Evidence map›Paper›PMID 20937897›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Role of the synaptobrevin C terminus in fusion pore formation.

Annita N Ngatchou, Kassandra Kisler, Qinghua Fang, Alexander M Walter, Ying Zhao, Dieter Bruns, Jakob B Sørensen, Manfred Lindau

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

66 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. A lever hypothesis for Synaptotagmin-1 action in neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. 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
  8. Article
  9. Article
  10. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  11. Review
  12. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  13. The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021
    Review
  18. Review
  19. Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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 at 4 institutions in 3 countries.

Annita N NgatchouSchool of Applied and Engineering Physics, 212 Clark Hall, Cornell University, Ithaca, NY 14853, USA.
Kassandra Kisler
Qinghua Fang
Alexander M Walter
Ying Zhao
Dieter Bruns
Jakob B Sørensen
Manfred Lindau
Max Planck Institute for Biophysical Chemistry · DECornell University · USSaarland University · DEMax Planck Society · DE

Funding

TRAINING IN MOLECULAR PHYSICS OF BIOLOGICAL SYSTEMST32GM008267 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, MICHELLE D. · 1988 to 2021
$9.6M
Mechanisms of Fusion &Transmitter releaseR01NS038200 · NINDS · CORNELL UNIVERSITY ITHACA · PI LINDAU, MANFRED · 2000 to 2007
$2.3M
Mechanisms of fusion and transmitter release in neurosecretionR01GM085808 · NIGMS · CORNELL UNIVERSITY · PI LINDAU, MANFRED · 2008 to 2012
$1.7M
NIGMS NIH HHS R01 GM085808NIGMS NIH HHS R01GM085808NIGMS NIH HHS T32 GM008267NIGMS NIH HHS T32GM008267NINDS NIH HHS R01 NS038200NINDS NIH HHS R01NS38200
6 · The paper itself

Abstract

Neurotransmitter release is mediated by the SNARE proteins synaptobrevin II (sybII, also known as VAMP2), syntaxin, and SNAP-25, generating a force transfer to the membranes and inducing fusion pore formation. However, the molecular mechanism by which this force leads to opening of a fusion pore remains elusive. Here we show that the ability of sybII to support exocytosis is inhibited by addition of one or two residues to the sybII C terminus depending on their energy of transfer from water to the membrane interface, following a Boltzmann distribution. These results suggest that following stimulation, the SNARE complex pulls the C terminus of sybII deeper into the vesicle membrane. We propose that this movement disrupts the vesicular membrane continuity leading to fusion pore formation. In contrast to current models, the experiments suggest that fusion pore formation begins with molecular rearrangements at the intravesicular membrane leaflet and not between the apposed cytoplasmic leaflets.

Indexed as

Amino Acid SequenceAnimalsBiophysical PhenomenaCells, CulturedChromaffin CellsExocytosisIn Vitro TechniquesMembrane FusionMiceMice, KnockoutModels, NeurologicalMolecular Sequence DataMutant ProteinsNeurotransmitter AgentsRatsRecombinant Fusion ProteinsMutant ProteinsNeurotransmitter AgentsRecombinant Fusion ProteinsVamp2 protein, ratVesicle-Associated Membrane Protein 2

Identifiers

PMID20937897
PMCPMC2972926
OpenAlexW1996037892

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.