Evidence map›Paper›PMID 29230050›Full record

ArticleNature neuroscience2018

Synaptic weight set by Munc13-1 supramolecular assemblies.

Hirokazu Sakamoto, Tetsuroh Ariyoshi, Naoya Kimpara, Kohtaroh Sugao, Isamu Taiko, Kenji Takikawa, Daisuke Asanuma, Shigeyuki Namiki, Kenzo Hirose

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In one paragraph

Article in Nature neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing 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

151 citing papers in PubMed.

  1. Article
  2. Article
  3. The Synaptic Vesicle Priming Protein Munc13 Mediates Evoked Somatodendritic Dopamine Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  4. Article
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  8. Deciphering the Nanoscale Architecture of Presynaptic Actin Using a Micropatterned Presynapse-on-Glass Model.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  9. Synaptic transmission: Munc13 assembles onto PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Munc13-1 couples DAG and CaScience advances · 2026
    Article
  11. Review
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91 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Hirokazu SakamotoDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Tetsuroh AriyoshiDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Naoya KimparaDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Kohtaroh SugaoDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Isamu TaikoDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Kenji TakikawaDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Daisuke AsanumaDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Shigeyuki NamikiDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Kenzo HiroseDepartment of Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan. kenzoh@m.u-tokyo.ac.jp.ORCID 0000-0002-8944-6513

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The weight of synaptic connections, which is controlled not only postsynaptically but also presynaptically, is a key determinant in neuronal network dynamics. The mechanisms controlling synaptic weight, especially on the presynaptic side, remain elusive. Using single-synapse imaging of the neurotransmitter glutamate combined with super-resolution imaging of presynaptic proteins, we identify a presynaptic mechanism for setting weight in central glutamatergic synapses. In the presynaptic terminal, Munc13-1 molecules form multiple and discrete supramolecular self-assemblies that serve as independent vesicular release sites by recruiting syntaxin-1, a soluble N-ethylmaleimide-sensitive-factor attachment receptor (SNARE) protein essential for synaptic vesicle exocytosis. The multiplicity of these Munc13-1 assemblies affords multiple stable states conferring presynaptic weight, potentially encoding several bits of information at individual synapses. Supramolecular assembling enables a stable synaptic weight, which confers robustness of synaptic computation on neuronal circuits and may be a general mechanism by which biological processes operate despite the presence of molecular noise.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCalciumCells, CulturedCytoskeletal ProteinsEmbryo, MammalianExocytosisGlutamic AcidGTP-Binding ProteinsHippocampusNerve Tissue ProteinsNeuronsNeuropeptidesPresynaptic TerminalsRatsRats, Sprague-DawleyAdaptor Proteins, Signal TransducingCalciumCytoskeletal ProteinsERC1 protein, ratGlutamic AcidGTP-Binding ProteinsNerve Tissue ProteinsNeuropeptidesPclo protein, ratRims1 protein, ratRNA, Small InterferingSyntaxin 1Unc13a protein, ratVesicular Glutamate Transport Protein 1

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.