PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Open accessAbstract
Loss-of-function mutations in PINK1 and Parkin cause parkinsonism in humans and mitochondrial dysfunction in model organisms. Parkin is selectively recruited from the cytosol to damaged mitochondria to trigger their autophagy. How Parkin recognizes damaged mitochondria, however, is unknown. Here, we show that expression of PINK1 on individual mitochondria is regulated by voltage-dependent proteolysis to maintain low levels of PINK1 on healthy, polarized mitochondria, while facilitating the rapid accumulation of PINK1 on mitochondria that sustain damage. PINK1 accumulation on mitochondria is both necessary and sufficient for Parkin recruitment to mitochondria, and disease-causing mutations in PINK1 and Parkin disrupt Parkin recruitment and Parkin-induced mitophagy at distinct steps. These findings provide a biochemical explanation for the genetic epistasis between PINK1 and Parkin in Drosophila melanogaster. In addition, they support a novel model for the negative selection of damaged mitochondria, in which PINK1 signals mitochondrial dysfunction to Parkin, and Parkin promotes their elimination.
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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 [4]
The Introduction (page unavailable) reports that PINK1 is required for Parkin recruitment to depolarized mitochondria and subsequent mitophagy. It describes the pathway’s role in preventing parkinsonism as consistent with a model, while the Discussion (page unavailable) says the pathway may promote damaged-mitochondrion turnover. Calling it neuroprotective and saying it “ensures” elimination states that proposed protective effect more definitively than the paper does. (LLM, conf=0.84)
Experimental — accuracy not yet measuredUpon mitochondrial damage, PINK1 is quickly stabilized on damaged mitochondria, leading to translocation of cytosolic Parkin to damaged mitochondria.
“Upon mitochondrial damage, PINK1 is quickly stabilized on damaged mitochondria, which leads to translocation of cytosolic Parkin to damaged mitochondria [11–13].”
From miR-27a and miR-27b regulate autophagic clearance of damaged mitochondria by targeting PTEN-induced putative kinase 1 (PINK1) (2016) · cites this paper as [12]
Biallelic loss-of-function mutations in GRN cause juvenile-onset neuronal ceroid lipofuscinosis (NCL).
“Subsequently, rare families with biallelic loss of function mutations in GRN were identified, and affected individuals were found to have a juvenile-onset neuronal ceroid lipofuscinosis (NCL).114–116”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [115]
The Discussion addresses recessive PINK1 and Parkin mutations in early-onset Parkinson disease, not GRN mutations or neuronal ceroid lipofuscinosis. Searches for GRN, biallelic loss of function, and juvenile-onset neuronal ceroid lipofuscinosis found no passage addressing the claim in our copy. (LLM, conf=0.78)
Experimental — accuracy not yet measuredThe most extensively studied mitophagy pathway involves the E3 ligase Parkin and PINK1.
“The most extensively studied mitophagy pathway involves the E3 ligase Parkin and PINK1 (Phosphatase and tensin homolog (PTEN)-induced kinase 1) [121,122,123,124,125].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [122]
PINK1-Parkin signaling maintains mitochondrial health.
“Early-onset Parkinson's disease-associated PINK1-Parkin signaling maintains mitochondrial health.”
From A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling (2020) · cites this paper as Narendra et al., 2010
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Self-citation
- Authors
- Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- Youle, Richard J.
- Venue
- PLoS Biology
- Publisher
- Public Library of Science (PLoS)
- Published
- 2010-01-26
- Volume
- 8
- Issue
- 1
- Pages
- e1000298
- ISSN
- 1544-9173 (ISSN-L)
- 1545-7885
- PMC
- PMC2811155
- OpenAlex
- W2108326484
- Cited by
- 2,944
- References
- 58
- Citations by year
- 2026: 189 · 2025: 174 · 2024: 195 · 2023: 151 · 2022: 195 · 2021: 225 · 2020: 199 · 2019: 172 · 2018: 206 · 2017: 170 · 2016: 175 · 2015: 168 · 2014: 166 · 2013: 168 · 2012: 159
- FWCI
- 104.93
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS Biology (publishedVersion, public-domain)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- National Institutes of Health
- Japan Society for the Promotion of Science
- National Institute of Neurological Disorders and Stroke (R01NS041779)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Keywords
- PINK1, Parkin, mitophagy, mitochondrial dysfunction, protein stabilization, genetic epistasis, Parkinson's disease, Drosophila melanogaster, mitochondrial quality control
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, HeLa Cells, Humans, Mitochondria, Models, Biological, Parkinson Disease, Protein Kinases, Ubiquitin-Protein Ligases, Metalloproteases, Mitochondrial Membranes, Mice, Rats, Membrane Potential, Mitochondrial
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