Evidence map›Paper›PMID 8790428›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Subcellular localization of gamma-aminobutyric acid type A receptors is determined by receptor beta subunits.

C N Connolly, J R Wooltorton, T G Smart, S J Moss

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.4field-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

47 citing papers in PubMed, 141 citations in OpenAlex.

  1. The grand challenge in cellular neurophysiology.Frontiers in cellular neuroscience · 2026
    Article
  2. Massive Activation of GABABiomolecules · 2025
    Review
  3. Article
  4. GABAFrontiers in cellular neuroscience · 2024
    Article
  5. Article
  6. Physiological Role of ATPase for GABAInternational journal of molecular sciences · 2022
    Article
  7. Review
  8. Article
  9. Intricacies of GABAInternational journal of molecular sciences · 2021
    Review
  10. GABAFrontiers in cellular neuroscience · 2020
    Article
  11. Mechanisms of GABAScientific reports · 2019
    Article
  12. Cell surface expression of homomeric GABAThe Journal of biological chemistry · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

C N ConnollyMedical Research Council Laboratory of Molecular Cell Biology, University College London, United Kingdom.
J R Wooltorton
T G Smart
S J Moss
MRC Laboratory for Molecular Cell Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

gamma-aminobutyric acid type A (GABAA) receptors are the major sites of fast synaptic inhibition in the brain. They are constructed from four subunit classes with multiple members: alpha (1-6), beta (1-4), gamma (1-4), and delta (1). The contribution of subunit diversity in determining receptor subcellular targeting was examined in polarized Madin-Darby canine kidney (MDCK) cells. Significant detection of cell surface homomeric receptor expression by a combination of both immunological and electrophysiological methodologies was only found for the beta 3 subunit. Expression of alpha/beta binary combinations resulted in a nonpolarized distribution for alpha 1 beta 1 complexes, but specific basolateral targeting of both alpha 1 beta 2 and alpha 1 beta 3 complexes. The polarized distribution of these alpha/beta complexes was unaffected by the presence of the gamma 2S subunit. Interestingly, delivery of receptors containing the beta 3 subunit to the basolateral domain occurs via the apical surface. These results show that beta subunits can selectively target GABAA receptors to distinct cellular locations. Changes in the spatial and temporal expression of beta-subunit isoforms may therefore provide a mechanism for relocating GABAA receptor function between distinct neuronal domains. Given the critical role of these receptors in mediating synaptic inhibition, the contribution of different beta subunits in GABAA receptor function, may have implications in neuronal development and for receptor localization/clustering.

Indexed as

AnimalsDNA, ComplementaryDogsElectrophysiologyEpitopesGene ExpressionKidneyMicroinjectionsMicroscopy, Phase-ContrastPentobarbitalPicrotoxinProtein ConformationReceptors, GABA-ASubcellular FractionsDNA, ComplementaryEpitopesPentobarbitalPicrotoxinReceptors, GABA-A

Identifiers

PMID8790428
PMCPMC38526
OpenAlexW2033602348

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.