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Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission
Open accessAbstract
Mutations in PTEN-induced kinase 1 (PINK1), a mitochondrial Ser/Thr kinase, cause an autosomal recessive form of Parkinson's disease (PD), PARK6. To investigate the mechanism of PINK1 pathogenesis, we used the Drosophila Pink1 knockout (KO) model. In mitochondria isolated from Pink1-KO flies, mitochondrial respiration driven by the electron transport chain (ETC) is significantly reduced. This reduction is the result of a decrease in ETC complex I and IV enzymatic activity. As a consequence, Pink1-KO flies also display a reduced mitochondrial ATP synthesis. Because mitochondrial dynamics is important for mitochondrial function and Pink1-KO flies have defects in mitochondrial fission, we explored whether fission machinery deficits underlie the bioenergetic defect in Pink1-KO flies. We found that the bioenergetic defects in the Pink1-KO can be ameliorated by expression of Drp1, a key molecule in mitochondrial fission. Further investigation of the ETC complex integrity in wild type, Pink1-KO, PInk1-KO/Drp1 transgenic, or Drp1 transgenic flies indicates that the reduced ETC complex activity is likely derived from a defect in the ETC complex assembly, which can be partially rescued by increasing mitochondrial fission. Taken together, these results suggest a unique pathogenic mechanism of PINK1 PD: The loss of PINK1 impairs mitochondrial fission, which causes defective assembly of the ETC complexes, leading to abnormal bioenergetics.
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“Reduced mitophagy associated Pink1- and Parkin-regulated ubiquitination of the outer mitochondrial membrane of damaged mitochondria in aged neurons (79, 99, 140) contribute to a greater accumulation of ROS (81).”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [79]
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Valer, F. B., Spegiorim, G. C., dos Santos, J. R., Azzolini, A. E. C. S., de Oliveira, M. F., & Alberici, L. C. (2026) · Biochimie · doi:10.1016/j.biochi.2026.09.007
Establishing the Drosophila Larval Neuroblast as a System to Study Regulated Cell Death in vivo.
Kuang, C. (2013) · Deep Blue (University of Michigan)
Metadata
- Authors
- Liu, W., Acín-Peréz, R., Geghman, K. D., Manfredi, G., Lu, B., & Li, C.
- Affiliations
- Cornell University (US)
- Department of Neurology and Neuroscience, Weill Medical College of Cornell University, New York, NY 10065; and
- Stanford Medicine (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2011-07-18
- Volume
- 108
- Issue
- 31
- Pages
- 12920-12924
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3150934
- OpenAlex
- W2026648000
- Cited by
- 190
- References
- 47
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 7 · 2023: 11 · 2022: 14 · 2021: 14 · 2020: 27 · 2019: 9 · 2018: 11 · 2017: 10 · 2016: 13 · 2015: 13 · 2014: 13 · 2013: 21 · 2012: 20
- FWCI
- 7.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R01NS054773)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR054926)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- 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
- Keywords
- PINK1, Parkinson's disease, PARK6, mitochondrial fission, Drp1, mitochondrial dynamics, electron transport chain, complex I, cytochrome c oxidase, oxidative phosphorylation, mitochondrial bioenergetics, Drosophila model, mitochondrial respiration, ATP production
- MeSH terms
- PTEN-Induced Putative Kinase, Adenosine Triphosphate, Animals, Electron Transport Complex IV, Cytoskeletal Proteins, Disease Models, Animal, Drosophila melanogaster, Electron Transport, Humans, Mitochondria, Mutation, Oxidative Phosphorylation, Oxygen Consumption, Parkinson Disease, Blotting, Western, Protein Serine-Threonine Kinases, GTP-Binding Proteins, Drosophila Proteins, Animals, Genetically Modified, Electron Transport Complex I, Gene Knockout Techniques
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