Evidence map›Paper›PMID 9430632›Full record

ArticleThe EMBO journal1998

The heterotrimeric G protein Go2 regulates catecholamine uptake by secretory vesicles.

G Ahnert-Hilger, B Nürnberg, T Exner, T Schäfer, R Jahn

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 63 citations in OpenAlex.

  1. Targeting GαBasic research in cardiology · 2024
    Article
  2. Article
  3. Vesicular neurotransmitter transporters in Drosophila melanogaster.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Vesicular and plasma membrane transporters for neurotransmitters.Cold Spring Harbor perspectives in biology · 2012
    Review
  9. Article
  10. Review
  11. An obligatory requirement for the heterotrimeric G protein Gi3 in the antiautophagic action of insulin in the liver.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  12. Galphao2 regulates vesicular glutamate transporter activity by changing its chloride dependence.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005
    Article
  13. Article
  14. Synaptic vesicle transporter expression regulates vesicle phenotype and quantal size.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  15. The neuronal monoamine transporter VMAT2 is regulated by the trimeric GTPase Go(2).The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  16. Posttranslational modification of Galphao1 generates Galphao3, an abundant G protein in brain.Proceedings of the National Academy of Sciences of the United States of America · 1999
    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

5 authors at 1 institution in 1 country.

G Ahnert-HilgerInstitut für Anatomie der Charité, Humboldt-Universität zu Berlin, Germany.
B Nürnberg
T Exner
T Schäfer
R Jahn
Humboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretory vesicles store neurotransmitters that are released by exocytosis. Their membrane contains transporters responsible for transmitter loading that are driven by an electrochemical proton gradient across the vesicle membrane. We have now examined whether uptake of noradrenaline is regulated by heterotrimeric G proteins. In streptolysin O-permeabilized PC 12 cells, GTP-analogues and AlF4- inhibited noradrenaline uptake, an effect that was sensitive to treatment with pertussis toxin. Inhibition of uptake was prevented by Galphao-specific antibodies and mimicked by purified activated Galphao2. No effect was seen when Galphao2 in its inactive GDP-bound form or purified activated Galphao1, Galphai1 and Galphai2 were tested. Down-regulation of uptake remained unchanged when exocytosis was inhibited by the light chain of tetanus toxin. Vesicular acidification was not affected whereas binding of [3H]reserpine was reduced by GTPgammaS and Galphao2. These data suggest that the monoamine transporter rather than the vacuolar ATPase is affected. We conclude that catecholamine uptake is controlled by Galphao2, suggesting a novel function for heterotrimeric G proteins in the control of neurotransmitter storage.

Indexed as

Membrane Transport ProteinsNeuropeptidesAnimalsBiological TransportCatecholaminesCytoplasmic GranulesDown-RegulationGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding ProteinsMembrane GlycoproteinsNeurotransmitter AgentsPC12 CellsRatsVesicular Biogenic Amine Transport ProteinsCatecholaminesGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding ProteinsMembrane GlycoproteinsMembrane Transport ProteinsNeuropeptidesNeurotransmitter AgentsVesicular Biogenic Amine Transport Proteins

Identifiers

PMID9430632
PMCPMC1170391
OpenAlexW2021167495

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.