Evidence map›Paper›PMID 33944780›Full record

ArticleeLife2021

Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering.

Hongki Song, Thomas L Torng, Amy S Orr, Axel T Brunger, William T Wickner

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Regulation of vacuole fusion in stomata by dephosphorylation of the HOPS subunit VPS39.The Plant journal : for cell and molecular biology · 2025
    Article
  3. SNARE disassembly requires Sec18/NSF side loading.Nature structural & molecular biology · 2025
    Article
  4. Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025
    Article
  5. SNARE disassembly requires Sec18/NSF side-loading.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Hongki SongDepartment of Biochemistry and Cell Biology Geisel School of Medicine at Dartmouth, Hanover, United States.ORCID 0000-0002-3761-5434
Thomas L TorngDepartment of Biochemistry and Cell Biology Geisel School of Medicine at Dartmouth, Hanover, United States.ORCID 0000-0003-2295-2777
Amy S OrrDepartment of Biochemistry and Cell Biology Geisel School of Medicine at Dartmouth, Hanover, United States.ORCID 0000-0002-0266-0390
Axel T BrungerHoward Hughes Medical Institute and Department of Molecular and Cellular Physiology Stanford University, Stanford, United States.ORCID 0000-0001-5121-2036
William T WicknerDepartment of Biochemistry and Cell Biology Geisel School of Medicine at Dartmouth, Hanover, United States.ORCID 0000-0001-8431-0468
Dartmouth College · USHoward Hughes Medical Institute · US

Funding

Mechanisms of Membrane FusionR35GM118037 · NIGMS · DARTMOUTH COLLEGE · PI WILLIAM Tobey WICKNER · 2016 to 2026
$8.6M
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
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM118037NIMH NIH HHS R01 MH063105NIMH NIH HHS R37 MH063105
6 · The paper itself

Abstract

Membrane fusion requires R-, Qa-, Qb-, and Qc-family SNAREs that zipper into RQaQbQc coiled coils, driven by the sequestration of apolar amino acids. Zippering has been thought to provide all the force driving fusion. Sec17/αSNAP can form an oligomeric assembly with SNAREs with the Sec17 C-terminus bound to Sec18/NSF, the central region bound to SNAREs, and a crucial apolar loop near the N-terminus poised to insert into membranes. We now report that Sec17 and Sec18 can drive robust fusion without requiring zippering completion. Zippering-driven fusion is blocked by deleting the C-terminal quarter of any Q-SNARE domain or by replacing the apolar amino acids of the Qa-SNARE that face the center of the 4-SNARE coiled coils with polar residues. These blocks, singly or combined, are bypassed by Sec17 and Sec18, and SNARE-dependent fusion is restored without help from completing zippering.

Indexed as

Adenosine TriphosphatasesCell CommunicationMembrane FusionProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVesicular Transport ProteinsAdenosine TriphosphatasesSaccharomyces cerevisiae ProteinsSEC17 protein, S cerevisiaeSEC18 protein, S cerevisiaeSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVesicular Transport Proteinsbiochemistrychemical biologyHOPSmembrane fusionS. cerevisiaeSec17Sec18SNAREsyeast vacuoles

Identifiers

PMID33944780
PMCPMC8143792
OpenAlexW3157245988

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.