Evidence map›Paper›PMID 40396016›Full record

ArticleAutophagy reports2022

Parkin-dependent mitophagy occurs via proteasome-dependent steps sequentially targeting separate mitochondrial sub-compartments for autophagy.

Anna Lechado-Terradas, Sandra Schepers, Katharina I Zittlau, Karan Sharma, Orkun Ok, Julia C Fitzgerald, Stefan Geimer, Benedikt Westermann, Boris Macek, Philipp J Kahle

Abstract read
In one paragraph

Article in Autophagy reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Mitochondria in Alzheimer's Disease Pathogenesis.Life (Basel, Switzerland) · 2024
    Review
  10. 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

10 authors.

Anna Lechado-TerradasLaboratory of Functional Neurogenetics, Department of Neurodegeneration, Hertie Institute for Clinical Brain Research, Faculty of Medicine, University of Tübingen, Tübingen, Germany.
Sandra SchepersLaboratory of Functional Neurogenetics, Department of Neurodegeneration, Hertie Institute for Clinical Brain Research, Faculty of Medicine, University of Tübingen, Tübingen, Germany.
Katharina I ZittlauQuantitative Proteomics Group, Department of Biology, Interfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Karan SharmaDepartment of Biochemistry, Faculty of Science, University of Tübingen, Tübingen, Germany.
Orkun OkLaboratory of Functional Neurogenetics, Department of Neurodegeneration, Hertie Institute for Clinical Brain Research, Faculty of Medicine, University of Tübingen, Tübingen, Germany.
Julia C FitzgeraldMitochondrial Biology of Parkinson's Disease, Department of Neurodegeneration, Hertie Institute for Clinical Brain Research, Faculty of Medicine, University of Tübingen, Tübingen, Germany.
Stefan GeimerLaboratory of Cell Biology and Electron Microscopy, University of Bayreuth, Bayreuth, Germany.
Benedikt WestermannLaboratory of Cell Biology and Electron Microscopy, University of Bayreuth, Bayreuth, Germany.
Boris MacekQuantitative Proteomics Group, Department of Biology, Interfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Philipp J KahleLaboratory of Functional Neurogenetics, Department of Neurodegeneration, Hertie Institute for Clinical Brain Research, Faculty of Medicine, University of Tübingen, Tübingen, Germany.ORCID https://orcid.org/0000-0002-8587-1731

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PINK1/parkin-dependent mitophagy initially involves (phospho)ubiquitin-directed proteasome-dependent degradation of certain outer mitochondrial membrane (OMM) proteins (e.g. mitofusins) and the recruitment of autophagy adaptors to a group of ubiquitinated OMM proteins, eventually leading to autophagic removal of damaged mitochondria in stressed cells. Here we provide evidence that mitochondrial degradation occurs via stepwise delivery of separate mitochondrial sub-compartments for autophagic degradation. OMM and inner mitochondrial material appears to become separately isolated for autophagolysosomal degradation, not only in parkin-overexpressing HeLa cells but also in cells that express endogenous parkin (human embryonic kidney cells and neural progenitor cells) with slower mitophagy kinetics. The remaining inner mitochondrial material becomes degraded only after much prolonged membrane depolarization, potentially involving another proteasome-sensitive step. The present combined microscopy and proteomics analyses support the idea that cell stress-induced parkin-dependent mitophagy is a complex multi-step process with distinct mitochondrial sub-compartments being separately targeted for autophagic degradation.

Indexed as

mitochondrial outer membranemitophagyparkinproteasomeubiquitin

Identifiers

PMID40396016
PMCPMC11864704

What OpenQuestion holds

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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.