Evidence map›Paper›PMID 18007597›Full record

ArticleThe EMBO journal2007

Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.

Youngsoo Jun, Hao Xu, Naomi Thorngren, William Wickner

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 37 citations in OpenAlex.

  1. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  2. The Transmembrane Domain of Synaptobrevin Influences Neurotransmitter Flux through Synaptic Fusion Pores.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  8. Article
  9. Article
  10. Article
  11. Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathway.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A lipid-anchored SNARE supports membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Article
  19. Article
  20. Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

4 authors at 1 institution in 1 country.

Youngsoo JunDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755-3844, USA.
Hao Xu
Naomi Thorngren
William Wickner
Dartmouth College · US

Funding

THE ASSEMBLY OF PROTEINS INTO BIOLOGICAL MEMBRANESR01GM023377 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WICKNER, WILLIAM TOBEY · 1985 to 2015
$17.9M
THE ASSEMBLY OF PROTEINS INTO BIOLOGICAL MEMBRANESR37GM023377 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WICKNER, WILLIAM TOBEY · 1988 to 1997
–
NIGMS NIH HHS GM23377NIGMS NIH HHS R01 GM023377
6 · The paper itself

Abstract

Intracellular membrane fusion requires SNARE proteins in a trans-complex, anchored to apposed membranes. Proteoliposome studies have suggested that SNAREs drive fusion by stressing the lipid bilayer via their transmembrane domains (TMDs), and that SNARE complexes require a TMD in each docked membrane to promote fusion. Yeast vacuole fusion is believed to require three Q-SNAREs from one vacuole and the R-SNARE Nyv1p from its fusion partner. In accord with this model, we find that fusion is abolished when the TMD of Nyv1p is replaced by lipid anchors, even though lipid-anchored Nyv1p assembles into trans-SNARE complexes. However, normal fusion is restored by the addition of both Sec18p and the soluble SNARE Vam7p. In restoring fusion, Sec18p promotes the disassembly of trans-SNARE complexes, and Vam7p enhances their assembly. Thus, either the TMD of this R-SNARE is not essential for fusion, and TMD-mediated membrane stress is not the only mode of trans-SNARE complex action, or these SNAREs have more flexibility than heretofore appreciated to form alternate functional complexes that violate the 3Q:1R rule.

Indexed as

Adenosine TriphosphatasesLipid BilayersMembrane FusionMembrane LipidsMembrane ProteinsMultiprotein ComplexesProtein ConformationProtein Structure, TertiaryQa-SNARE ProteinsQc-SNARE ProteinsRecombinant Fusion ProteinsR-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsSynaptosomal-Associated Protein 25Adenosine TriphosphatasesLipid BilayersMembrane LipidsMembrane ProteinsMultiprotein ComplexesNyv1 protein, S cerevisiaeQa-SNARE ProteinsQc-SNARE ProteinsRecombinant Fusion ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEC18 protein, S cerevisiaeSNARE ProteinsSynaptosomal-Associated Protein 25VAM3 protein, S cerevisiaeVAM7 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID18007597
PMCPMC2140102
OpenAlexW2136635037

What OpenQuestion holds

Textmetadata
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.