Evidence map›Paper›PMID 10779550›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

The role of members of the pertussis toxin-sensitive family of G proteins in coupling receptors to the activation of the G protein-gated inwardly rectifying potassium channel.

J L Leaney, A Tinker

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Serotonin 5-HTACS chemical neuroscience · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Mechanisms and Regulation of Neuronal GABACurrent topics in behavioral neurosciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. The role of inhibitory heterotrimeric G proteins in the control of in vivo heart rate dynamics.American journal of physiology. Regulatory, integrative and comparative physiology · 2008
    Article
  19. Coregulation of natively expressed pertussis toxin-sensitive muscarinic receptors with G-protein-activated potassium channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  20. Article
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

2 authors at 1 institution in 1 country.

J L LeaneyCentre for Clinical Pharmacology, Department of Medicine, University College London, The Rayne Institute, 5 University Street, London WC1E 6JJ, United Kingdom.
A Tinker
University College London · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Inwardly rectifying potassium (K(+)) channels gated by G proteins (Kir3.x family) are widely distributed in neuronal, atrial, and endocrine tissues and play key roles in generating late inhibitory postsynaptic potentials, slowing the heart rate and modulating hormone release. They are directly activated by G(betagamma) subunits released from G protein heterotrimers of the G(i/o) family upon appropriate receptor stimulation. Here we examine the role of isoforms of pertussis toxin (PTx)-sensitive G protein alpha subunits (G(ialpha1-3) and G(oalphaA)) in mediating coupling between various receptor systems (A(1), alpha(2A), D(2S), M(4), GABA(B)1a+2, and GABA(B)1b+2) and the cloned counterpart of the neuronal channel (Kir3.1+3.2A). The expression of mutant PTx-resistant G(i/oalpha) subunits in PTx-treated HEK293 cells stably expressing Kir3.1+3.2A allows us to selectively investigate that coupling. We find that, for those receptors (A(1), alpha(2A)) known to interact with all isoforms, G(ialpha1-3) and G(oalphaA) can all support a significant degree of coupling to Kir3.1+3.2A. The M(4) receptor appears to preferentially couple to G(ialpha2) while another group of receptors (D(2S), GABA(B)1a+2, GABA(B)1b+2) activates the channel predominantly through G(betagamma) liberated from G(oA) heterotrimers. Interestingly, we have also found a distinct difference in G protein coupling between the two splice variants of GABA(B)1. Our data reveal selective pathways of receptor activation through different G(i/oalpha) isoforms for stimulation of the G protein-gated inwardly rectifying K(+) channel.

Indexed as

Pertussis ToxinPotassium Channels, Inwardly RectifyingCell LineGTP-Binding Protein alpha Subunits, Gi-GoHeterotrimeric GTP-Binding ProteinsHumansMembrane PotentialsNeuronsPatch-Clamp TechniquesPoint MutationPotassium ChannelsProtein IsoformsReceptors, GABA-BReceptors, Purinergic P1Recombinant ProteinsTransfectionGTP-Binding Protein alpha Subunits, Gi-GoHeterotrimeric GTP-Binding ProteinsPertussis ToxinPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein IsoformsReceptors, GABA-BReceptors, Purinergic P1Recombinant ProteinsVirulence Factors, Bordetella

Identifiers

PMID10779550
PMCPMC25883
OpenAlexW1984139177

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.