Evidence map›Paper›PMID 21552208›Full record

ArticleThe EMBO journal2011

The oligomeric state sets GABA(B) receptor signalling efficacy.

Laëtitia Comps-Agrar, Julie Kniazeff, Lenea Nørskov-Lauritsen, Damien Maurel, Martin Gassmann, Nathalie Gregor, Laurent Prézeau, Bernhard Bettler, Thierry Durroux, Eric Trinquet and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Impact of aging on the GABAbioRxiv : the preprint server for biology · 2024
    Article
  4. Article
  5. Article
  6. Structural Basis of GABACurrent topics in behavioral neurosciences · 2022
    Review
  7. Mechanisms and Regulation of Neuronal GABACurrent topics in behavioral neurosciences · 2022
    Review
  8. GABACurrent topics in behavioral neurosciences · 2022
    Review
  9. Article
  10. Review
  11. Multiple GPCR Functional Assays Based on Resonance Energy Transfer Sensors.Frontiers in cell and developmental biology · 2021
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. GPCRs and Signal Transducers: Interaction Stoichiometry.Trends in pharmacological sciences · 2018
    Review
  20. Diversity of structure and function of GABAProceedings of the Japan Academy. Series B, Physical and biological sciences · 2018
    Review
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

11 authors at 6 institutions in 2 countries.

Laëtitia Comps-AgrarCNRS, UMR5203, Institut de Génomique Fonctionnelle, Department of Molecular Pharmacology, Montpellier, France.
Julie Kniazeff
Lenea Nørskov-Lauritsen
Damien Maurel
Martin Gassmann
Nathalie Gregor
Laurent Prézeau
Bernhard Bettler
Thierry Durroux
Eric Trinquet
Jean-Philippe Pin
Centre National de la Recherche Scientifique · FRCisbio (France) · FRInstitut de Génomique Fonctionnelle · FRUniversité de Montpellier · FRUniversity of Basel · CHInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) have key roles in cell-cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric GABA(B) receptor is one of the most abundant, being distributed in most brain regions, on either pre- or post-synaptic elements. Here, using specific antibodies labelled with time-resolved FRET compatible fluorophores, we provide evidence that the heterodimeric GABA(B) receptor can form higher-ordered oligomers in the brain, as suggested by the close proximity of the GABA(B1) subunits. Destabilizing the oligomers using a competitor or a GABA(B1) mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such GABA(B) receptor oligomers composed of a wild-type and a non-functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the GABA(B) heterodimers.

Indexed as

Allosteric RegulationAnimalsChlorocebus aethiopsCOS CellsHEK293 CellsHumansMiceMice, Inbred BALB CMice, KnockoutMutagenesis, Site-DirectedProtein IsoformsProtein MultimerizationProtein StabilityReceptors, GABA-BSignal TransductionProtein IsoformsReceptors, GABA-B

Identifiers

PMID21552208
PMCPMC3116278
OpenAlexW2098303384

What OpenQuestion holds

Textmetadata
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.