The PINK1-Parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo
Open accessAbstract
The accumulation of damaged mitochondria has been proposed as a key factor in aging and the pathogenesis of many common age-related diseases, including Parkinson disease (PD). Recently, in vitro studies of the PD-related proteins Parkin and PINK1 have found that these factors act in a common pathway to promote the selective autophagic degradation of damaged mitochondria (mitophagy). However, whether Parkin and PINK1 promote mitophagy under normal physiological conditions in vivo is unknown. To address this question, we used a proteomic approach in Drosophila to compare the rates of mitochondrial protein turnover in parkin mutants, PINK1 mutants, and control flies. We found that parkin null mutants showed a significant overall slowing of mitochondrial protein turnover, similar to but less severe than the slowing seen in autophagy-deficient Atg7 mutants, consistent with the model that Parkin acts upstream of Atg7 to promote mitophagy. By contrast, the turnover of many mitochondrial respiratory chain (RC) subunits showed greater impairment in parkin than Atg7 mutants, and RC turnover was also selectively impaired in PINK1 mutants. Our findings show that the PINK1–Parkin pathway promotes mitophagy in vivo and, unexpectedly, also promotes selective turnover of mitochondrial RC subunits. Failure to degrade damaged RC proteins could account for the RC deficits seen in many PD patients and may play an important role in PD pathogenesis.
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Mitophagy increases with aging, and this age-dependent increase is abolished by loss of Pink1 or parkin in Drosophila.
“studies have shown that mitophagy increases with aging, and this age-dependent increase is abolished by loss of Pink1 or parkin in Drosophila[17, 18]”
From Overexpression of pink1 or parkin in indirect flight muscles promotes mitochondrial proteostasis and extends lifespan in Drosophila melanogaster (2019) · cites this paper as [17]
Loss of pink1 or parkin in Drosophila blocks mitophagy in an age-dependent manner.
“loss of pink1 or parkin in Drosophila block mitophagy in an age-dependent manner[17, 18]”
From Overexpression of pink1 or parkin in indirect flight muscles promotes mitochondrial proteostasis and extends lifespan in Drosophila melanogaster (2019) · cites this paper as [17]
Mitophagy is activated by mitochondrial membrane depolarization, followed by stabilization of Pink1 on the mitochondrial outer membrane, which recruits Parkin from the cytosol.
“Mitophagy is activated by mitochondrial membrane depolarization, followed by stabilization of a phosphatase and tensin homolog-induced putative kinase 1 (Pink1) on mitochondrial outer membrane, which then recruits an E3 ubiquitin ligase (Parkin) from the cytosol (17–19).”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [19]
Autophagosomes containing damaged mitochondria fuse with lysosomes and are cleared from cells.
“These autophagosomes containing the damaged mitochondria fuse with lysosomes which are cleared from the cells (16–21).”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [19]
Parkin is a core mitophagy-regulating protein, which is recruited to damaged or depolarized mitochondria to induce mitochondrial clearance.
“Parkin is a core mitophagy-regulating protein, which is recruited to damaged or depolarized mitochondria to induce mitochondrial clearance (16–19).”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [19]
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- Authors
- Vincow, E. S., Merrihew, G., Thomas, R. E., Shulman, N. J., Beyer, R. P., MacCoss, M. J., & Pallanck, L. J.
- Affiliations
- University of Washington (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2013-03-18
- Volume
- 110
- Issue
- 16
- Pages
- 6400-6405
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3631677
- OpenAlex
- W2011124366
- Cited by
- 478
- References
- 45
- Citations by year
- 2026: 18 · 2025: 20 · 2024: 20 · 2023: 21 · 2022: 39 · 2021: 36 · 2020: 44 · 2019: 35 · 2018: 37 · 2017: 35 · 2016: 47 · 2015: 41 · 2014: 58 · 2013: 25
- FWCI
- 41.53
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (P30AG013280)
- National Institute of General Medical Sciences (P41GM103551, R01GM103551, P41GM103533, R01GM086394)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK069386)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- PINK1, Parkin, mitophagy, selective autophagy, mitochondrial protein turnover, Parkinson's disease, ATG7, Drosophila, damaged mitochondria, aging
- MeSH terms
- Autophagy-Related Protein 7, PTEN-Induced Putative Kinase, Animals, Brain, Drosophila, Electron Transport, Half-Life, Isotope Labeling, Parkinson Disease, Mass Spectrometry, Signal Transduction, Protein Serine-Threonine Kinases, Mitochondrial Proteins, Drosophila Proteins, Ubiquitin-Protein Ligases, Mice, Mitophagy
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Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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