PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, Sven; Holmström, Kira M.; Skujat, Diana; Fiesel, Fabienne C.; Rothfuss, Oliver C.; Kahle, Philipp J.; Springer, Wolfdieter

doi:10.1038/ncb2012

Cited by 2,835Parkinson's Disease Mechanisms and TreatmentsAutophagy in Disease and TherapyUbiquitin and proteasome pathways

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, Sven, Holmström, Kira M., Skujat, Diana, Fiesel, Fabienne C., Rothfuss, Oliver C., Kahle, Philipp J., Springer, Wolfdieter·2010·Nature Cell Biology

DOI 10.1038/ncb2012

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Abstract

Parkinson's disease is the most common neurodegenerative movement disorder. Mutations in PINK1 and PARKIN are the most frequent causes of recessive Parkinson's disease. However, their molecular contribution to pathogenesis remains unclear. Here, we reveal important mechanistic steps of a PINK1/Parkin-directed pathway linking mitochondrial damage, ubiquitylation and autophagy in non-neuronal and neuronal cells. PINK1 kinase activity and its mitochondrial localization sequence are prerequisites to induce translocation of the E3 ligase Parkin to depolarized mitochondria. Subsequently, Parkin mediates the formation of two distinct poly-ubiquitin chains, linked through Lys 63 and Lys 27. In addition, the autophagic adaptor p62/SQSTM1 is recruited to mitochondrial clusters and is essential for the clearance of mitochondria. Strikingly, we identified VDAC1 (voltage-dependent anion channel 1) as a target for Parkin-mediated Lys 27 poly-ubiquitylation and mitophagy. Moreover, pathogenic Parkin mutations interfere with distinct steps of mitochondrial translocation, ubiquitylation and/or final clearance through mitophagy. Thus, our data provide functional links between PINK1, Parkin and the selective autophagy of mitochondria, which is implicated in the pathogenesis of Parkinson's disease.

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PINK1 and PRKN direct a neuroprotective pathway that ensures elimination of damaged mitochondria via autophagy.
“Together, the encoded enzymes direct a neuroprotective pathway that ensures the elimination of damaged mitochondria via autophagy.”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [3]
Chaperone-mediated autophagy diminishes with age.
“Additionally, chaperone-mediated autophagy (CMA), described in detail below, diminishes with age.61”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [61]
Genetic risk alleles may combine with aging to lead to late-onset neurodegeneration.
“First, CMA is diminished with age, thus genetic risk alleles may combine with aging to lead to late-onset neurodegeneration.61”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [61]
CMA is diminished with age.
“First, CMA is diminished with age, thus genetic risk alleles may combine with aging to lead to late-onset neurodegeneration.61”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [61]
Mitophagy can also occur through Parkin-independent pathways.
“Mitophagy can also occur through Parkin-independent pathways.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [130]

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Authors: Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W.
Affiliations: University of Tübingen (DE)
Hertie Institute for Clinical Brain Research (DE)
Corresponding author: Kahle, Philipp J.
Springer, Wolfdieter
ORCID: Geisler, Sven
Holmström, Kira M.
Fiesel, Fabienne C.
Kahle, Philipp J.
Springer, Wolfdieter
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2010-01-24
Volume: 12
Issue: 2
Pages: 119-131
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb2012
OpenAlex: W2034087770
Cited by: 2,835
References: 40
Citations by year: 2026: 114 · 2025: 176 · 2024: 179 · 2023: 147 · 2022: 173 · 2021: 207 · 2020: 196 · 2019: 159 · 2018: 163 · 2017: 166 · 2016: 177 · 2015: 181 · 2014: 179 · 2013: 169 · 2012: 171
FWCI: 117.77
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: mitophagy, PINK1, Parkin, VDAC1, p62, Parkinson's disease, mitochondrial depolarization, ubiquitination, E3 ubiquitin ligase, selective autophagy, mitochondrial translocation, parkin mutations
MeSH terms: Sequestosome-1 Protein, PTEN-Induced Putative Kinase, Autophagy, Biological Transport, Fluorescent Antibody Technique, HeLa Cells, Humans, Mitochondria, Mutation, Parkinson Disease, Protein Kinases, Immunoblotting, RNA Interference, Ubiquitin-Protein Ligases, Cell Line, Tumor, Immunoprecipitation, Adaptor Proteins, Signal Transducing, Voltage-Dependent Anion Channel 1

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PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

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