpellier, France.

Gilles Ferry (G)

Pole d'expertise Biotechnologie, Chimie & Biologie, Institut de Recherches Servier, Croissy-sur-Seine, France.

Articles similaires

Tumor Microenvironment Nanoparticles Immunotherapy Cellular Senescence Animals
Cobalt Azo Compounds Ferric Compounds Polyesters Photolysis
Neoplastic Stem Cells Animals Humans Aldehyde Dehydrogenase Tretinoin

Classifications MeSH