Evidence map›Paper›PMID 10908612›Full record

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

The SNARE Vti1a-beta is localized to small synaptic vesicles and participates in a novel SNARE complex.

W Antonin, D Riedel, G F von Mollard

Open access · greenAbstract 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 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

39 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
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  6. A look beyond the QR code of SNARE proteins.Protein science : a publication of the Protein Society · 2024
    Article
  7. Article
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  10. Review
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  14. Ablation of All Synaptobrevin vSNAREs Blocks Evoked But Not Spontaneous Neurotransmitter Release at Neuromuscular Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  15. Article
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  17. Review
  18. Loss of Doc2-Dependent Spontaneous Neurotransmission Augments Glutamatergic Synaptic Strength.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  19. Review
  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

3 authors at 1 institution in 1 country.

W AntoninZentrum Biochemie und Molekulare Zellbiologie, Abteilung Biochemie II, Universität Göttingen, Germany.
D Riedel
G F von Mollard
Biologie Labor · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specific soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor (SNARE) proteins are required for different membrane transport steps. The SNARE Vti1a has been colocalized with Golgi markers and Vti1b with Golgi and the trans-Golgi network or endosomal markers in fibroblast cell lines. Here we study the distribution of Vti1a and Vti1b in brain. Vti1b was found in synaptic vesicles but was not enriched in this organelle. A brain-specific splice variant of Vti1a was identified that had an insertion of seven amino acid residues next to the putative SNARE-interacting helix. This Vti1a-beta was enriched in small synaptic vesicles and clathrin-coated vesicles isolated from nerve terminals. Vti1a-beta also copurified with the synaptic vesicle R-SNARE synaptobrevin during immunoisolation of synaptic vesicles and endosomes. Therefore, both synaptobrevin and Vti1a-beta are integral parts of synaptic vesicles throughout their life cycle. Vti1a-beta was part of a SNARE complex in nerve terminals, which bound N-ethylmaleimide-sensitive factor and alpha-SNAP. This SNARE complex was different from the exocytic SNARE complex because Vti1a-beta was not coimmunoprecipitated with syntaxin 1 or SNAP-25. These data suggest that Vti1a-beta does not function in exocytosis but in a separate SNARE complex in a membrane fusion step during recycling or biogenesis of synaptic vesicles.

Indexed as

Vesicular Transport ProteinsAlternative SplicingAnimalsAntibodiesBiological TransportBrainCarrier ProteinsClathrinCloning, MolecularCoated VesiclesEndosomesGene ExpressionMembrane ProteinsMicroscopy, ImmunoelectronMolecular Sequence DataMutagenesis, InsertionalAntibodiesCarrier ProteinsClathrinMembrane ProteinsN-Ethylmaleimide-Sensitive ProteinsNsf protein, mouseNsf protein, ratQb-SNARE ProteinsRNA, MessengerR-SNARE ProteinsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsStx1a protein, mouseStx1a protein, ratSynaptophysinSyntaxin 1Vesicular Transport ProteinsVti1a protein, ratVti1b protein, mouse

Identifiers

PMID10908612
PMCPMC6772562
OpenAlexW2137635572

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.