Evidence map›Paper›PMID 22940675›Full record

ArticleNature structural & molecular biology2012

Controlling synaptotagmin activity by electrostatic screening.

Yongsoo Park, Javier M Hernandez, Geert van den Bogaart, Saheeb Ahmed, Matthew Holt, Dietmar Riedel, Reinhard Jahn

Open access · bronzeAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

45 citing papers in PubMed, 84 citations in OpenAlex.

  1. Synaptotagmin-1 serves as a primary ZnNature communications · 2025
    Article
  2. CaScience advances · 2025
    Article
  3. Article
  4. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  5. Article
  6. Article
  7. Synaptotagmin rings as high-sensitivity regulators of synaptic vesicle docking and fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Isolation of Synaptic Vesicles from Mammalian Brain.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structural basis for the clamping and CaNature communications · 2019
    Article
  17. Unraveling the mechanisms of calcium-dependent secretion.The Journal of general physiology · 2019
    Review
  18. Article
  19. Mechanism of neurotransmitter release coming into focus.Protein science : a publication of the Protein Society · 2018
    Review
  20. Review
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

7 authors at 1 institution in 1 country.

Yongsoo ParkDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Javier M Hernandez
Geert van den Bogaart
Saheeb Ahmed
Matthew Holt
Dietmar Riedel
Reinhard Jahn
Max Planck Institute for Biophysical Chemistry · DE

Funding

Structural Dynamics of the Exocytotic Fusion Machine in Neurons.P01GM072694 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI TAMM, LUKAS K · 2005 to 2021
$17.4M
NIGMS NIH HHS 2 P01 GM072694-06A1NIGMS NIH HHS P01 GM072694
6 · The paper itself

Abstract

Exocytosis of neurosecretory vesicles is mediated by the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins syntaxin-1, synaptobrevin and SNAP-25, with synaptotagmin functioning as the major Ca(2+) sensor for triggering membrane fusion. Here we show that bovine chromaffin granules readily fuse with large unilamellar liposomes in a SNARE-dependent manner. Fusion is enhanced by Ca(2+), but only when the target liposomes contain phosphatidylinositol-4,5-bisphosphate and when polyphosphate anions, such as nucleotides or pyrophosphate, are present. Ca(2+)-dependent enhancement is mediated by endogenous synaptotagmin-1. Polyphosphates operate by an electrostatic mechanism that reverses an inactivating cis association of synaptotagmin-1 with its own membrane without affecting trans binding. Hence, the balancing of trans- and cis-membrane interactions of synaptotagmin-1 could be a crucial element in the pathway of Ca(2+)-dependent exocytosis.

Indexed as

Adenosine TriphosphateAnimalsCalciumCattleChromaffin GranulesExocytosisLiposomesMembrane FusionPhosphatidylinositol 4,5-DiphosphatePhospholipidsPolyphosphatesRatsSNARE ProteinsStatic ElectricitySynaptosomal-Associated Protein 25Synaptotagmin IAdenosine TriphosphateCalciumLiposomesPhosphatidylinositol 4,5-DiphosphatePhospholipidsPolyphosphatesSnap25 protein, ratSNARE ProteinsSynaptosomal-Associated Protein 25Synaptotagmin ISyntaxin 1

Identifiers

PMID22940675
PMCPMC3465474
OpenAlexW2053515408

What OpenQuestion holds

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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.