Evidence map›Paper›PMID 36514953›Full record

ArticleThe EMBO journal2023

NDP52 acts as a redox sensor in PINK1/Parkin-mediated mitophagy.

Tetsushi Kataura, Elsje G Otten, Yoana Rabanal-Ruiz, Elias Adriaenssens, Francesca Urselli, Filippo Scialo, Lanyu Fan, Graham R Smith, William M Dawson, Xingxiang Chen and 6 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. 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
8.1field-weighted citation impact, top 2% 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, 55 citations in OpenAlex.

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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

16 authors at 5 institutions in 5 countries.

Tetsushi KatauraFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.ORCID 0000-0002-3958-5232
Elsje G OttenFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.ORCID 0000-0002-8716-3560
Yoana Rabanal-RuizFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.
Elias AdriaenssensMax Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0001-9430-917X
Francesca UrselliFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.ORCID 0000-0002-5839-7384
Filippo ScialoFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.
Lanyu FanChemistry - School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne, UK.
Graham R SmithBioinformatics Support Unit (BSU), Faculty of Medical Sciences, Newcastle University, Newcastle Upon Tyne, UK.
William M DawsonSchool of Chemistry, University of Bristol, Bristol, UK.ORCID 0000-0003-2710-6879
Xingxiang ChenCollege of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China.
Wyatt W YueFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.
Agnieszka K BronowskaChemistry - School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne, UK.
Bernadette CarrollSchool of Biochemistry, University of Bristol, Bristol, UK.ORCID 0000-0001-5673-9371
Sascha MartensMax Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0003-3786-8199
Michael LazarouDepartment of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Melbourne, VIC, Australia.ORCID 0000-0003-2150-5545
Viktor I KorolchukFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.ORCID 0000-0002-4071-592X
Newcastle University · GBUniversity of Bristol · GBUniversity of Vienna · ATNanjing Agricultural University · CNWalter and Eliza Hall Institute of Medical Research · AU

Funding

Austrian Science Fund FWF FWF SFB F79Austrian Science Fund FWF W 1261Biotechnology and Biological Sciences Research Council BB/M023389/1Biotechnology and Biological Sciences Research Council BB/R008167/2Marie Curie 101062916Wellcome TrustWellcome Trust 218547/Z/19/Z
6 · The paper itself

Abstract

Mitophagy, the elimination of mitochondria via the autophagy-lysosome pathway, is essential for the maintenance of cellular homeostasis. The best characterised mitophagy pathway is mediated by stabilisation of the protein kinase PINK1 and recruitment of the ubiquitin ligase Parkin to damaged mitochondria. Ubiquitinated mitochondrial surface proteins are recognised by autophagy receptors including NDP52 which initiate the formation of an autophagic vesicle around the mitochondria. Damaged mitochondria also generate reactive oxygen species (ROS) which have been proposed to act as a signal for mitophagy, however the mechanism of ROS sensing is unknown. Here we found that oxidation of NDP52 is essential for the efficient PINK1/Parkin-dependent mitophagy. We identified redox-sensitive cysteine residues involved in disulphide bond formation and oligomerisation of NDP52 on damaged mitochondria. Oligomerisation of NDP52 facilitates the recruitment of autophagy machinery for rapid mitochondrial degradation. We propose that redox sensing by NDP52 allows mitophagy to function as a mechanism of oxidative stress response.

Indexed as

MitophagyNuclear ProteinsProtein KinasesAutophagyHeLa CellsHumansOxidation-ReductionReactive Oxygen SpeciesUbiquitinUbiquitin-Protein LigasesCALCOCO2 protein, humanNuclear ProteinsProtein KinasesReactive Oxygen SpeciesUbiquitinUbiquitin-Protein LigasesautophagymitophagyNDP52p62redox

Identifiers

PMID36514953
PMCPMC9975939
OpenAlexW4311502524

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.