Evidence map›Paper›PMID 19386605›Full record

ArticleThe Journal of biological chemistry2009

The major role of the Rab Ypt7p in vacuole fusion is supporting HOPS membrane association.

Christopher M Hickey, Christopher Stroupe, William Wickner

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Regulation of vacuole fusion in stomata by dephosphorylation of the HOPS subunit VPS39.The Plant journal : for cell and molecular biology · 2025
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  9. A Rab prenyl membrane-anchor allows effector recognition to be regulated by guanine nucleotide.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Phosphoinositides control the localization of HOPS subunit VPS41, which together with VPS33 mediates vacuole fusion in plants.Proceedings of the National Academy of Sciences of the United States of America · 2018
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  19. Bioengineered yeast-derived vacuoles with enhanced tissue-penetrating ability for targeted cancer therapy.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016
    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.

Christopher M HickeyFrom the Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755.
Christopher StroupeFrom the Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755.
William WicknerFrom the Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755. Electronic address: Bill.Wickner@dartmouth.edu.

Funding

THE ASSEMBLY OF PROTEINS INTO BIOLOGICAL MEMBRANESR01GM023377 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WICKNER, WILLIAM TOBEY · 1985 to 2015
$17.9M
Molecular and Cellular Biology at DartmouthT32GM008704 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 1998 to 2018
$6.8M
AUTOIMMUNITY &CONNECTIVE TISSUE BIOLOGY TRAININGT32AR007576 · NIAMS · DARTMOUTH COLLEGE · PI RIGBY, WILLIAM FREDERICK CARSON · 1994 to 2008
$1.7M
NIAMS NIH HHS T32 AR007576NIAMS NIH HHS T32AR007576NIGMS NIH HHS R01 GM023377NIGMS NIH HHS R01GM23377NIGMS NIH HHS T32 GM008704NIGMS NIH HHS T32GM008704
6 · The paper itself

Abstract

Yeast vacuole fusion requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), the Rab GTPase Ypt7p, vacuolar lipids, Sec17p and Sec18p, and the homotypic fusion and vacuole protein sorting complex (HOPS). HOPS is a multisubunit protein with direct affinities for SNAREs, vacuolar lipids, and the GTP-bound form of Ypt7p; each of these affinities contributes to HOPS association with the organelle. Using all-purified components, we have reconstituted fusion, but the Rab Ypt7p was not required. We now report that phosphorylation of HOPS by the vacuolar kinase Yck3p blocks HOPS binding to vacuolar lipids, making HOPS membrane association and the ensuing fusion depend on the presence of Ypt7p. In accord with this finding in the reconstituted fusion reaction, the inactivation of Ypt7p by the GTPase-activating protein Gyp1-46p only blocks the fusion of purified vacuoles when Yck3p is present and active. Thus, although Ypt7p may contribute to other fusion functions, its central role is to bind HOPS to the membrane.

Indexed as

Casein Kinase IMembrane FusionMembrane ProteinsPhosphorylationrab GTP-Binding ProteinsRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsVacuolesCasein Kinase IMembrane Proteinsrab GTP-Binding ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsYCK3 protein, S cerevisiaeYPT7 protein, S cerevisiae

Identifiers

PMID19386605
PMCPMC2713515

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.