Evidence map›Paper›PMID 24657987›Full record

ArticleAutophagy2014

Deficiency of the exportomer components Pex1, Pex6, and Pex15 causes enhanced pexophagy in Saccharomyces cerevisiae.

James M Nuttall, Alison M Motley, Ewald H Hettema

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.9field-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

45 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Regulatory Mechanism of Peroxisome Number Reduction Caused byJournal of fungi (Basel, Switzerland) · 2023
    Article
  5. Article
  6. Targeted Modifications of the Yeast Genome to Study Peroxisomes.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. The Peroxisomal PTS1-Import Defect ofInternational journal of molecular sciences · 2020
    Article
  19. Pexophagy: A Model for Selective Autophagy.International journal of molecular sciences · 2020
    Review
  20. Structural Mapping of Missense Mutations in the Pex1/Pex6 Complex.International journal of molecular sciences · 2019
    Review
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

3 authors at 1 institution in 1 country.

James M NuttallDepartment of Molecular Biology and Biotechnology; University of Sheffield, Western Bank; Sheffield, UK.
Alison M MotleyDepartment of Molecular Biology and Biotechnology; University of Sheffield, Western Bank; Sheffield, UK.
Ewald H HettemaDepartment of Molecular Biology and Biotechnology; University of Sheffield, Western Bank; Sheffield, UK.
University of Sheffield · GB

Funding

Wellcome Trust WT084265MA
6 · The paper itself

Abstract

Turnover of damaged, dysfunctional, or excess organelles is critical to cellular homeostasis. We screened mutants disturbed in peroxisomal protein import, and found that a deficiency in the exportomer subunits Pex1, Pex6, and Pex15 results in enhanced turnover of peroxisomal membrane structures compared with other mutants. Strikingly, almost all peroxisomal membranes were associated with phagophore assembly sites in pex1Δ atg1Δ cells. Degradation depended on Atg11 and the pexophagy receptor Atg36, which mediates degradation of superfluous peroxisomes. Mutants of PEX1, PEX6, and PEX15 accumulate ubiquitinated receptors at the peroxisomal membrane. This accumulation has been suggested to trigger pexophagy in mammalian cells. We show by genetic analysis that preventing this accumulation does not abolish pexophagy in Saccharomyces cerevisiae. We find Atg36 is modified in pex1Δ cells even when Atg11 binding is prevented, suggesting Atg36 modification is an early event in the degradation of dysfunctional peroxisomal structures in pex1Δ cells via pexophagy.

Indexed as

Adenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesAutophagyAutophagy-Related ProteinsIntracellular MembranesMembrane ProteinsOrganisms, Genetically ModifiedPeroxisomesPhosphoproteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinated ProteinsAdenosine TriphosphatasesATG36 protein, S cerevisiaeATPases Associated with Diverse Cellular ActivitiesAutophagy-Related ProteinsMembrane ProteinsPEX15 protein, S cerevisiaePEX1 protein, S cerevisiaePEX6 protein, S cerevisiaePhosphoproteinsSaccharomyces cerevisiae ProteinsUbiquitinated ProteinsAtg36exportomerperoxinperoxisomePex1Pex6pexophagyselective autophagy

Identifiers

PMID24657987
PMCPMC5119063
OpenAlexW1972830435

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.