Evidence map›Paper›PMID 24778182›Full record

ArticleThe Journal of biological chemistry2014

α-SNAP interferes with the zippering of the SNARE protein membrane fusion machinery.

Yongsoo Park, Wensi Vennekate, Halenur Yavuz, Julia Preobraschenski, Javier M Hernandez, Dietmar Riedel, Peter Jomo Walla, Reinhard Jahn

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Article
  2. CaScience advances · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Selected tools to visualize membrane interactions.European biophysics journal : EBJ · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  13. Mechanism of neurotransmitter release coming into focus.Protein science : a publication of the Protein Society · 2018
    Review
  14. Article
  15. Arrest ofThe Journal of biological chemistry · 2018
    Article
  16. Article
  17. Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Protein science : a publication of the Protein Society · 2017
    Review
  18. Article
  19. Gasotransmitter Heterocellular Signaling.Antioxidants & redox signaling · 2017
    Article
  20. NaeLife · 2017
    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.

Yongsoo ParkFrom the Department of Neurobiology.
Wensi VennekateFrom the Department of Neurobiology, the AG Biomolecular Spectroscopy and Single-Molecule Detection, and.
Halenur YavuzFrom the Department of Neurobiology.
Julia PreobraschenskiFrom the Department of Neurobiology.
Javier M HernandezFrom the Department of Neurobiology.
Dietmar Riedelthe Facility for Electron Microscopy, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen and.
Peter Jomo Wallathe AG Biomolecular Spectroscopy and Single-Molecule Detection, and the Department of Biophysical Chemistry, Institute for Physical and Theoretical Chemistry, Technical University of Braunschweig, 38106 Braunschweig, Germany.
Reinhard JahnFrom the Department of Neurobiology, rjahn@gwdg.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 P01 GM072694
6 · The paper itself

Abstract

Neuronal exocytosis is mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins. Before fusion, SNARE proteins form complexes bridging the membrane followed by assembly toward the C-terminal membrane anchors, thus initiating membrane fusion. After fusion, the SNARE complex is disassembled by the AAA-ATPase N-ethylmaleimide-sensitive factor that requires the cofactor α-SNAP to first bind to the assembled SNARE complex. Using chromaffin granules and liposomes we now show that α-SNAP on its own interferes with the zippering of membrane-anchored SNARE complexes midway through the zippering reaction, arresting SNAREs in a partially assembled trans-complex and preventing fusion. Intriguingly, the interference does not result in an inhibitory effect on synaptic vesicles, suggesting that membrane properties also influence the final outcome of α-SNAP interference with SNARE zippering. We suggest that binding of α-SNAP to the SNARE complex affects the ability of the SNARE complex to harness energy or transmit force to the membrane.

Indexed as

Membrane FusionAnimalsCattleEndocytosisFluorescence PolarizationFluorescence Resonance Energy TransferProteolipidsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsProteolipidsproteoliposomesSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsChromaffin CellsFusion ProteinNeurobiologySoluble NSF Attachment Protein Receptor (SNARE)SynapseVesicles

Identifiers

PMID24778182
PMCPMC4047401

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.