Evidence map›Paper›PMID 24596153›Full record

ArticleeLife2014

Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion.

Michael Zick, Christopher Stroupe, Amy Orr, Deborah Douville, William T Wickner

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

59 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Review
  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. Review
  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.

Michael ZickDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, United States.
Christopher Stroupe
Amy Orr
Deborah Douville
William T Wickner
Dartmouth College · USUniversity of Virginia · US

Funding

THE ASSEMBLY OF PROTEINS INTO BIOLOGICAL MEMBRANESR01GM023377 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WICKNER, WILLIAM TOBEY · 1985 to 2015
$17.9M
NIGMS NIH HHS R01 GM023377NIGMS NIH HHS R01 GM23377-38
6 · The paper itself

Abstract

Like other intracellular fusion events, the homotypic fusion of yeast vacuoles requires a Rab GTPase, a large Rab effector complex, SNARE proteins which can form a 4-helical bundle, and the SNARE disassembly chaperones Sec17p and Sec18p. In addition to these proteins, specific vacuole lipids are required for efficient fusion in vivo and with the purified organelle. Reconstitution of vacuole fusion with all purified components reveals that high SNARE levels can mask the requirement for a complex mixture of vacuole lipids. At lower, more physiological SNARE levels, neutral lipids with small headgroups that tend to form non-bilayer structures (phosphatidylethanolamine, diacylglycerol, and ergosterol) are essential. Membranes without these three lipids can dock and complete trans-SNARE pairing but cannot rearrange their lipids for fusion. DOI: http://dx.doi.org/10.7554/eLife.01879.001.

Indexed as

Membrane FusionMembranes, ArtificialAdenosine TriphosphatasesBinding SitesMembrane LipidsMolecular StructureProtein BindingProtein ConformationProteolipidsQ-SNARE ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsTime FactorsVacuolesVesicular Transport ProteinsAdenosine TriphosphatasesMembrane LipidsMembranes, ArtificialProteolipidsproteoliposomesQ-SNARE ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEC17 protein, S cerevisiaeSEC18 protein, S cerevisiaeSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVesicular Transport Proteinsdiacylglycerolergosterolmembrane fusionphosphatidylethanolamineSNAREs

Identifiers

PMID24596153
PMCPMC3937803
OpenAlexW2150052026

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.