Evidence map›Paper›PMID 25420878›Full record

ArticleCellular and molecular life sciences : CMLS2015

Ligand-dependent localization and function of ORP-VAP complexes at membrane contact sites.

Marion Weber-Boyvat, Henriikka Kentala, Johan Peränen, Vesa M Olkkonen

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

36 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Organelle contact sites in cancer cells.Cell death & disease · 2026
    Review
  5. Role of Oxysterol-Binding Protein Family in Cholesterol Metabolism and Cancer Progression: A Review.Medical science monitor : international medical journal of experimental and clinical research · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. ER-PM Contact Sites - SNARING Actors in Emerging Functions.Frontiers in cell and developmental biology · 2021
    Review
  19. Review
  20. Maintaining social contacts: The physiological relevance of organelle interactions.Biochimica et biophysica acta. Molecular cell research · 2020
    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

4 authors at 2 institutions in 1 country.

Marion Weber-BoyvatMinerva Foundation Institute for Medical Research, Biomedicum 2U, Tukholmankatu 8, 00290, Helsinki, Finland.
Henriikka Kentala
Johan Peränen
Vesa M Olkkonen
Minerva Foundation · FIUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxysterol-binding protein/OSBP-related proteins (ORPs) constitute a conserved family of sterol/phospholipid-binding proteins with lipid transporter or sensor functions. We investigated the spatial occurrence and regulation of the interactions of human OSBP/ORPs or the S. cerevisiae orthologs, the Osh (OSBP homolog) proteins, with their endoplasmic reticulum (ER) anchors, the VAMP-associated proteins (VAPs), by employing bimolecular fluorescence complementation and pull-down set-ups. The ORP-VAP interactions localize frequently at distinct subcellular sites, shown in several cases to represent membrane contact sites (MCSs). Using established ORP ligand-binding domain mutants and pull-down assays with recombinant proteins, we show that ORP liganding regulates the ORP-VAP association, alters the subcellular targeting of ORP-VAP complexes, or modifies organelle morphology. There is distinct protein specificity in the effects of the mutants on subcellular targeting of ORP-VAP complexes. We provide evidence that complexes of human ORP2 and VAPs at ER-lipid droplet interfaces regulate the hydrolysis of triglycerides and lipid droplet turnover. The data suggest evolutionarily conserved, complex ligand-dependent functions of ORP-VAP complexes at MCSs, with implications for cellular lipid homeostasis and signaling.

Indexed as

Amine Oxidase (Copper-Containing)Cell Adhesion MoleculesCell Line, TumorEndoplasmic ReticulumFluorescent Antibody TechniqueGenetic Complementation TestHumansHydrolysisLipid DropletsMicroscopy, Electron, TransmissionMicroscopy, FluorescenceMultiprotein ComplexesOxysterol Binding ProteinsReceptors, SteroidRecombinant ProteinsRNA InterferenceAmine Oxidase (Copper-Containing)AOC3 protein, humanCell Adhesion MoleculesMultiprotein ComplexesOSBPL2 protein, humanOxysterol Binding ProteinsReceptors, SteroidRecombinant ProteinsTriglycerides

Identifiers

PMID25420878
PMCPMC11114005
OpenAlexW1975240013

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.