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

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 establis... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America April 24, 2018, Vol.115(17), pp.4501-4506
Main Author: Damian, Marjorie
Other Authors: Pons, Véronique , Renault, Pedro , M'Kadmi, Céline , Delort, Bartholomé , Hartmann, Lucie , Kaya, Ali I , Louet, Maxime , Gagne, Didier , Ben Haj Salah, Khoubaib , Denoyelle, Séverine , Ferry, Gilles , Boutin, Jean A , Wagner, Renaud , Fehrentz
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1712725115
Link: http://search.proquest.com/docview/2023728685/?pq-origsite=primo
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title: GHSR-D2R heteromerization modulates dopamine signaling through an effect on G protein conformation.
format: Article
creator:
  • Damian, Marjorie
  • Pons, Véronique
  • Renault, Pedro
  • M'Kadmi, Céline
  • Delort, Bartholomé
  • Hartmann, Lucie
  • Kaya, Ali I
  • Louet, Maxime
  • Gagne, Didier
  • Ben Haj Salah, Khoubaib
  • Denoyelle, Séverine
  • Ferry, Gilles
  • Boutin, Jean A
  • Wagner, Renaud
  • Fehrentz
subjects:
  • Dopamine–Chemistry
  • Gtp-Binding Protein Alpha Subunits, Gi-Go–Genetics
  • Humans–Metabolism
  • Protein Multimerization–Chemistry
  • Receptors, Dopamine D2–Genetics
  • Receptors, Ghrelin–Metabolism
  • Signal Transduction–Chemistry
  • Signal Transduction–Genetics
  • Signal Transduction–Metabolism
  • Signal Transduction–Chemistry
  • Signal Transduction–Genetics
  • Signal Transduction–Metabolism
  • Receptors, Dopamine D2
  • Receptors, Ghrelin
  • Gtp-Binding Protein Alpha Subunits, Gi-Go
  • Dopamine
  • G Protein
  • Gpcr
  • Conformational Dynamics
  • Heteromer
ispartof: Proceedings of the National Academy of Sciences of the United States of America, April 24, 2018, Vol.115(17), pp.4501-4506
description: 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...
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1712725115
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleGHSR-D2R heteromerization modulates dopamine signaling through an effect on G protein conformation.
creatorDamian, Marjorie ; Pons, Véronique ; Renault, Pedro ; M'Kadmi, Céline ; Delort, Bartholomé ; Hartmann, Lucie ; Kaya, Ali I ; Louet, Maxime ; Gagne, Didier ; Ben Haj Salah, Khoubaib ; Denoyelle, Séverine ; Ferry, Gilles ; Boutin, Jean A ; Wagner, Renaud ; Fehrentz
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ispartofProceedings of the National Academy of Sciences of the United States of America, April 24, 2018, Vol.115(17), pp.4501-4506
identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1712725115
subjectDopamine–Chemistry ; Gtp-Binding Protein Alpha Subunits, Gi-Go–Genetics ; Humans–Metabolism ; Protein Multimerization–Chemistry ; Receptors, Dopamine D2–Genetics ; Receptors, Ghrelin–Metabolism ; Signal Transduction–Chemistry ; Signal Transduction–Genetics ; Signal Transduction–Metabolism ; Signal Transduction–Chemistry ; Signal Transduction–Genetics ; Signal Transduction–Metabolism ; Receptors, Dopamine D2 ; Receptors, Ghrelin ; Gtp-Binding Protein Alpha Subunits, Gi-Go ; Dopamine ; G Protein ; Gpcr ; Conformational Dynamics ; Heteromer
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descriptionThe 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...
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titleGHSR-D2R heteromerization modulates dopamine signaling through an effect on G protein conformation.
authorDamian, Marjorie ; Pons, Véronique ; Renault, Pedro ; M'Kadmi, Céline ; Delort, Bartholomé ; Hartmann, Lucie ; Kaya, Ali I ; Louet, Maxime ; Gagne, Didier ; Ben Haj Salah, Khoubaib ; Denoyelle, Séverine ; Ferry, Gilles ; Boutin, Jean A ; Wagner, Renaud ; Fehrentz
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