Evidence map›Paper›PMID 30622273›Full record

ArticleNature communications2019

Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly.

Shen Wang, Yun Li, Jihong Gong, Sheng Ye, Xiaofei Yang, Rongguang Zhang, Cong Ma

Abstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing 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

77 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Munc13 serves as a molecular filter for SNARE sorting and assembly in active zone condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Synaptic transmission: Munc13 assembles onto PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Review
  9. Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. A specific negatively charged sequence confers intramolecular regulation on Munc13-1 function in synaptic exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

17 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

7 authors.

Shen WangKey Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 430074, Wuhan, China.ORCID http://orcid.org/0000-0002-5013-1039
Yun LiKey Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 430074, Wuhan, China.
Jihong GongKey Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 430074, Wuhan, China.
Sheng YeNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, China.
Xiaofei YangKey Laboratory of Cognitive Science, Hubei Key Laboratory of Medical Information Analysis and Tumor Diagnosis and Treatment, Laboratory of Membrane Ion Channels and Medicine, College of Biomedical Engineering, South-Central University for Nationalities, 430074, Wuhan, China.
Rongguang ZhangNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, China.
Cong MaKey Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 430074, Wuhan, China. cong.ma@hust.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly.

Indexed as

AnimalsExocytosisGene Knockdown TechniquesHEK293 CellsHumansMiceMunc18 ProteinsNerve Tissue ProteinsNeuronsPrimary Cell CultureProtein BindingProtein DomainsSynaptosomal-Associated Protein 25Syntaxin 1Vesicle-Associated Membrane Protein 2Munc18 ProteinsNerve Tissue ProteinsSNAP25 protein, humanStx1a protein, ratStxbp1 protein, ratSynaptosomal-Associated Protein 25Syntaxin 1Unc13a protein, mouseUnc13a protein, ratVamp2 protein, ratVesicle-Associated Membrane Protein 2

Identifiers

PMID30622273
PMCPMC6325239

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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.