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PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
Open accessAbstract
Parkinson's disease (PD) is a prevalent neurodegenerative disorder. Recent identification of genes linked to familial forms of PD such as Parkin and PINK1 (PTEN-induced putative kinase 1) has revealed that ubiquitylation and mitochondrial integrity are key factors in disease pathogenesis. However, the exact mechanism underlying the functional interplay between Parkin-catalyzed ubiquitylation and PINK1-regulated mitochondrial quality control remains an enigma. In this study, we show that PINK1 is rapidly and constitutively degraded under steady-state conditions in a mitochondrial membrane potential-dependent manner and that a loss in mitochondrial membrane potential stabilizes PINK1 mitochondrial accumulation. Furthermore, PINK1 recruits Parkin from the cytoplasm to mitochondria with low membrane potential to initiate the autophagic degradation of damaged mitochondria. Interestingly, the ubiquitin ligase activity of Parkin is repressed in the cytoplasm under steady-state conditions; however, PINK1-dependent mitochondrial localization liberates the latent enzymatic activity of Parkin. Some pathogenic mutations of PINK1 and Parkin interfere with the aforementioned events, suggesting an etiological importance. These results provide crucial insight into the pathogenic mechanisms of PD.
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“where it ubiquitinates a number of mitochondrial proteins (Chan et al, 2011;Sarraf et al, 2013), in addition to ubiquitinating itself (Matsuda et al, 2010;Lazarou et al, 2013).”
From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as Matsuda et al, 2010
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“Parkin-mediated ubiquitination is critical for the efficient elimination of depolarized dysfunctional mitochondria by autophagy (mitophagy).”
From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as Matsuda et al, 2010
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“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 [13]
In the citing paper
“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 [125]
In the citing paper
“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 Matsuda et al., 2010
In the citing paper
“Concurrently with the changes in parkin levels, the electrophoretic mobility of parkin was transiently shifted upward, consistent with a CCCP-induced activation of parkin and parkin auto-ubiquitination, as reported previously (Matsuda et al, 2010;Lazarou et al, 2013).”
From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as Matsuda et al, 2010
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“In 2000, we and others found that dysfunction of an E3 ubiquitin ligase (Imai et al., 2000; Shimura et al., 2000; Zhang et al., 2000) termed Parkin causes autosomal recessive juvenile Parkinsonism (Kitada et al., 1998).”
BackgroundSelf-citationDrosophila pink1 is required for mitochondrial function and interacts genetically with parkin
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Metadata
- Authors
- Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., Kimura, M., Komatsu, M., Hattori, N., & Tanaka, K.
- Affiliations
- Tokyo Metropolitan Institute of Medical Science (JP)
- Juntendo University (JP)
- Center for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115 4
- Japan Science and Technology Agency (JP)
- Corresponding author
- Matsuda, Noriyuki
- Tanaka, Keiji
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2010-04-19
- Volume
- 189
- Issue
- 2
- Pages
- 211-221
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2856912
- OpenAlex
- W2138311396
- Cited by
- 1,969
- References
- 32
- Citations by year
- 2026: 98 · 2025: 115 · 2024: 118 · 2023: 121 · 2022: 144 · 2021: 152 · 2020: 175 · 2019: 131 · 2018: 123 · 2017: 100 · 2016: 110 · 2015: 118 · 2014: 119 · 2013: 116 · 2012: 101
- FWCI
- 65.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- PINK1, Parkin, Parkinson's disease, mitophagy, mitochondrial membrane potential, mitochondrial depolarization, ubiquitination, ubiquitin ligase activity, mitochondrial quality control, PINK1 mutations, parkin mutations, protein stabilization
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Dimethyl Sulfoxide, Fibroblasts, Fluorescent Dyes, HeLa Cells, Humans, Mitochondria, Parkinson Disease, Protein Kinases, Recombinant Fusion Proteins, Solvents, Uncoupling Agents, Biomarkers, Receptors, Cytoplasmic and Nuclear, Mice, Knockout, Mitochondrial Proteins, Ubiquitin-Protein Ligases, Mice, Membrane Potential, Mitochondrial
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