Evidence map›Paper›PMID 22733816›Full record

ArticleThe Journal of biological chemistry2012

Peroxisomal proteostasis involves a Lon family protein that functions as protease and chaperone.

Magdalena Bartoszewska, Chris Williams, Alexey Kikhney, Łukasz Opaliński, Carlo W T van Roermund, Rinse de Boer, Marten Veenhuis, Ida J van der Klei

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Peroxisomal Metabolite and Cofactor Transport in Humans.Frontiers in cell and developmental biology · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. The peroxisome: an update on mysteries 2.0.Histochemistry and cell biology · 2018
    Review
  14. Lon Peptidase 2, Peroxisomal (LONP2) Contributes to Cervical Carcinogenesis via Oxidative Stress.Medical science monitor : international medical journal of experimental and clinical research · 2018
    Article
  15. Review
  16. Review
  17. Review
  18. Pexophagy and peroxisomal protein turnover in plants.Biochimica et biophysica acta · 2016
    Review
  19. 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

8 authors at 3 institutions in 2 countries.

Magdalena BartoszewskaMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Kluyver Centre for Genomics of Industrial Fermentation, P. O. Box 11103, 9700CC Groningen, The Netherlands.
Chris Williams
Alexey Kikhney
Łukasz Opaliński
Carlo W T van Roermund
Rinse de Boer
Marten Veenhuis
Ida J van der Klei
University of Groningen · NLEuropean Molecular Biology Laboratory · DEAcademic Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are subject to continuous quality control for optimal proteostasis. The knowledge of peroxisome quality control systems is still in its infancy. Here we show that peroxisomes contain a member of the Lon family of proteases (Pln). We show that Pln is a heptameric protein and acts as an ATP-fueled protease and chaperone. Hence, Pln is the first chaperone identified in fungal peroxisomes. In cells of a PLN deletion strain peroxisomes contain protein aggregates, a major component of which is catalase-peroxidase. We show that this enzyme is sensitive to oxidative damage. The oxidatively damaged, but not the native protein, is a substrate of the Pln protease. Cells of the pln strain contain enhanced levels of catalase-peroxidase protein but reduced catalase-peroxidase enzyme activities. Together with the observation that Pln has chaperone activity in vitro, our data suggest that catalase-peroxidase aggregates accumulate in peroxisomes of pln cells due to the combined absence of Pln protease and chaperone activities.

Indexed as

ATP-Dependent EndopeptidasesCatalaseFungal ProteinsMolecular ChaperonesOxidative StressPenicillium chrysogenumPeroxisomesATP-Dependent EndopeptidasesCatalaseFungal ProteinsMolecular Chaperones

Identifiers

PMID22733816
PMCPMC3431691
OpenAlexW2035951331

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.