Evidence map›Paper›PMID 22162133›Full record

ArticleThe Journal of cell biology2011

Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers.

Maud de Saint-Jean, Vanessa Delfosse, Dominique Douguet, Gaëtan Chicanne, Bernard Payrastre, William Bourguet, Bruno Antonny, Guillaume Drin

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

190 citing papers in PubMed, 390 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Subcellular Cartography of the Phosphoinositide Multiverse.Biochimica et biophysica acta. Molecular and cell biology of lipids · 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. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. The Inner Nuclear Membrane Has a Unique Lipid Signature.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  12. PI(4)P recruits CIDE proteins to promote the formation of unilocular lipid droplets during adipogenesis and hepatic steatosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Review
  15. Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  16. Nonvesicular cholesterol transport in physiology.The Journal of clinical investigation · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Article

130 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

Maud de Saint-JeanInstitut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and Centre National de la Recherche Scientifique, 06560 Valbonne, France.
Vanessa Delfosse
Dominique Douguet
Gaëtan Chicanne
Bernard Payrastre
William Bourguet
Bruno Antonny
Guillaume Drin
Institut de Pharmacologie Moléculaire et Cellulaire · FRCentre de Biologie Structurale · FRCentre Hospitalier Universitaire de Toulouse · FRCentre National de la Recherche Scientifique · FR

Funding

European Research Council 268888
6 · The paper itself

Abstract

Osh/Orp proteins transport sterols between organelles and are involved in phosphoinositide metabolism. The link between these two aspects remains elusive. Using novel assays, we address the influence of membrane composition on the ability of Osh4p/Kes1p to extract, deliver, or transport dehydroergosterol (DHE). Surprisingly, phosphatidylinositol 4-phosphate (PI(4)P) specifically inhibited DHE extraction because PI(4)P was itself efficiently extracted by Osh4p. We solve the structure of the Osh4p-PI(4)P complex and reveal how Osh4p selectively substitutes PI(4)P for sterol. Last, we show that Osh4p quickly exchanges DHE for PI(4)P and, thereby, can transport these two lipids between membranes along opposite routes. These results suggest a model in which Osh4p transports sterol from the ER to late compartments pinpointed by PI(4)P and, in turn, transports PI(4)P backward. Coupled to PI(4)P metabolism, this transport cycle would create sterol gradients. Because the residues that recognize PI(4)P are conserved in Osh4p homologues, other Osh/Orp are potential sterol/phosphoinositol phosphate exchangers.

Indexed as

ErgosterolLipid BilayersLiposomesMembrane ProteinsOxysterol Binding ProteinsPhosphatidylinositol PhosphatesProtein Structure, TertiaryReceptors, SteroidSaccharomyces cerevisiae ProteinsdehydroergosterolErgosterolKES1 protein, S cerevisiaeLipid BilayersLiposomesMembrane ProteinsOxysterol Binding Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesReceptors, SteroidSaccharomyces cerevisiae Proteins

Identifiers

PMID22162133
PMCPMC3241724
OpenAlexW2064892346

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.