Evidence map›Paper›PMID 24493260›Full record

ArticleEMBO reports2014

SNARE and regulatory proteins induce local membrane protrusions to prime docked vesicles for fast calcium-triggered fusion.

Tanmay A M Bharat, Jörg Malsam, Wim J H Hagen, Andrea Scheutzow, Thomas H Söllner, John A G Briggs

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. TheFrontiers in cell and developmental biology · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Article
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  13. The 2018 biomembrane curvature and remodeling roadmap.Journal of physics D: Applied physics · 2018
    Article
  14. Hydrodynamics govern the pre-fusion docking time of synaptic vesicles.Journal of the Royal Society, Interface · 2018
    Article
  15. Morphologies of synaptic protein membrane fusion interfaces.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Protein science : a publication of the Protein Society · 2017
    Review
  17. Entropic forces drive self-organization and membrane fusion by SNARE proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Review
  19. 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

6 authors at 3 institutions in 2 countries.

Tanmay A M BharatStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Jörg Malsam
Wim J H Hagen
Andrea Scheutzow
Thomas H Söllner
John A G Briggs
Heidelberg University · DEEuropean Molecular Biology Laboratory · DEMRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptic vesicles fuse with the plasma membrane in response to Ca(2+) influx, thereby releasing neurotransmitters into the synaptic cleft. The protein machinery that mediates this process, consisting of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and regulatory proteins, is well known, but the mechanisms by which these proteins prime synaptic membranes for fusion are debated. In this study, we applied large-scale, automated cryo-electron tomography to image an in vitro system that reconstitutes synaptic fusion. Our findings suggest that upon docking and priming of vesicles for fast Ca(2)(+)-triggered fusion, SNARE proteins act in concert with regulatory proteins to induce a local protrusion in the plasma membrane, directed towards the primed vesicle. The SNAREs and regulatory proteins thereby stabilize the membrane in a high-energy state from which the activation energy for fusion is profoundly reduced, allowing synchronous and instantaneous fusion upon release of the complexin clamp.

Indexed as

Membrane FusionCalciumCell MembraneCryoelectron MicroscopyElectron Microscope TomographyHumansMunc18 ProteinsSynaptotagmin IUnilamellar LiposomesVesicle-Associated Membrane Protein 2CalciumMunc18 ProteinsSynaptotagmin IUnilamellar LiposomesVesicle-Associated Membrane Protein 2

Identifiers

PMID24493260
PMCPMC3989697
OpenAlexW2158988413

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.