Evidence map›Paper›PMID 23469084›Full record

ArticlePloS one2013

Differential roles for snapin and synaptotagmin in the synaptic vesicle cycle.

Szi-Chieh Yu, Susan M Klosterman, Ashley A Martin, Elena O Gracheva, Janet E Richmond

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Review
  6. Article
  7. Snapin Specifically Up-Regulates CaInternational journal of molecular sciences · 2021
    Article
  8. Article
  9. Article
  10. SNT-1 Functions as the CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  11. The presynaptic machinery at the synapse of C. elegans.Invertebrate neuroscience : IN · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. 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 2 institutions in 1 country.

Szi-Chieh YuBiological Sciences, University of Illinois at Chicago, Chicago, Illinois, United States of America.
Susan M Klosterman
Ashley A Martin
Elena O Gracheva
Janet E Richmond
University of Illinois Chicago · USYale University · US

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
The role of tomosyn in synaptic transmission.R01MH073156 · NIMH · UNIVERSITY OF ILLINOIS AT CHICAGO · PI RICHMOND, JANET E · 2006 to 2010
$2.0M
NIH HHS P40 OD010440NIMH NIH HHS R01 MH073156NIMH NIH HHS R01 MH073156-03
6 · The paper itself

Abstract

Evoked synaptic transmission is dependent on interactions between the calcium sensor Synaptotagmin I and the SNARE complex, comprised of Syntaxin, SNAP-25, and Synaptobrevin. Recent evidence suggests that Snapin may be an important intermediate in this process, through simultaneous interactions of Snapin dimers with SNAP-25 and Synaptotagmin. In support of this model, cultured neurons derived from embryonically lethal Snapin null mutant mice exhibit desynchronized release and a reduced readily releasable vesicle pool. Based on evidence that a dimerization-defective Snapin mutation specifically disrupts priming, Snapin is hypothesized to stabilize primed vesicles by structurally coupling Synaptotagmin and SNAP-25. To explore this model in vivo we examined synaptic transmission in viable, adult C. elegans Snapin (snpn-1) mutants. The kinetics of synaptic transmission were unaffected at snpn-1 mutant neuromuscular junctions (NMJs), but the number of docked, fusion competent vesicles was significantly reduced. However, analyses of snt-1 and snt-1;snpn-1 double mutants suggest that the docking role of SNPN-1 is independent of Synaptotagmin. Based on these results we propose that the primary role of Snapin in C. elegans is to promote vesicle priming, consistent with the stabilization of SNARE complex formation through established interactions with SNAP-25 upstream of the actions of Synaptotagmin in calcium-sensing and endocytosis.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsMiceMutationSynaptic VesiclesSynaptotagminsVesicular Transport ProteinsCaenorhabditis elegans Proteinssnpn-1 protein, C elegansSynaptotagminsVesicular Transport Proteins

Identifiers

PMID23469084
PMCPMC3585204
OpenAlexW1984502589

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.