Evidence map›Paper›PMID 10366609›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1999

Sequestration of G-protein beta gamma subunits by different G-protein alpha subunits blocks voltage-dependent modulation of Ca2+ channels in rat sympathetic neurons.

S W Jeong, S R Ikeda

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. 5-HT7R/G12 signaling regulates neuronal morphology and function in an age-dependent manner.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  6. Article
  7. Origin of the voltage dependence of G-protein regulation of P/Q-type Ca2+ channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
  8. Article
  9. Article
  10. G-protein alpha subunit isoforms couple differentially to receptors that mediate presynaptic inhibition at rat hippocampal synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  11. Article
  12. The C terminus of the Ca channel alpha1B subunit mediates selective inhibition by G-protein-coupled receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  13. Article
  14. GTP-binding protein beta gamma subunits mediate presynaptic calcium current inhibition by GABA(B) receptor.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  15. Activation and inhibition of G protein-coupled inwardly rectifying potassium (Kir3) channels by G protein beta gamma subunits.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  16. Endogenous regulator of G-protein signaling proteins modify N-type calcium channel modulation in rat sympathetic neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  17. Article
  18. Article
  19. P2Y purinoceptors inhibit exocytosis in adrenal chromaffin cells via modulation of voltage-operated calcium channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    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.

S W JeongLaboratory of Molecular Physiology, Guthrie Research Institute, Sayre, Pennsylvania 18840, USA.
S R Ikeda
Guthrie Foundation · US

Funding

MOLECULAR MECHANISMS OF N TYPE CALCIUM CHANNEL MODULATIOR01GM056180 · NIGMS · GUTHRIE FOUNDATION FOR EDUCATION AND RES · PI IKEDA, STEPHEN R · 1997 to 2001
$485k
NIGMS NIH HHS GM 56180
6 · The paper itself

Abstract

The membrane-delimited and voltage-dependent inhibition of N-type Ca2+ channels is mediated by Gbeta gamma subunits. Previously, exogenous excess GDP-bound GalphaoA has been shown to dramatically attenuate the norepinephrine (NE)-mediated Ca2+ current inhibition by sequestration of Gbeta gamma subunits in rat superior cervical ganglion (SCG) neurons. In the present study, we determined whether the attenuation of NE-mediated modulation is specific to GalphaoA or shared by a number of closely related (Galphatr, GalphaoB, Galphai1, Galphai2, Galphai3, Galphaz) or unrelated (Galphas, Galphaq, Galpha11, Galpha16, Galpha12, Galpha13) Galpha subunits. Individual Galpha subunits from different subfamilies were transiently overexpressed in SCG neurons by intranuclear injection of mammalian expression vectors encoding the desired protein. Strikingly, all Galpha subunits except Galphaz nearly blocked basal facilitation and NE-mediated modulation. Likewise, VIP-mediated Ca2+ current inhibition, which is mediated by cholera toxin-sensitive G-protein, was also completely suppressed by a number of Galpha subunits overexpressed in neurons. Galphas expression produced either enhancement or attenuation of the VIP-mediated modulation-an effect that seemed to depend on the expression level. The onset of the nonhydrolyzable GTP analog, guanylylimidodiphosphate-mediated facilitation was significantly delayed by overexpression of different GDP-bound Galpha subunits. Taken together, these data suggest that a wide variety of Galpha subunits are capable of forming heterotrimers with endogenous Gbeta gamma subunits mediating voltage-dependent Ca2+ channel inhibition. In conclusion, coupling specificity in signal transduction is unlikely to arise as a result of restricted Galpha/Gbeta gamma interaction.

Indexed as

GTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsHeterotrimeric GTP-Binding ProteinsAdrenergic beta-AgonistsAnimalsCalcium ChannelsElectrophysiologyGene ExpressionGTP-Binding Protein alpha Subunits, GsGTP-Binding ProteinsGuanylyl ImidodiphosphateMaleMembrane PotentialsMuscarineMuscarinic AgonistsNeuronsAdrenergic beta-AgonistsCalcium ChannelsG-protein Beta gammaGTP-Binding Protein alpha Subunits, GsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsGTP-Binding ProteinsGuanylyl ImidodiphosphateHeterotrimeric GTP-Binding ProteinsMuscarineMuscarinic AgonistsNorepinephrinePotassium ChannelsReceptors, MuscarinicVasoactive Intestinal PeptideVirulence Factors, Bordetella

Identifiers

PMID10366609
PMCPMC6782646
OpenAlexW1759476206

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.