Evidence map›Paper›PMID 30482862›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Molecular mechanism of fusion pore formation driven by the neuronal SNARE complex.

Satyan Sharma, Manfred Lindau

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Molecular Dynamics Simulation for Membrane Fusion.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  9. Assignment of a Physical Energy Scale for the Dimensionless Interaction Energies within the PRIME20 Peptide Model.Chemphyschem : a European journal of chemical physics and physical chemistry · 2024
    Article
  10. Review
  11. Article
  12. Molecular mechanism underlying SNARE-mediated membrane fusion enlightened by all-atom molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  14. All SNAP25 molecules in the vesicle-plasma membrane contact zone change conformation during vesicle priming.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. CHARMM-GUIJournal of chemical theory and computation · 2023
    Review
  17. Review
  18. Article
  19. 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

2 authors at 2 institutions in 2 countries.

Satyan SharmaLaboratory for Nanoscale Cell Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany satyan.sharma@mpibpc.mpg.de.ORCID 0000-0001-5732-7002
Manfred LindauLaboratory for Nanoscale Cell Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.ORCID 0000-0002-5722-9557
Cornell University · USMax Planck Institute for Biophysical Chemistry · DE

Funding

Mechanisms of Vesicle Fusion and Transmitter ReleaseR01GM121787 · NIGMS · CORNELL UNIVERSITY · PI LINDAU, MANFRED · 2017 to 2020
$1.3M
NIGMS NIH HHS R01 GM121787
6 · The paper itself

Abstract

Release of neurotransmitters from synaptic vesicles begins with a narrow fusion pore, the structure of which remains unresolved. To obtain a structural model of the fusion pore, we performed coarse-grained molecular dynamics simulations of fusion between a nanodisc and a planar bilayer bridged by four partially unzipped SNARE complexes. The simulations revealed that zipping of SNARE complexes pulls the polar C-terminal residues of the synaptobrevin 2 and syntaxin 1A transmembrane domains to form a hydrophilic core between the two distal leaflets, inducing fusion pore formation. The estimated conductances of these fusion pores are in good agreement with experimental values. Two SNARE protein mutants inhibiting fusion experimentally produced no fusion pore formation. In simulations in which the nanodisc was replaced by a 40-nm vesicle, an extended hemifusion diaphragm formed but a fusion pore did not, indicating that restricted SNARE mobility is required for rapid fusion pore formation. Accordingly, rapid fusion pore formation also occurred in the 40-nm vesicle system when SNARE mobility was restricted by external forces. Removal of the restriction is required for fusion pore expansion.

Indexed as

CytoplasmDiaphragmHydrophobic and Hydrophilic InteractionsMembrane FusionMembrane ProteinsModels, StructuralMutant ProteinsNeuronsNeurotransmitter AgentsProtein DomainsSNARE ProteinsSynaptic VesiclesSyntaxin 1Vesicle-Associated Membrane Protein 2Membrane ProteinsMutant ProteinsNeurotransmitter AgentsSNARE ProteinsSyntaxin 1Vesicle-Associated Membrane Protein 2exocytosismembrane fusionmolecular dynamicsnanodisctransmitter release

Identifiers

PMID30482862
PMCPMC6294955
OpenAlexW2902332755

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.