Evidence map›Paper›PMID 28137749›Full record

ArticleThe EMBO journal2017

Conformational change of syntaxin linker region induced by Munc13s initiates SNARE complex formation in synaptic exocytosis.

Shen Wang, Ucheor B Choi, Jihong Gong, Xiaoyu Yang, Yun Li, Austin L Wang, Xiaofei Yang, Axel T Brunger, Cong Ma

Abstract read
In one paragraph

Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing 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

65 citing papers in PubMed.

  1. Article
  2. 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
  3. Article
  4. Article
  5. Article
  6. 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
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Article
  20. Review

5 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

9 authors.

Shen WangKey Laboratory of Molecular Biophysics of Ministry of Education, College of Life Science and Technology and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, Wuhan, China.ORCID 0000-0002-5013-1039
Ucheor B ChoiDepartments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Photon Science, and Structural Biology, Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA.
Jihong GongKey Laboratory of Cognitive Science, Hubei Key Laboratory of Medical Information Analysis and Tumor Diagnosis & Treatment, Laboratory of Membrane Ion Channels and Medicine, College of Biomedical Engineering, College of Life Science, South-Central University for Nationalities, Wuhan, China.
Xiaoyu YangKey Laboratory of Molecular Biophysics of Ministry of Education, College of Life Science and Technology and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, Wuhan, China.
Yun LiKey Laboratory of Molecular Biophysics of Ministry of Education, College of Life Science and Technology and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, Wuhan, China.
Austin L WangDepartments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Photon Science, and Structural Biology, Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA.
Xiaofei YangKey Laboratory of Cognitive Science, Hubei Key Laboratory of Medical Information Analysis and Tumor Diagnosis & Treatment, Laboratory of Membrane Ion Channels and Medicine, College of Biomedical Engineering, College of Life Science, South-Central University for Nationalities, Wuhan, China sunlittlefly@hotmail.com brunger@stanford.edu cong.ma@hust.edu.cn.
Axel T BrungerDepartments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Photon Science, and Structural Biology, Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA sunlittlefly@hotmail.com brunger@stanford.edu cong.ma@hust.edu.cn.
Cong MaKey Laboratory of Molecular Biophysics of Ministry of Education, College of Life Science and Technology and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, Wuhan, China sunlittlefly@hotmail.com brunger@stanford.edu cong.ma@hust.edu.cn.ORCID 0000-0002-7814-0500

Funding

STRUCTURE OF PROTEINS INVOLVED IN SYNAPTIC EXOCYTOSISR01MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2000 to 2025
$4.7M
Single molecule studies of SNARE-induced vesicle fusionR37MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2011 to 2020
$4.7M
NIMH NIH HHS R01 MH063105NIMH NIH HHS R37 MH063105
6 · The paper itself

Abstract

The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein syntaxin-1 adopts a closed conformation when bound to Munc18-1, preventing binding to synaptobrevin-2 and SNAP-25 to form the ternary SNARE complex. Although it is known that the MUN domain of Munc13-1 catalyzes the transition from the Munc18-1/syntaxin-1 complex to the SNARE complex, the molecular mechanism is unclear. Here, we identified two conserved residues (R151, I155) in the syntaxin-1 linker region as key sites for the MUN domain interaction. This interaction is essential for SNARE complex formation

Indexed as

ExocytosisAnimalsCells, CulturedHumansModels, BiologicalMunc18 ProteinsNerve Tissue ProteinsNeuronsProtein ConformationQa-SNARE ProteinsRatsSNARE ProteinsSynapsesMunc18 ProteinsNerve Tissue ProteinsQa-SNARE ProteinsSNARE ProteinsStxbp1 protein, ratUnc13a protein, ratMunc13Munc18neurotransmitter releasesynaptic vesicle fusionsyntaxin

Identifiers

PMID28137749
PMCPMC5350566

What OpenQuestion holds

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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.