Evidence map›Paper›PMID 24120845›Full record

ArticleNeuron2013

Lipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter release.

Peng Zhou, Taulant Bacaj, Xiaofei Yang, Zhiping P Pang, Thomas C Südhof

Abstract read
In one paragraph

Article in Neuron, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed.

  1. Review
  2. Article
  3. 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
  4. 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
  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. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  9. Article
  10. Article
  11. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Rapid Capture of Cancer Extracellular Vesicles by Lipid Patch Microarrays.Advanced materials (Deerfield Beach, Fla.) · 2021
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Peng ZhouDepartment of Molecular and Cellular Physiology and Howard Hughes Medical Institute, Stanford University School of Medicine, 265 Campus Drive, Stanford, CA 94305, USA.
Taulant Bacaj
Xiaofei Yang
Zhiping P Pang
Thomas C Südhof

Funding

Role of synaptotagmins and neurexin ligands in homeostatic synaptic plasticityP50MH086403 · NIMH · STANFORD UNIVERSITY · PI CHEN, LU · 2009 to 2019
$18.4M
Large-Scale Molecular Interrogation of Synaptic TransmissionR01NS077906 · NINDS · STANFORD UNIVERSITY · PI CHEN, LU, MALENKA, ROBERT C · 2011 to 2014
$2.5M
A systematic test of the relation of ASD heterogeneity to synaptic functionR01MH089054 · NIMH · STANFORD UNIVERSITY · PI MALENKA, ROBERT C, SUDHOF, THOMAS C. · 2009 to 2010
$1.8M
Role of Doc2 in calcium regulation of synapsesF32NS067896 · NINDS · STANFORD UNIVERSITY · PI BACAJ, TAULANT · 2010 to 2012
$146k
Howard Hughes Medical InstituteNIMH NIH HHS 1R01 MH089054NIMH NIH HHS P50 MH086403NIMH NIH HHS R01 MH089054NINDS NIH HHS 1F32NS067896NINDS NIH HHS F32 NS067896NINDS NIH HHS R01 NS077906
6 · The paper itself

Abstract

Synaptic vesicle fusion during neurotransmitter release is mediated by assembly of SNARE- and SM-protein complexes composed of syntaxin-1, SNAP-25, synaptobrevin-2/VAMP2, and Munc18-1. Current models suggest that SNARE-complex assembly catalyzes membrane fusion by pulling the transmembrane regions (TMRs) of SNARE proteins together, thus allowing their TMRs to form a fusion pore. These models are consistent with the requirement for TMRs in viral fusion proteins. However, the role of the SNARE TMRs in synaptic vesicle fusion has not yet been tested physiologically. Here, we examined whether synaptic SNAREs require TMRs for catalysis of synaptic vesicle fusion, which was monitored electrophysiologically at millisecond time resolution. Surprisingly, we find that both lipid-anchored syntaxin-1 and lipid-anchored synaptobrevin-2 lacking TMRs efficiently promoted spontaneous and Ca(2+)-triggered membrane fusion. Our data suggest that SNARE proteins function during fusion primarily as force generators, consistent with the notion that forcing lipid membranes close together suffices to induce membrane fusion.

Indexed as

AnimalsCells, CulturedInhibitory Postsynaptic PotentialsMembrane FusionMembrane LipidsMiceMice, KnockoutMice, TransgenicNeuronsNeurotransmitter AgentsSNARE ProteinsSynaptic TransmissionSynaptic VesiclesSyntaxin 1Vesicle-Associated Membrane Protein 2Membrane LipidsNeurotransmitter AgentsSNARE ProteinsSyntaxin 1Vesicle-Associated Membrane Protein 2

Identifiers

PMID24120845
PMCPMC3872166

What OpenQuestion holds

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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.