Evidence map›Paper›PMID 17082764›Full record

ArticleThe EMBO journal2006

Reversible, cooperative reactions of yeast vacuole docking.

Youngsoo Jun, Naomi Thorngren, Vincent J Starai, Rutilio A Fratti, Kevin Collins, William Wickner

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. In vitro assay using engineered yeast vacuoles for neuronal SNARE-mediated membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  6. Article
  7. Article
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  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Membrane fusion.Nature structural & molecular biology · 2008
    Review
  15. Article
  16. Article
  17. Excess vacuolar SNAREs drive lysis and Rab bypass fusion.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  18. Assays of vacuole fusion resolve the stages of docking, lipid mixing, and content mixing.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  19. Trans-SNARE complex assembly and yeast vacuole membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

6 authors at 1 institution in 1 country.

Youngsoo JunDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
Naomi Thorngren
Vincent J Starai
Rutilio A Fratti
Kevin Collins
William Wickner
Dartmouth College · US

Funding

NIAMS NIH HHS T32 AR97576
6 · The paper itself

Abstract

Homotypic yeast vacuole fusion occurs in three stages: (i) priming reactions, which are independent of vacuole clustering, (ii) docking, in which vacuoles cluster and accumulate fusion proteins and fusion regulatory lipids at a ring-shaped microdomain surrounding the apposed membranes of each docked vacuole, where fusion will occur, and (iii) bilayer fusion/compartment mixing. These stages require vacuolar SNAREs, SNARE-chaperones, GTPases, effector complexes, and chemically minor but functionally important lipids. For each, we have developed specific ligands that block fusion and conditions that reverse each block. Using them, we test whether docking entails a linearly ordered series of catalytic events, marked by sequential acquisition of resistance to inhibitors, or whether docking subreactions are cooperative and/or reversible. We find that each fusion protein and regulatory lipid is needed throughout docking, indicative of a reversible or highly cooperative assembly of the fusion-competent vertex ring. In accord with this cooperativity, vertices enriched in one fusion catalyst are enriched in others. Docked vacuoles finally assemble SNARE complexes, yet still require physiological temperature and lipid rearrangements to complete fusion.

Indexed as

CatalysisIntracellular MembranesLigandsMembrane FusionQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsQ-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSynaptosomal-Associated Protein 25VacuolesLigandsQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsQ-SNARE ProteinsSaccharomyces cerevisiae ProteinsSynaptosomal-Associated Protein 25VAM3 protein, S cerevisiaeVAM7 protein, S cerevisiaeVTI1 protein, S cerevisiae

Identifiers

PMID17082764
PMCPMC1636623
OpenAlexW2157704580

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.