Evidence map›Paper›PMID 28739947›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Morphologies of synaptic protein membrane fusion interfaces.

Preeti Gipson, Yoshiyuki Fukuda, Radostin Danev, Ying Lai, Dong-Hua Chen, Wolfgang Baumeister, Axel T Brunger

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed, 64 citations in OpenAlex.

  1. Synaptic transmission: Munc13 assembles onto PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. 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
  7. Review
  8. Taking a closer look at the synapse.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Handling Difficult Cryo-ET Samples: A Study with Primary Neurons from Drosophila melanogaster.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2023
    Article
  11. Article
  12. Article
  13. The Core Complex of the CaJournal of molecular biology · 2023
    Review
  14. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Preeti GipsonDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305.
Yoshiyuki FukudaDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Radostin DanevDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Ying LaiDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305.
Dong-Hua ChenDepartment of Structural Biology, Stanford University, Stanford, CA 94305.
Wolfgang BaumeisterDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Axel T BrungerDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305; brunger@stanford.edu.
Max Planck Institute of Biochemistry · DEHoward Hughes Medical Institute · USStanford University · US

Funding

Single molecule studies of SNARE-induced vesicle fusionR37MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2011 to 2020
$4.7M
Howard Hughes Medical InstituteNIMH NIH HHS R37 MH063105
6 · The paper itself

Abstract

Neurotransmitter release is orchestrated by synaptic proteins, such as SNAREs, synaptotagmin, and complexin, but the molecular mechanisms remain unclear. We visualized functionally active synaptic proteins reconstituted into proteoliposomes and their interactions in a native membrane environment by electron cryotomography with a Volta phase plate for improved resolvability. The images revealed individual synaptic proteins and synaptic protein complex densities at prefusion contact sites between membranes. We observed distinct morphologies of individual synaptic proteins and their complexes. The minimal system, consisting of neuronal SNAREs and synaptotagmin-1, produced point and long-contact prefusion states. Morphologies and populations of these states changed as the regulatory factors complexin and Munc13 were added. Complexin increased the membrane separation, along with a higher propensity of point contacts. Further inclusion of the priming factor Munc13 exclusively restricted prefusion states to point contacts, all of which efficiently fused upon Ca

Indexed as

Membrane FusionAnimalsCalciumCryoelectron MicroscopyMembrane Fusion ProteinsModels, MolecularNerve Tissue ProteinsNeuronsProtein BindingProtein DomainsProteolipidsSNARE ProteinsSynaptic MembranesSynaptic VesiclesSynaptotagmin ICalciumMembrane Fusion ProteinsNerve Tissue ProteinsProteolipidsproteoliposomesSNARE ProteinsSynaptotagmin Ielectron cryotomographyMunc13neurotransmitter releasesynaptic vesicle fusionVolta phase plate

Identifiers

PMID28739947
PMCPMC5576828
OpenAlexW2738720031

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.