Evidence map›Paper›PMID 37190052›Full record

ArticleCells2023

USP8 Down-Regulation Promotes Parkin-Independent Mitophagy in the

Sofia Mauri, Greta Bernardo, Aitor Martinez, Mariavittoria Favaro, Marta Trevisan, Gael Cobraiville, Marianne Fillet, Federico Caicci, Alexander J Whitworth, Elena Ziviani

Open access · goldAbstract read
In one paragraph

Article in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Molecular biology of the cell · 2026
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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 at 3 institutions in 3 countries.

Sofia MauriDepartment of Biology, University of Padova, 35121 Padova, Italy.ORCID 0000-0003-3931-1490
Greta BernardoDepartment of Biology, University of Padova, 35121 Padova, Italy.
Aitor MartinezMRC Mitochondrial Biology Unit, Cambridge Biomedical Campus, University of Cambridge, Cambridge CB2 0XY, UK.ORCID 0000-0003-1648-9448
Mariavittoria FavaroDepartment of Biology, University of Padova, 35121 Padova, Italy.
Marta TrevisanDepartment of Molecular Medicine (DMM), University of Padova, 35121 Padova, Italy.ORCID 0000-0002-3148-7240
Gael CobraivilleLaboratory for the Analysis of Medicines, Center for Interdisciplinary Research on Medicines (CIRM), Quartier Hopital, University of Liege, Avenue Hippocrate 15, 4000 Liege, Belgium.
Marianne FilletLaboratory for the Analysis of Medicines, Center for Interdisciplinary Research on Medicines (CIRM), Quartier Hopital, University of Liege, Avenue Hippocrate 15, 4000 Liege, Belgium.ORCID 0000-0002-1453-6282
Federico CaicciDepartment of Biology, University of Padova, 35121 Padova, Italy.ORCID 0000-0001-6981-449X
Alexander J WhitworthMRC Mitochondrial Biology Unit, Cambridge Biomedical Campus, University of Cambridge, Cambridge CB2 0XY, UK.ORCID 0000-0002-1154-6629
Elena ZivianiDepartment of Biology, University of Padova, 35121 Padova, Italy.ORCID 0000-0002-0864-8309
University of Padua · ITUniversity of Cambridge · GBUniversity of Liège · BE

Funding

Medical Research Council MC_UU_00028/6
6 · The paper itself

Abstract

Stress-induced mitophagy, a tightly regulated process that targets dysfunctional mitochondria for autophagy-dependent degradation, mainly relies on two proteins, PINK1 and Parkin, which genes are mutated in some forms of familiar Parkinson's Disease (PD). Upon mitochondrial damage, the protein kinase PINK1 accumulates on the organelle surface where it controls the recruitment of the E3-ubiquitin ligase Parkin. On mitochondria, Parkin ubiquitinates a subset of mitochondrial-resident proteins located on the outer mitochondrial membrane, leading to the recruitment of downstream cytosolic autophagic adaptors and subsequent autophagosome formation. Importantly, PINK1/Parkin-independent mitophagy pathways also exist that can be counteracted by specific deubiquitinating enzymes (DUBs). Down-regulation of these specific DUBs can presumably enhance basal mitophagy and be beneficial in models in which the accumulation of defective mitochondria is implicated. Among these DUBs, USP8 is an interesting target because of its role in the endosomal pathway and autophagy and its beneficial effects, when inhibited, in models of neurodegeneration. Based on this, we evaluated autophagy and mitophagy levels when USP8 activity is altered. We used genetic approaches in

Indexed as

Drosophila ProteinsMitophagyAnimalsBrainDown-RegulationDrosophilaDrosophila melanogasterEndopeptidasesEndosomal Sorting Complexes Required for TransportHumansNeuronsProtein KinasesProtein Serine-Threonine KinasesPTEN-Induced Putative KinaseUbiquitin-Protein LigasesUbiquitin ThiolesteraseDrosophila ProteinsEndopeptidasesEndosomal Sorting Complexes Required for TransportPINK1 protein, DrosophilaProtein KinasesProtein Serine-Threonine KinasesPTEN-Induced Putative KinaseUbiquitin-Protein LigasesUbiquitin ThiolesteraseUSP8 protein, humanautophagyDUBsmitophagyParkinUSP8

Identifiers

PMID37190052
PMCPMC10136645
OpenAlexW4365448823

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.