Evidence map›Paper›PMID 20154681›Full record

ArticleNature cell biology2010

The peroxisomal importomer constitutes a large and highly dynamic pore.

Michael Meinecke, Christian Cizmowski, Wolfgang Schliebs, Vivien Krüger, Sabrina Beck, Richard Wagner, Ralf Erdmann

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
11.6field-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

137 citing papers in PubMed, 290 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Aging impairs peroxisome biogenesis in human B cells.The journals of gerontology. Series A, Biological sciences and medical sciences · 2026
    Article
  5. Article
  6. Article
  7. A peroxisomal membrane protein hub.Nature chemical biology · 2025
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Mammalian pexophagy at a glance.Journal of cell science · 2024
    Review
  14. Review
  15. Article
  16. The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024
    Review
  17. Article
  18. Article
  19. mBio · 2023
    Article
  20. Article

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

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

7 authors at 3 institutions in 2 countries.

Michael MeineckeBiophysik, FB Biologie/Chemie, Universität Osnabrück, Germany.
Christian Cizmowski
Wolfgang Schliebs
Vivien Krüger
Sabrina Beck
Richard Wagner
Ralf Erdmann
Ruhr University Bochum · DEOsnabrück University · DEMRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The peroxisomal protein import machinery differs fundamentally from known translocons (endoplasmic reticulum, mitochondria, chloroplasts, bacteria) as it allows membrane passage of folded, even oligomerized proteins. However, the mechanistic principles of protein translocation across the peroxisomal membrane remain unknown. There are various models that consider membrane invagination events, vesicle fusion or the existence of large import pores. Current data show that a proteinaceous peroxisomal importomer enables docking of the cytosolic cargo-loaded receptors, cargo translocation and receptor recycling. Remarkably, the cycling import receptor Pex5p changes its topology from a soluble cytosolic form to an integral membrane-bound form. According to the transient pore hypothesis, the membrane-bound receptor is proposed to form the core component of the peroxisomal import pore. Here, we demonstrate that the membrane-associated import receptor Pex5p together with its docking partner Pex14p forms a gated ion-conducting channel which can be opened to a diameter of about 9 nm by the cytosolic receptor-cargo complex. The newly identified pore shows striking dynamics, as expected for an import machinery translocating proteins of variable sizes.

Indexed as

Acyl-CoA OxidaseCarrier ProteinsElectrophysiological PhenomenaGene DeletionIon Channel GatingIon ChannelsMembrane PotentialsMembrane ProteinsMembranes, ArtificialMembrane Transport ProteinsModels, BiologicalMultiprotein ComplexesPeroxinsPeroxisomesPeroxisome-Targeting Signal 1 ReceptorPorinsAcyl-CoA OxidaseCarrier ProteinsIon ChannelsMembrane ProteinsMembranes, ArtificialMembrane Transport ProteinsMultiprotein ComplexesPeroxinsPeroxisome-Targeting Signal 1 ReceptorPEX10 protein, S cerevisiaePEX12 protein, S cerevisiaePEX13 protein, S cerevisiaePEX14 protein, S cerevisiaePEX17 protein, S cerevisiaePEX18 protein, S cerevisiaePEX21 protein, S cerevisiaePEX5 protein, S cerevisiaePex8 protein, S cerevisiaePorinsPOX1 protein, S cerevisiaeReceptors, Cytoplasmic and NuclearRepressor ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesUnilamellar Liposomes

Identifiers

PMID20154681
OpenAlexW2007209781

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.