Home > Publications Database > Parkin-dependent mitophagy occurs via proteasome-dependent steps sequentially targeting separate mitochondrial sub-compartments for autophagy > print

001     266473
005     20240318103438.0
024 7 _ |a 10.1080/27694127.2022.2143214
|2 doi
037 _ _ |a DZNE-2023-01158
082 _ _ |a 610
100 1 _ |a Lechado-Terradas, Anna
|0 P:(DE-HGF)0
|b 0
245 _ _ |a Parkin-dependent mitophagy occurs via proteasome-dependent steps sequentially targeting separate mitochondrial sub-compartments for autophagy
260 _ _ |a London
|c 2022
|b Taylor & Francis Group
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1704969833_10751
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a 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.
536 _ _ |a 352 - Disease Mechanisms (POF4-352)
|0 G:(DE-HGF)POF4-352
|c POF4-352
|f POF IV
|x 0
588 _ _ |a Dataset connected to CrossRef, Journals: pub.dzne.de
700 1 _ |a Schepers, Sandra
|b 1
700 1 _ |a Zittlau, Katharina I.
|b 2
700 1 _ |a Sharma, Karan
|0 P:(DE-HGF)0
|b 3
700 1 _ |a Ok, Orkun
|b 4
700 1 _ |a Fitzgerald, Julia C.
|0 P:(DE-HGF)0
|b 5
700 1 _ |a Geimer, Stefan
|b 6
700 1 _ |a Westermann, Benedikt
|b 7
700 1 _ |a Macek, Boris
|b 8
700 1 _ |a Kahle, Philipp
|0 P:(DE-2719)2810803
|b 9
|e Last author
|u dzne
773 _ _ |a 10.1080/27694127.2022.2143214
|g Vol. 1, no. 1, p. 576 - 602
|0 PERI:(DE-600)3122278-X
|n 1
|p 576 - 602
|t Autophagy reports
|v 1
|y 2022
|x 2769-4127
856 4 _ |u https://pub.dzne.de/record/266473/files/DZNE-2023-01158.pdf
|y OpenAccess
856 4 _ |u https://pub.dzne.de/record/266473/files/DZNE-2023-01158.pdf?subformat=pdfa
|x pdfa
|y OpenAccess
909 C O |o oai:pub.dzne.de:266473
|p openaire
|p open_access
|p VDB
|p driver
|p dnbdelivery
910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
|0 I:(DE-588)1065079516
|k DZNE
|b 9
|6 P:(DE-2719)2810803
913 1 _ |a DE-HGF
|b Gesundheit
|l Neurodegenerative Diseases
|1 G:(DE-HGF)POF4-350
|0 G:(DE-HGF)POF4-352
|3 G:(DE-HGF)POF4
|2 G:(DE-HGF)POF4-300
|4 G:(DE-HGF)POF
|v Disease Mechanisms
|x 0
914 1 _ |y 2022
915 _ _ |a OpenAccess
|0 StatID:(DE-HGF)0510
|2 StatID
915 _ _ |a Creative Commons Attribution CC BY 4.0
|0 LIC:(DE-HGF)CCBY4
|2 HGFVOC
920 1 _ |0 I:(DE-2719)1210000-4
|k AG Kahle
|l Functional Neurogenetics
|x 0
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a I:(DE-2719)1210000-4
980 _ _ |a UNRESTRICTED
980 1 _ |a FullTexts

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21