Evidence map›Paper›PMID 18552827›Full record

ArticleNature structural & molecular biology2008

Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion.

Xiaobing Lu, Yinghui Zhang, Yeon-Kyun Shin

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Membrane fusion byMolecular biology of the cell · 2022
    Article
  4. The Magnetosome Protein, Mms6 fromInternational journal of molecular sciences · 2022
    Article
  5. SNARE zippering requires activation by SNARE-like peptides in Sec1/Munc18 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Syntaxin1A lateral diffusion reveals transient and local SNARE interactions.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  19. Article
  20. 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

3 authors.

Xiaobing LuDepartment of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
Yinghui Zhang
Yeon-Kyun Shin

Funding

Regulations of SNARE-dependent membrane fusionR01GM051290 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SHIN, YEON-KYUN · 1999 to 2019
$5.0M
Yeast SNARE Assembly and Membrane FusionR01GM067629 · NIGMS · IOWA STATE UNIVERSITY · PI SHIN, YEON-KYUN · 2003 to 2010
$1.9M
NIGMS NIH HHS R01 GM051290NIGMS NIH HHS R01 GM067629
6 · The paper itself

Abstract

Formation of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex facilitates intracellular membrane fusion. A single SNARE complex is thought to be insufficient; multiple copies of SNARE complexes must work cooperatively. However, the mechanism by which such a higher-order SNARE protein structure is assembled is unknown. EPR and fluorescence analyses show that at least three copies of target-membrane SNARE proteins self-assemble through the interaction between the transmembrane domains (TMDs), and this multimeric structure serves as scaffolding for trans-SNARE assembly. SNARE core formation in solution induces oligomerization of the TMDs of vesicle-associated SNAREs in the apposing membrane, transiently forming a supramolecular protein structure spanning two membranes. This higher-order protein intermediate evolves, by involving lipid molecules, to the hemifusion state. Hemifusion is subsequently followed by distal leaflet mixing and formation of the cis-SNARE complex.

Indexed as

Electron Spin Resonance SpectroscopyFluorescenceKineticsMembrane FusionModels, BiologicalProtein Structure, QuaternaryProtein Structure, TertiaryQa-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsQa-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsSSO1 protein, S cerevisiae

Identifiers

PMID18552827
PMCPMC2575085

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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.