Evidence map›Paper›PMID 7604029›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Evidence that neuronal G-protein-gated inwardly rectifying K+ channels are activated by G beta gamma subunits and function as heteromultimers.

P Kofuji, N Davidson, H A Lester

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
12.4field-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

105 citing papers in PubMed, 306 citations in OpenAlex.

  1. Article
  2. Review
  3. G protein-gated inwardly rectifying KHistology and histopathology · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. SNAP25 differentially contributes to GFrontiers in cellular neuroscience · 2023
    Article
  9. Review
  10. Neuronal G protein-gated KAmerican journal of physiology. Cell physiology · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    Article
  17. Identification ofToxins · 2019
    Article
  18. GIRK Channel Activity in Dopamine Neurons of the Ventral Tegmental Area Bidirectionally Regulates Behavioral Sensitivity to Cocaine.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  19. Review
  20. Article

45 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

3 authors at 1 institution in 1 country.

P KofujiDivision of Biology, California Institute of Technology, Pasadena 91225, USA.
N Davidson
H A Lester
California Institute of Technology · US

Funding

SYNAPTIC TRANSMISSION AT A VERTEBRATE GIANT SYNAPSEP50MH049176 · NIMH · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI FRASER, SCOTT E · 1992 to 2001
$4.2M
INTRACELLULAR SECOND MESSENGERS, BIOPHYSICAL STUDIESR01GM029836 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI LESTER, HENRY A. · 1985 to 2002
$1.2M
NIGMS NIH HHS GM29836NIMH NIH HHS MH49176
6 · The paper itself

Abstract

Guanine nucleotide-binding proteins (G proteins) activate K+ conductances in cardiac atrial cells to slow heart rate and in neurons to decrease excitability. cDNAs encoding three isoforms of a G-protein-coupled, inwardly rectifying K+ channel (GIRK) have recently been cloned from cardiac (GIRK1/Kir 3.1) and brain cDNA libraries (GIRK2/Kir 3.2 and GIRK3/Kir 3.3). Here we report that GIRK2 but not GIRK3 can be activated by G protein subunits G beta 1 and G gamma 2 in Xenopus oocytes. Furthermore, when either GIRK3 or GIRK2 was coexpressed with GIRK1 and activated either by muscarinic receptors or by G beta gamma subunits, G-protein-mediated inward currents were increased by 5- to 40-fold. The single-channel conductance for GIRK1 plus GIRK2 coexpression was intermediate between those for GIRK1 alone and for GIRK2 alone, and voltage-jump kinetics for the coexpressed channels displayed new kinetic properties. On the other hand, coexpression of GIRK3 with GIRK2 suppressed the GIRK2 alone response. These studies suggest that formation of heteromultimers involving the several GIRKs is an important mechanism for generating diversity in expression level and function of neurotransmitter-coupled, inward rectifier K+ channels.

Indexed as

Potassium Channels, Inwardly RectifyingAcetylcholineAnimalsBrainCloning, MolecularEvoked PotentialsFemaleG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGTP-Binding ProteinsHeartMacromolecular SubstancesMembrane PotentialsMiceMyocardiumNeuronsOocytesAcetylcholineG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGTP-Binding Proteinsinward rectifier potassium channel 2Kcnj9 protein, mouseMacromolecular SubstancesPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingReceptors, MuscarinicRNA, Complementary

Identifiers

PMID7604029
PMCPMC41554
OpenAlexW2028360988

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.