Evidence map›Paper›PMID 20400944›Full record

ArticleNature2010

Native GABA(B) receptors are heteromultimers with a family of auxiliary subunits.

Jochen Schwenk, Michaela Metz, Gerd Zolles, Rostislav Turecek, Thorsten Fritzius, Wolfgang Bildl, Etsuko Tarusawa, Akos Kulik, Andreas Unger, Klara Ivankova and 9 more

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 170 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
170citing papers in PubMed, 1 pooled it
9.5field-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

170 citing papers in PubMed, 1 synthesis or guideline pooled it, 324 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Pareto optimality reveals an atlas of cellular archetypes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. GABAeNeuro · 2026
    Article
  11. GABAFrontiers in pharmacology · 2026
    Review
  12. Article
  13. KCTD Family: Emerging Regulators of GPCR Biased Signaling.Handbook of experimental pharmacology · 2026
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Genetic implication of GABAFrontiers in pharmacology · 2025
    Review

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

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

19 authors at 4 institutions in 3 countries.

Jochen SchwenkInstitute of Physiology II, University of Freiburg, Engesserstrasse 4, 79108 Freiburg, Germany.
Michaela Metz
Gerd Zolles
Rostislav Turecek
Thorsten Fritzius
Wolfgang Bildl
Etsuko Tarusawa
Akos Kulik
Andreas Unger
Klara Ivankova
Riad Seddik
Jim Y Tiao
Mathieu Rajalu
Johana Trojanova
Volker Rohde
Martin Gassmann
Uwe Schulte
Bernd Fakler
Bernhard Bettler
University of Basel · CHUniversity of Freiburg · DECzech Academy of Sciences, Institute of Experimental Medicine · CZLogopharm (Germany) · DE

Funding

Wellcome Trust
6 · The paper itself

Abstract

GABA(B) receptors are the G-protein-coupled receptors for gamma-aminobutyric acid (GABA), the main inhibitory neurotransmitter in the brain. They are expressed in almost all neurons of the brain, where they regulate synaptic transmission and signal propagation by controlling the activity of voltage-gated calcium (Ca(v)) and inward-rectifier potassium (K(ir)) channels. Molecular cloning revealed that functional GABA(B) receptors are formed by the heteromeric assembly of GABA(B1) with GABA(B2) subunits. However, cloned GABA(B(1,2)) receptors failed to reproduce the functional diversity observed with native GABA(B) receptors. Here we show by functional proteomics that GABA(B) receptors in the brain are high-molecular-mass complexes of GABA(B1), GABA(B2) and members of a subfamily of the KCTD (potassium channel tetramerization domain-containing) proteins. KCTD proteins 8, 12, 12b and 16 show distinct expression profiles in the brain and associate tightly with the carboxy terminus of GABA(B2) as tetramers. This co-assembly changes the properties of the GABA(B(1,2)) core receptor: the KCTD proteins increase agonist potency and markedly alter the G-protein signalling of the receptors by accelerating onset and promoting desensitization in a KCTD-subtype-specific manner. Taken together, our results establish the KCTD proteins as auxiliary subunits of GABA(B) receptors that determine the pharmacology and kinetics of the receptor response.

Indexed as

Protein MultimerizationAnimalsCHO CellsCricetinaeCricetulusElectric ConductivityGABA-B Receptor AgonistsHeterotrimeric GTP-Binding ProteinsKineticsMiceMultiprotein ComplexesNeuronsOocytesPotassiumPotassium ChannelsProtein Structure, TertiaryGABA-B Receptor AgonistsHeterotrimeric GTP-Binding ProteinsMultiprotein ComplexesPotassiumPotassium ChannelsProtein SubunitsReceptors, GABA-B

Identifiers

PMID20400944
OpenAlexW2063062496

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.