Evidence map›Paper›PMID 10704487›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2000

The neuronal monoamine transporter VMAT2 is regulated by the trimeric GTPase Go(2).

M Höltje, B von Jagow, I Pahner, M Lautenschlager, H Hörtnagl, B Nürnberg, R Jahn, G Ahnert-Hilger

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
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  3. Targeting GαBasic research in cardiology · 2024
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  17. Review
  18. Deletion of Go2alpha abolishes cocaine-induced behavioral sensitization by disturbing the striatal dopamine system.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008
    Article
  19. Evidence for defective mesolimbic dopamine exocytosis in obesity-prone rats.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008
    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

8 authors at 4 institutions in 2 countries.

M HöltjeInstitut für Anatomie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.
B von Jagow
I Pahner
M Lautenschlager
H Hörtnagl
B Nürnberg
R Jahn
G Ahnert-Hilger
Institut de Chimie · FRCharité - Universitätsmedizin Berlin · DEFreie Universität Berlin · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monoamines such as noradrenaline and serotonin are stored in secretory vesicles and released by exocytosis. Two related monoamine transporters, VMAT1 and VMAT2, mediate vesicular transmitter uptake. Previously we have reported that in the rat pheochromocytoma cell line PC 12 VMAT1, localized to peptide-containing secretory granules, is controlled by the heterotrimeric G-protein Go(2). We now show that in BON cells, a human serotonergic neuroendocrine cell line derived from a pancreatic tumor expressing both transporters on large, dense-core vesicles, VMAT2 is even more sensitive to G-protein regulation than VMAT1. The activity of both transporters is only downregulated by Galphao(2), whereas comparable concentrations of Galphao(1) are without effect. In serotonergic raphe neurons in primary culture VMAT2 is also downregulated by pertussis toxin-sensitive Go(2). By electron microscopic analysis from prefrontal cortex we show that VMAT2 and Galphao(2) associate preferentially to locally recycling small synaptic vesicles in serotonergic terminals. In addition, Go(2)-dependent modulation of VMAT2 also works when using a crude synaptic vesicle preparation from this brain area. We conclude that regulation of monoamine uptake by the heterotrimeric G proteins is a general feature of monoaminergic neurons that controls the content of both large, dense-core and small synaptic vesicles.

Indexed as

Membrane Transport ProteinsNeuropeptidesAnimalsCarcinoid TumorCell Membrane PermeabilityDown-RegulationGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gi-GoHeterotrimeric GTP-Binding ProteinsHistamineHumansMembrane GlycoproteinsMicroscopy, ImmunoelectronNeuronal PlasticityNeuronsPancreatic NeoplasmsGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gi-GoHeterotrimeric GTP-Binding ProteinsHistamineMembrane GlycoproteinsMembrane Transport ProteinsNeuropeptidesolfactory G protein subunit alpha olfRecombinant Fusion ProteinsSerotoninSLC18A1 protein, humanSlc18a1 protein, ratSLC18A2 protein, humanSlc18a2 protein, ratTritiumVesicular Biogenic Amine Transport ProteinsVesicular Monoamine Transport Proteins

Identifiers

PMID10704487
PMCPMC6772484
OpenAlexW2151942681

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.