Evidence map›Paper›PMID 19648932›Full record

ArticleNature chemical biology2009

Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation.

Yang Han, Irina S Moreira, Eneko Urizar, Harel Weinstein, Jonathan A Javitch

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 176 papers.

0numbers the graph read from it
0cells of the map it votes in
176citing papers in PubMed
16.5field-weighted citation impact, top 1% 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

176 citing papers in PubMed, 329 citations in OpenAlex.

  1. Review
  2. Article
  3. FDA Drug Repurposing Uncovers Modulators of Dopamine DJournal of medicinal chemistry · 2025
    Article
  4. Asymmetric Dynamics Between the Protomers of the σ2 Receptor Homodimer.Journal of chemical information and modeling · 2025
    Article
  5. Article
  6. Article
  7. Stabilized DNature communications · 2025
    Article
  8. Article
  9. Article
  10. The World of GPCR dimers - Mapping dopamine receptor DComputational and structural biotechnology journal · 2023
    Article
  11. MUG: A mutation overview of GPCR subfamily A17 receptors.Computational and structural biotechnology journal · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

116 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Yang HanCenter for Molecular Recognition, Columbia University College of Physicians and Surgeons, New York, NY, USA.
Irina S Moreira
Eneko Urizar
Harel Weinstein
Jonathan A Javitch
Columbia University · USCornell University · USNew York State Psychiatric Institute

Funding

Structure of the Dopamine D2-Like Receptor Binding SitesR01MH054137 · NIMH · NEW YORK STATE PSYCHIATRIC INSTITUTE DBA RESEARCH FOUNDATION FOR MENTAL HYGIENE, INC · PI JAVITCH, JONATHAN A · 1995 to 2025
$12.0M
HALLUCINOGENS IN SPECIFIC SIGNALING AND CIRCUITRYP01DA012923 · NIDA · WEILL MEDICAL COLL OF CORNELL UNIV · PI WEINSTEIN, HAREL · 2000 to 2011
$8.6M
Molecular Determinants for the Action of PsychostimulantsK05DA022413 · NIDA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI JAVITCH, JONATHAN A · 2007 to 2016
$1.3M
NIDA NIH HHS DA012923NIDA NIH HHS DA022413NIDA NIH HHS K05 DA022413NIDA NIH HHS P01 DA012923NIMH NIH HHS MH054137NIMH NIH HHS R01 MH054137
6 · The paper itself

Abstract

A major obstacle to understanding the functional importance of dimerization between class A G protein-coupled receptors (GPCRs) has been the methodological limitation in achieving control of the identity of the components comprising the signaling unit. We have developed a functional complementation assay that enables such control, and we demonstrate it here for the human dopamine D2 receptor. The minimal signaling unit, two receptors and a single G protein, is maximally activated by agonist binding to a single protomer, which suggests an asymmetrical activated dimer. Inverse agonist binding to the second protomer enhances signaling, whereas agonist binding to the second protomer blunts signaling. Ligand-independent constitutive activation of the second protomer also inhibits signaling. Thus, GPCR dimer function can be modulated by the activity state of the second protomer, which for a heterodimer may be altered in pathological states. Our new methodology also makes possible the characterization of signaling from a defined heterodimer unit.

Indexed as

Promoter Regions, GeneticSignal TransductionAllosteric RegulationCell LineComputational BiologyDopamine D2 Receptor AntagonistsGTP-Binding ProteinsHumansModels, BiologicalModels, MolecularProtein MultimerizationQuinpiroleReceptors, Dopamine D2Receptors, G-Protein-CoupledDopamine D2 Receptor AntagonistsGTP-Binding ProteinsQuinpiroleReceptors, Dopamine D2Receptors, G-Protein-Coupled

Identifiers

PMID19648932
PMCPMC2817978
OpenAlexW2098876955

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.