Evidence map›Paper›PMID 39106189›Full record

ArticleeLife2024

The ORP9-ORP11 dimer promotes sphingomyelin synthesis.

Birol Cabukusta, Shalom Borst Pauwels, Jimmy J L L Akkermans, Niek Blomberg, Aat A Mulder, Roman I Koning, Martin Giera, Jacques Neefjes

Abstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. 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
  8. Article
  9. Review
  10. Article
  11. 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

8 authors.

Birol CabukustaCell and Chemical Biology, Oncode Institute, Leiden University Medical Center, Leiden, Netherlands.ORCID https://orcid.org/0000-0002-1187-3048
Shalom Borst PauwelsCell and Chemical Biology, Oncode Institute, Leiden University Medical Center, Leiden, Netherlands.ORCID https://orcid.org/0000-0001-5596-2512
Jimmy J L L AkkermansCell and Chemical Biology, Oncode Institute, Leiden University Medical Center, Leiden, Netherlands.
Niek BlombergCentre for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, Netherlands.
Aat A MulderElectron Microscopy Facility, Cell and Chemical Biology, Leiden University Medical Center, Leiden, Netherlands.ORCID https://orcid.org/0000-0002-4779-099X
Roman I KoningElectron Microscopy Facility, Cell and Chemical Biology, Leiden University Medical Center, Leiden, Netherlands.ORCID https://orcid.org/0000-0001-6736-7147
Martin GieraCentre for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, Netherlands.ORCID https://orcid.org/0000-0003-1684-1894
Jacques NeefjesCell and Chemical Biology, Oncode Institute, Leiden University Medical Center, Leiden, Netherlands.ORCID https://orcid.org/0000-0001-6763-2211

Funding

Nederlandse Organisatie voor Wetenschappelijk Onderzoek Spinoza 00897590
6 · The paper itself

Abstract

Numerous lipids are heterogeneously distributed among organelles. Most lipid trafficking between organelles is achieved by a group of lipid transfer proteins (LTPs) that carry lipids using their hydrophobic cavities. The human genome encodes many intracellular LTPs responsible for lipid trafficking and the function of many LTPs in defining cellular lipid levels and distributions is unclear. Here, we created a gene knockout library targeting 90 intracellular LTPs and performed whole-cell lipidomics analysis. This analysis confirmed known lipid disturbances and identified new ones caused by the loss of LTPs. Among these, we found major sphingolipid imbalances in ORP9 and ORP11 knockout cells, two proteins of previously unknown function in sphingolipid metabolism. ORP9 and ORP11 form a heterodimer to localize at the ER-

Indexed as

Endoplasmic ReticulumSphingomyelinsCarrier ProteinsGene Knockout TechniquesGolgi ApparatusHumansOxysterol Binding ProteinsPhosphatidylinositol PhosphatesProtein MultimerizationReceptors, SteroidCarrier ProteinsOxysterol Binding ProteinsPhosphatidylinositol PhosphatesReceptors, SteroidSphingomyelinsbiochemistrycell biologychemical biologyhumanLipidomicslipid transfer proteinsmembrane contact sitesORP11ORP9Sphingomyelin

Identifiers

PMID39106189
PMCPMC11302984

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.