Evidence map›Paper›PMID 27846375›Full record

ArticleAutophagy2017

Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy.

Naïma Belgareh-Touzé, Laetitia Cavellini, Mickael M Cohen

Abstract read
In one paragraph

Article in Autophagy, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
–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

36 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Guideline
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The Mitochondrial Distribution and Morphology Family 33 GeneJournal of fungi (Basel, Switzerland) · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Yeast mitophagy: Unanswered questions.Biochimica et biophysica acta. General subjects · 2021
    Review
  19. Review
  20. Protein Quality Control at the Mitochondrial Surface.Frontiers in cell and developmental biology · 2021
    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.

Naïma Belgareh-Touzéa UMR8226, CNRS/UPMC, Sorbonne Université, Institut de Biologie Physico-Chimique , Paris , France.
Laetitia Cavellinia UMR8226, CNRS/UPMC, Sorbonne Université, Institut de Biologie Physico-Chimique , Paris , France.
Mickael M Cohena UMR8226, CNRS/UPMC, Sorbonne Université, Institut de Biologie Physico-Chimique , Paris , France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are dynamic organelles that undergo permanent fission and fusion events. These processes play an essential role in maintaining normal cellular function. In the yeast Saccharomyces cerevisiae, the endoplasmic reticulum-mitochondrial encounter structure (ERMES) is a marker of sites of mitochondrial division, but it is also involved in a plethora of other mitochondrial functions. However, it remains unclear how these different functions are regulated. We show here that Mdm34 and Mdm12, 2 components of ERMES, are ubiquitinated by the E3 ligase Rsp5. This ubiquitination is not involved in mitochondrial dynamics or in the distribution and turnover of ERMES. Nevertheless, the ubiquitination of Mdm34 and Mdm12 was required for efficient mitophagy. We thus report here the first identification of ubiquitinated substrates participating in yeast mitophagy.

Indexed as

UbiquitinationAmino Acid MotifsAutophagyEndoplasmic ReticulumEndosomal Sorting Complexes Required for TransportHydrogen-Ion ConcentrationMembrane ProteinsMitochondriaMitochondrial DynamicsMitochondrial ProteinsMitophagyPlasmidsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesEndosomal Sorting Complexes Required for TransportMdm12 protein, S cerevisiaemdm34 protein, S cerevisiaeMembrane ProteinsMitochondrial ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesERERMESMdm12Mdm34mitochondriamitophagyRsp5S. cerevisiaeubiquitin

Identifiers

PMID27846375
PMCPMC5240830

What OpenQuestion holds

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LicenceCC BY-NC
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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.