Evidence map›Paper›PMID 25995379›Full record

ArticleMolecular biology of the cell2015

The HOPS/class C Vps complex tethers membranes by binding to one Rab GTPase in each apposed membrane.

Ruoya Ho, Christopher Stroupe

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
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  8. Review
  9. Review
  10. Homotypic and heterotypicThe Journal of biological chemistry · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
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  18. Article
  19. Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016
    Review
  20. Membrane Tethering Complexes in the Endosomal System.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

2 authors at 1 institution in 1 country.

Ruoya HoDepartment of Molecular Physiology and Biological Physics and Center for Membrane Biology, University of Virginia School of Medicine, Charlottesville, VA 22908.
Christopher StroupeDepartment of Molecular Physiology and Biological Physics and Center for Membrane Biology, University of Virginia School of Medicine, Charlottesville, VA 22908 chris.stroupe@virginia.edu.
University of Virginia · US

Funding

Molecular Electron Microscopy Core Facility ImprovementsG20RR031199 · NCRR · UNIVERSITY OF VIRGINIA · PI SHUPNIK, MARGARET A · 2010 to 2010
$2.0M
NCRR NIH HHS G20 RR031199NCRR NIH HHS G20-RR31199
6 · The paper itself

Abstract

Many Rab GTPase effectors are membrane-tethering factors, that is, they physically link two apposed membranes before intracellular membrane fusion. In this study, we investigate the distinct binding factors needed on apposed membranes for Rab effector-dependent tethering. We show that the homotypic fusion and protein-sorting/class C vacuole protein-sorting (HOPS/class C Vps) complex can tether low-curvature membranes, that is, liposomes with a diameter of ∼100 nm, only when the yeast vacuolar Rab GTPase Ypt7p is present in both tethered membranes. When HOPS is phosphorylated by the vacuolar casein kinase I, Yck3p, tethering only takes place when GTP-bound Ypt7p is present in both tethered membranes. When HOPS is not phosphorylated, however, its tethering activity shows little specificity for the nucleotide-binding state of Ypt7p. These results suggest a model for HOPS-mediated tethering in which HOPS tethers membranes by binding to Ypt7p in each of the two tethered membranes. Moreover, because vacuole-associated HOPS is presumably phosphorylated by Yck3p, our results suggest that nucleotide exchange of Ypt7p on multivesicular bodies (MVBs)/late endosomes must take place before HOPS can mediate tethering at vacuoles.

Indexed as

Adaptor Proteins, Vesicular TransportCasein Kinase IClass III Phosphatidylinositol 3-KinasesFungal ProteinsIntracellular MembranesMembrane FusionMultivesicular BodiesPhosphorylationProtein Bindingrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesVesicular Transport ProteinsAdaptor Proteins, Vesicular TransportCasein Kinase IClass III Phosphatidylinositol 3-KinasesFungal Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsVAM6 protein, S cerevisiaeVesicular Transport ProteinsVPS33 protein, S cerevisiaeVPS41 protein, S cerevisiaeYCK3 protein, S cerevisiaeYPT7 protein, S cerevisiae

Identifiers

PMID25995379
PMCPMC4501362
OpenAlexW2118151565

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.