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Parkinson's Disease–Associated Kinase PINK1 Regulates Miro Protein Level and Axonal Transport of Mitochondria
Open accessAbstract
Mutations in Pten-induced kinase 1 (PINK1) are linked to early-onset familial Parkinson's disease (FPD). PINK1 has previously been implicated in mitochondrial fission/fusion dynamics, quality control, and electron transport chain function. However, it is not clear how these processes are interconnected and whether they are sufficient to explain all aspects of PINK1 pathogenesis. Here we show that PINK1 also controls mitochondrial motility. In Drosophila, downregulation of dMiro or other components of the mitochondrial transport machinery rescued dPINK1 mutant phenotypes in the muscle and dopaminergic (DA) neurons, whereas dMiro overexpression alone caused DA neuron loss. dMiro protein level was increased in dPINK1 mutant but decreased in dPINK1 or dParkin overexpression conditions. In Drosophila larval motor neurons, overexpression of dPINK1 inhibited axonal mitochondria transport in both anterograde and retrograde directions, whereas dPINK1 knockdown promoted anterograde transport. In HeLa cells, overexpressed hPINK1 worked together with hParkin, another FPD gene, to regulate the ubiquitination and degradation of hMiro1 and hMiro2, apparently in a Ser-156 phosphorylation-independent manner. Also in HeLa cells, loss of hMiro promoted the perinuclear clustering of mitochondria and facilitated autophagy of damaged mitochondria, effects previously associated with activation of the PINK1/Parkin pathway. These newly identified functions of PINK1/Parkin and Miro in mitochondrial transport and mitophagy contribute to our understanding of the complex interplays in mitochondrial quality control that are critically involved in PD pathogenesis, and they may explain the peripheral neuropathy symptoms seen in some PD patients carrying particular PINK1 or Parkin mutations. Moreover, the different effects of loss of PINK1 function on Miro protein level in Drosophila and mouse cells may offer one explanation of the distinct phenotypic manifestations of PINK1 mutants in these two species.
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“Once activated, Parkin has been reported to facilitate ubiquitination of numerous OMM proteins, including Mfn1 [126,127,128], Mfn2 [129], VDAC [130], Tom20 (translocase of the outer membrane 20) [121], and Miro [131].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [131]
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Metadata
- Authors
- Liu, S., Sawada, T., Lee, S., Yu, W., Silverio, G., Alapatt, P., Millan, I., Shen, A., Saxton, W., Kanao, T., Takahashi, R., Hattori, N., Imai, Y., & Lu, B.
- Affiliations
- Stanford Medicine (US)
- Kyoto University (JP)
- Washington University in St. Louis (US)
- University of California, Santa Cruz (US)
- Juntendo University (JP)
- Corresponding author
- Imai, Yuzuru
- Lu, Bingwei
- Venue
- PLoS Genetics
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-03-01
- Volume
- 8
- Issue
- 3
- Pages
- e1002537
- ISSN
- 1553-7390 (ISSN-L)
- 1553-7404
- PMC
- PMC3291531
- OpenAlex
- W2148819754
- Cited by
- 371
- References
- 59
- Citations by year
- 2026: 11 · 2025: 10 · 2024: 10 · 2023: 11 · 2022: 18 · 2021: 35 · 2020: 29 · 2019: 22 · 2018: 28 · 2017: 30 · 2016: 36 · 2015: 32 · 2014: 42 · 2013: 33 · 2012: 23
- FWCI
- 27.18
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Genetics (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology (CREST)
- Dainippon Sumitomo Pharma
- Ministry of Health, Labour and Welfare
- National Institutes of Health
- Japan Society for the Promotion of Science (23390232, 23111002, 23890206, 23790973)
- National Institute of Mental Health (R01MH080378)
- National Institute of General Medical Sciences (R01GM084947, GM084947)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR054926)
- Core Research for Evolutional Science and Technology
- 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 › Mitochondrial Function and Pathology
- Keywords
- PINK1, Miro1, Miro2, Parkinson's disease, mitochondrial motility, Parkin, mitophagy, mitochondrial quality control, dopaminergic neurons, motor neurons, ubiquitin-mediated proteolysis, peripheral neuropathy, Drosophila
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, Autophagy, Axonal Transport, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Disease Models, Animal, Drosophila, Gene Expression Regulation, HeLa Cells, Humans, Mitochondria, Motor Neurons, Parkinson Disease, Protein Serine-Threonine Kinases, Mice, Knockout, rho GTP-Binding Proteins, Drosophila Proteins, Ubiquitin-Protein Ligases, Mutant Proteins, Mice, Dopaminergic Neurons, Proton Ionophores
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