Evidence map›Paper›PMID 36151854›Full record

ReviewCritical reviews in biochemistry and molecular biology2022

Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.

Yongli Zhang, Lu Ma, Huan Bao

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Mutations of Single Residues in the Complexin N-terminus Exhibit Distinct Phenotypes in Synaptic Vesicle Fusion.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. SIP30 involvement in vesicle exocytosis from PC12 cells.Biochemistry and biophysics reports · 2024
    Article
  12. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  13. All SNAP25 molecules in the vesicle-plasma membrane contact zone change conformation during vesicle priming.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. The machinery of vesicle fusion.Current opinion in cell biology · 2023
    Review
  15. Article
  16. Article
  17. A dynamic template complex mediates Munc18-chaperoned SNARE assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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

3 authors at 3 institutions in 2 countries.

Yongli ZhangDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.ORCID 0000-0001-7079-7973
Lu MaDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Huan BaoDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL, USA.ORCID 0000-0002-4301-4627
Chinese Academy of Sciences · CNScripps Research Institute · USYale University · US

Funding

Single-molecule studies of SNARE assembly and lipid transferR35GM131714 · NIGMS · YALE UNIVERSITY · PI Yongli Zhang · 2019 to 2026
$5.0M
Developing next-generation nanodiscs for the study and modulation of membrane proteinsDP2GM140920 · NIGMS · UNIVERSITY OF VIRGINIA · PI BAO, HUAN · 2020 to 2020
$2.7M
NIGMS NIH HHS DP2 GM140920NIGMS NIH HHS R35 GM131714
6 · The paper itself

Abstract

Fusion of transmitter-containing vesicles with plasma membranes at the synaptic and neuromuscular junctions mediates neurotransmission and muscle contractions, respectively, thereby underlying all thoughts and actions. The fusion process is driven by the coupled folding and assembly of three synaptic SNARE proteins--syntaxin-1 and SNAP-25 on the target plasma membrane (t-SNAREs) and VAMP2 on the vesicular membrane (v-SNARE) into a four-helix bundle. Their assembly is chaperoned by Munc18-1 and many other proteins to achieve the speed and accuracy required for neurotransmission. However, the physiological pathway of SNARE assembly and its coupling to membrane fusion remains unclear. Here, we review recent progress in understanding SNARE assembly and membrane fusion, with a focus on results obtained by single-molecule manipulation approaches and electric recordings of single fusion pores. We describe two pathways of synaptic SNARE assembly, their associated intermediates, energetics, and kinetics. Assembly of the three SNAREs

Indexed as

Membrane FusionSNARE ProteinsKineticsMunc18 ProteinsQa-SNARE ProteinsVesicle-Associated Membrane Protein 2Munc18 ProteinsQa-SNARE ProteinsSNARE ProteinsVesicle-Associated Membrane Protein 2electric recordingfusion poresmembrane fusionMunc18-1optical tweezersprotein foldingSNAREstemplate complexes

Identifiers

PMID36151854
PMCPMC9588726
OpenAlexW4297183488

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.