Evidence map›Paper›PMID 32804076›Full record

ArticleeLife2020

The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation.

Travis J Eisemann, Frederick Allen, Kelly Lau, Gregory R Shimamura, Philip D Jeffrey, Frederick M Hughson

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The machinery of vesicle fusion.Current opinion in cell biology · 2023
    Review
  5. Article
  6. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  7. Article
  8. A humanizedmicroPublication biology · 2023
    Article
  9. A dynamic template complex mediates Munc18-chaperoned SNARE assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Review
  11. Article
  12. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022
    Review
  17. Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021
    Review
  18. Review
  19. Article
  20. Extracellular Vesicles (EVs) in Tumor Diagnosis and Therapy.Technology in cancer research & treatment
    Review
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 1 institution in 1 country.

Travis J EisemannDepartment of Molecular Biology, Princeton University, Princeton, United States.ORCID 0000-0003-3602-2677
Frederick Allen *Department of Molecular Biology, Princeton University, Princeton, United States.ORCID 0000-0002-2969-8137
Kelly Lau *Department of Molecular Biology, Princeton University, Princeton, United States.
Gregory R Shimamura *Department of Molecular Biology, Princeton University, Princeton, United States.ORCID 0000-0003-2104-5518
Philip D JeffreyDepartment of Molecular Biology, Princeton University, Princeton, United States.
Frederick M HughsonDepartment of Molecular Biology, Princeton University, Princeton, United States.ORCID 0000-0002-4057-0281
Princeton University · US

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
Training and OutreachP30GM124166 · NIGMS · CORNELL UNIVERSITY · PI RICHARD A. CERIONE · 2019 to 2026
$28.3M
PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Structural Analysis of Membrane Tethering and Fusion ProteinsR01GM071574 · NIGMS · PRINCETON UNIVERSITY · PI HUGHSON, FREDERICK M · 2005 to 2024
$6.8M
NIGMS NIH HHS P30 GM124166NIGMS NIH HHS P30 GM133893NIGMS NIH HHS R01 GM071574NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

Fusion of intracellular trafficking vesicles is mediated by the assembly of SNARE proteins into membrane-bridging complexes. SNARE-mediated membrane fusion requires Sec1/Munc18-family (SM) proteins, SNARE chaperones that can function as templates to catalyze SNARE complex assembly. Paradoxically, the SM protein Munc18-1 traps the Qa-SNARE protein syntaxin-1 in an autoinhibited closed conformation. Here we present the structure of a second SM-Qa-SNARE complex, Vps45-Tlg2. Strikingly, Vps45 holds Tlg2 in an open conformation, with its SNARE motif disengaged from its Habc domain and its linker region unfolded. The domain 3a helical hairpin of Vps45 is unfurled, exposing the presumptive R-SNARE binding site to allow template complex formation. Although Tlg2 has a pronounced tendency to form homo-tetramers, Vps45 can rescue Tlg2 tetramers into stoichiometric Vps45-Tlg2 complexes. Our findings demonstrate that SM proteins can engage Qa-SNAREs using at least two different modes, one in which the SNARE is closed and one in which it is open.

Indexed as

ChaetomiumFungal ProteinsMunc18 ProteinsProtein BindingProtein ConformationQa-SNARE ProteinsRecombinant ProteinsFungal ProteinsMunc18 ProteinsQa-SNARE ProteinsRecombinant Proteinscell biologymembrane fusionmolecular biophysicsnonesec1/munc18 (SM) proteinsSNAREsstructural biology

Identifiers

PMID32804076
PMCPMC7470827
OpenAlexW3050167679

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.