Evidence map›Paper›PMID 21987819›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

A lipid-anchored SNARE supports membrane fusion.

Hao Xu, Michael Zick, William T Wickner, Youngsoo Jun

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Molecular mechanism underlying SNARE-mediated membrane fusion enlightened by all-atom molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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
  10. Mechanism of neurotransmitter release coming into focus.Protein science : a publication of the Protein Society · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. SM protein Munc18-2 facilitates transition of Syntaxin 11-mediated lipid mixing to complete fusion for T-lymphocyte cytotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Review
  16. Hemifusion in Synaptic Vesicle Cycle.Frontiers in molecular neuroscience · 2017
    Review
  17. Review
  18. Review
  19. Article
  20. 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.

Hao XuDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755-3844, USA.
Michael Zick
William T Wickner
Youngsoo Jun

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 R-SNAREs and Q-SNAREs to assemble into a four-helical parallel coiled-coil, with their hydrophobic anchors spanning the two apposed membranes. Based on the fusion properties of chemically defined SNARE- proteoliposomes, it has been proposed that the assembly of this helical bundle transduces force through the entire bilayer via the transmembrane SNARE anchor domains to drive fusion. However, an R-SNARE, Nyv1p, with a genetically engineered lipid anchor that spans half of the bilayer suffices for the fusion of isolated vacuoles, although this organelle has other R-SNAREs. To demonstrate unequivocally the fusion activity of lipid-anchored Nyv1p, we reconstituted proteoliposomes with purified lipid-anchored Nyv1p as the only protein. When these proteoliposomes were incubated with those bearing cognate Q-SNAREs, there was trans-SNARE complex assembly but, in accord with prior studies of the neuronal SNAREs, little lipid mixing. However, the addition of physiological fusion accessory proteins (HOPS, Sec17p, and Sec18p) allows lipid-anchored Nyv1p to support fusion, suggesting that trans-SNARE complex function is not limited to force transduction across the bilayers through the transmembrane domains.

Indexed as

Lipid-Linked ProteinsMembrane FusionMembrane ProteinsProtein MultimerizationProteolipidsQ-SNARE ProteinsRecombinant ProteinsR-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsVacuolesLipid-Linked ProteinsMembrane ProteinsNyv1 protein, S cerevisiaeProteolipidsproteoliposomesQ-SNARE ProteinsRecombinant ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNARE Proteins

Identifiers

PMID21987819
PMCPMC3198343

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.