Evidence map›Paper›PMID 15738267›Full record

ArticleThe Journal of cell biology2005

Dynamic ergosterol- and ceramide-rich domains in the peroxisomal membrane serve as an organizing platform for peroxisome fusion.

Tatiana Boukh-Viner, Tong Guo, Alex Alexandrian, André Cerracchio, Christopher Gregg, Sandra Haile, Robert Kyskan, Svetlana Milijevic, Daniel Oren, Jonathan Solomon and 5 more

Abstract read
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Determinants of Peroxisome Membrane Dynamics.Frontiers in physiology · 2022
    Review
  5. Molecular Basis of Mitochondrial and Peroxisomal Division Machineries.International journal of molecular sciences · 2020
    Review
  6. Ceramide regulates interaction of Hsd17b4 with Pex5 and function of peroxisomes.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. 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

15 authors.

Tatiana Boukh-VinerDepartment of Biology, Concordia University, Montreal, Quebec H4B 1R6, Canada.
Tong Guo
Alex Alexandrian
André Cerracchio
Christopher Gregg
Sandra Haile
Robert Kyskan
Svetlana Milijevic
Daniel Oren
Jonathan Solomon
Vivianne Wong
Jean-Marc Nicaud
Richard A Rachubinski
Ann M English
Vladimir I Titorenko

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We describe unusual ergosterol- and ceramide-rich (ECR) domains in the membrane of yeast peroxisomes. Several key features of these detergent-resistant domains, including the nature of their sphingolipid constituent and its unusual distribution across the membrane bilayer, clearly distinguish them from well characterized detergent-insoluble lipid rafts in the plasma membrane. A distinct set of peroxisomal proteins, including two ATPases, Pex1p and Pex6p, as well as phosphoinositide- and GTP-binding proteins, transiently associates with the cytosolic face of ECR domains. All of these proteins are essential for the fusion of the immature peroxisomal vesicles P1 and P2, the earliest intermediates in a multistep pathway leading to the formation of mature, metabolically active peroxisomes. Peroxisome fusion depends on the lateral movement of Pex1p, Pex6p, and phosphatidylinositol-4,5-bisphosphate-binding proteins from ECR domains to a detergent-soluble portion of the membrane, followed by their release to the cytosol. Our data suggest a model for the multistep reorganization of the multicomponent peroxisome fusion machinery that transiently associates with ECR domains.

Indexed as

Adenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCeramidesDetergentsErgosterolFungal ProteinsGTP-Binding ProteinsMembrane FusionPeroxisomesSphingolipidsYarrowiaAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCeramidesDetergentsErgosterolFungal ProteinsGTP-Binding ProteinsPEX6 protein, Yarrowia lipolyticaSphingolipids

Identifiers

PMID15738267
PMCPMC2171827

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.