Evidence map›Paper›PMID 23395379›Full record

ArticleNeuron2013

LTP requires a unique postsynaptic SNARE fusion machinery.

Sandra Jurado, Debanjan Goswami, Yingsha Zhang, Alfredo J Miñano Molina, Thomas C Südhof, Robert C Malenka

Open access · bronzeAbstract readVideo-Audio Media
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 130 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed, 1 pooled it
10.3field-weighted citation impact, top 1% 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

130 citing papers in PubMed, 1 synthesis or guideline pooled it, 248 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Postsynaptic Complexin Mediates Constitutive Exocytosis of Nicotinic Acetylcholine Receptor.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Molecular organization of central cholinergic synapses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Review
  20. Understanding the molecular diversity of synapses.Nature reviews. Neuroscience · 2025
    Review

70 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

6 authors at 3 institutions in 2 countries.

Sandra JuradoNancy Pritzker Laboratory, Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, 265 Campus Drive, Stanford, CA 94305, USA.
Debanjan Goswami
Yingsha Zhang
Alfredo J Miñano Molina
Thomas C Südhof
Robert C Malenka
Stanford University · USHoward Hughes Medical Institute · USUniversitat Autònoma de Barcelona · ES

Funding

Role of synaptotagmins and neurexin ligands in homeostatic synaptic plasticityP50MH086403 · NIMH · STANFORD UNIVERSITY · PI DEISSEROTH, KARL A. · 2009 to 2019
$18.4M
Mechanisms of Synaptic Plasticity in the HippocampusR37MH063394 · NIMH · STANFORD UNIVERSITY · PI MALENKA, ROBERT C · 2001 to 2010
$4.1M
Mechanisms of Synaptic Plasticity in the HippocampusR01MH063394 · NIMH · STANFORD UNIVERSITY · PI MALENKA, ROBERT C · 2011 to 2012
$893k
Howard Hughes Medical InstituteNIMH NIH HHS MH063394NIMH NIH HHS MH086403NIMH NIH HHS P50 MH086403NIMH NIH HHS R01 MH063394NIMH NIH HHS R37 MH063394
6 · The paper itself

Abstract

Membrane fusion during exocytosis is mediated by assemblies of SNARE (soluble NSF-attachment protein receptor) and SM (Sec1/Munc18-like) proteins. The SNARE/SM proteins involved in vesicle fusion during neurotransmitter release are well understood, whereas little is known about the protein machinery that mediates activity-dependent AMPA receptor (AMPAR) exocytosis during long-term potentiation (LTP). Using direct measurements of LTP in acute hippocampal slices and an in vitro LTP model of stimulated AMPAR exocytosis, we demonstrate that the Q-SNARE proteins syntaxin-3 and SNAP-47 are required for regulated AMPAR exocytosis during LTP but not for constitutive basal AMPAR exocytosis. In contrast, the R-SNARE protein synaptobrevin-2/VAMP2 contributes to both regulated and constitutive AMPAR exocytosis. Both the central complexin-binding and the N-terminal Munc18-binding sites of syntaxin-3 are essential for its postsynaptic role in LTP. Thus, postsynaptic exocytosis of AMPARs during LTP is mediated by a unique fusion machinery that is distinct from that used during presynaptic neurotransmitter release.

Indexed as

AnimalsAnimals, NewbornBiophysicsCells, CulturedElectric StimulationExcitatory Amino Acid AntagonistsExocytosisGene Transfer TechniquesGlycineHippocampusIn Vitro TechniquesLong-Term PotentiationMembrane FusionMiceMice, Inbred C57BLNeurons2,3-dioxo-6-nitro-7-sulfamoylbenzo(f)quinoxalineExcitatory Amino Acid AntagonistsGlycineQa-SNARE ProteinsQuinoxalinesReceptors, AMPAReceptors, TransferrinSNARE ProteinsSyntaxin 1Vesicle-Associated Membrane Protein 2Vesicular Transport Proteins

Identifiers

PMID23395379
PMCPMC3569727
OpenAlexW2012632097

What OpenQuestion holds

Textmetadata
LicenceTDM
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.