Evidence map›Paper›PMID 29358326›Full record

ArticleThe Journal of biological chemistry2018

Oxysterol-binding protein-related protein 5 (ORP5) promotes cell proliferation by activation of mTORC1 signaling.

Ximing Du, Armella Zadoorian, Ivan E Lukmantara, Yanfei Qi, Andrew J Brown, Hongyuan Yang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. 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
  3. Mitochondria-ER crosstalk via MAMS: Bridging cellular homeostasis and cancer progression.Apoptosis : an international journal on programmed cell death · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Intracellular Cholesterol Synthesis and Transport.Frontiers in cell and developmental biology · 2022
    Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Lipid Transfer Proteins and Membrane Contact Sites in Human Cancer.Frontiers in cell and developmental biology · 2019
    Review
  20. 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

6 authors at 1 institution in 1 country.

Ximing DuFrom the School of Biotechnology and Biomolecular Sciences, the University of New South Wales, Sydney, New South Wales 2052, Australia x.r.du@unsw.edu.au.
Armella ZadoorianFrom the School of Biotechnology and Biomolecular Sciences, the University of New South Wales, Sydney, New South Wales 2052, Australia.
Ivan E LukmantaraFrom the School of Biotechnology and Biomolecular Sciences, the University of New South Wales, Sydney, New South Wales 2052, Australia.
Yanfei QiFrom the School of Biotechnology and Biomolecular Sciences, the University of New South Wales, Sydney, New South Wales 2052, Australia.
Andrew J BrownFrom the School of Biotechnology and Biomolecular Sciences, the University of New South Wales, Sydney, New South Wales 2052, Australia.
Hongyuan YangFrom the School of Biotechnology and Biomolecular Sciences, the University of New South Wales, Sydney, New South Wales 2052, Australia h.rob.yang@unsw.edu.au.
UNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) constitute a large family of proteins that mainly function in lipid transport and sensing. ORP5 is an endoplasmic reticulum (ER)-anchored protein implicated in lipid transfer at the contact sites between the ER and other membranes. Recent studies indicate that ORP5 is also involved in cancer cell invasion and tumor progression. However, the molecular mechanism underlying ORP5's involvement in cancer is unclear. Here, we report that ORP5 promotes cell proliferation and motility of HeLa cells, an effect that depends on its functional OSBP-related domain (ORD). We also found that ORP5 depletion or substitutions of key residues located within ORP5-ORD and responsible for interactions with lipids interfered with cell proliferation, migration, and invasion. ORP5 interacted with the protein mechanistic target of rapamycin (mTOR), and this interaction also required ORP5-ORD. Of note, whereas ORP5 overexpression induced mTOR complex 1 (mTORC1) activity, ORP5 down-regulation had the opposite effect. Finally, ORP5-depleted cells exhibited impaired mTOR localization to lysosomes, which may have accounted for the blunted mTORC1 activation. Together, our results suggest that ORP5 expression is positively correlated with mTORC1 signaling and that ORP5 stimulates cell proliferation, at least in part, by activating mTORC1.

Indexed as

Signal TransductionUp-RegulationAmino Acid SubstitutionCell Line, TumorCell MovementCell ProliferationEnzyme ActivationGene DeletionGreen Fluorescent ProteinsHumansLysosomesMechanistic Target of Rapamycin Complex 1Neoplasm InvasivenessNeoplasm ProteinsNeoplasmsOxysterol Binding ProteinsGreen Fluorescent ProteinsMechanistic Target of Rapamycin Complex 1MTOR protein, humanNeoplasm ProteinsOxysterol Binding ProteinsReceptors, SteroidRecombinant Fusion ProteinsTOR Serine-Threonine Kinasescancercell proliferationcell signalinglipidsmammalian target of rapamycin (mTOR)mTOR complex (mTORC)ORP5ORP8OSBPphosphoinositide

Identifiers

PMID29358326
PMCPMC5846161
OpenAlexW2785253223

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.