Evidence map›Paper›PMID 29632174›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

GHSR-D2R heteromerization modulates dopamine signaling through an effect on G protein conformation.

Marjorie Damian, Véronique Pons, Pedro Renault, Céline M'Kadmi, Bartholomé Delort, Lucie Hartmann, Ali I Kaya, Maxime Louet, Didier Gagne, Khoubaib Ben Haj Salah and 12 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
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  6. Genetic variants of accessory proteins and G proteins in human genetic disease.Critical reviews in clinical laboratory sciences · 2025
    Review
  7. Article
  8. Review
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  10. "Sibling" battle or harmony: crosstalk between nesfatin-1 and ghrelin.Cellular and molecular life sciences : CMLS · 2022
    Review
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  14. Article
  15. Review
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  17. Review
  18. Ligand-induced conformational changes in a SMALP-encapsulated GPCR.Biochimica et biophysica acta. Biomembranes · 2020
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

22 authors at 4 institutions in 2 countries.

Marjorie DamianInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Véronique PonsI2MC, INSERM U1048, Université de Toulouse, F-31432 Toulouse, France.
Pedro RenaultInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Céline M'KadmiInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Bartholomé DelortInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Lucie HartmannIntegral Membrane Proteins Research and Services (IMPReSs), UMR 7242 CNRS, Ecole Superieure de Biotechnologie de Strasbourg, Université de Strasbourg, F-67412 Illkirch, France.
Ali I KayaDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6600.
Maxime LouetInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Didier GagneInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Khoubaib Ben Haj SalahInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.ORCID 0000-0002-2313-2773
Séverine DenoyelleInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Gilles FerryPole d'expertise Biotechnologie, Chimie, Biologie, Institut de Recherches Servier, F-78290 Croissy-sur-Seine, France.
Jean A BoutinPole d'expertise Biotechnologie, Chimie, Biologie, Institut de Recherches Servier, F-78290 Croissy-sur-Seine, France.
Renaud WagnerIntegral Membrane Proteins Research and Services (IMPReSs), UMR 7242 CNRS, Ecole Superieure de Biotechnologie de Strasbourg, Université de Strasbourg, F-67412 Illkirch, France.
Jean-Alain FehrentzInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Jean MartinezInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Jacky MarieInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Nicolas FloquetInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Céline GalèsI2MC, INSERM U1048, Université de Toulouse, F-31432 Toulouse, France.
Sophie MaryInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France.
Heidi E HammDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6600.
Jean-Louis BanèresInstitut des Biomolécules Max Mousseron, CNRS, Ecole Nationale Superieure de Chimie de Montepellier, Université Montpellier, 34093 Montpellier, France; jean-louis.baneres@umontpellier.fr.
Centre National de la Recherche Scientifique · FRInserm · FRServier (France) · FRVanderbilt University Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The growth hormone secretagogue receptor (GHSR) and dopamine receptor (D2R) have been shown to oligomerize in hypothalamic neurons with a significant effect on dopamine signaling, but the molecular processes underlying this effect are still obscure. We used here the purified GHSR and D2R to establish that these two receptors assemble in a lipid environment as a tetrameric complex composed of two each of the receptors. This complex further recruits G proteins to give rise to an assembly with only two G protein trimers bound to a receptor tetramer. We further demonstrate that receptor heteromerization directly impacts on dopamine-mediated Gi protein activation by modulating the conformation of its α-subunit. Indeed, association to the purified GHSR:D2R heteromer triggers a different active conformation of Gαi that is linked to a higher rate of GTP binding and a faster dissociation from the heteromeric receptor. This is an additional mechanism to expand the repertoire of GPCR signaling modulation that could have implications for the control of dopamine signaling in normal and physiopathological conditions.

Indexed as

Protein MultimerizationSignal TransductionDopamineGTP-Binding Protein alpha Subunits, Gi-GoHumansReceptors, Dopamine D2Receptors, GhrelinDopamineGTP-Binding Protein alpha Subunits, Gi-GoReceptors, Dopamine D2Receptors, Ghrelinconformational dynamicsGPCRG proteinheteromersignaling

Identifiers

PMID29632174
PMCPMC5924877
OpenAlexW2797691255

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.