Loss of Parkin impairs mitochondrial function and leads to muscle atrophy
Open accessAbstract
Parkinson's disease is a neurodegenerative disease characterized by tremors, muscle stiffness, and muscle weakness. Molecular genetic analysis has confirmed that mutations in PARKIN and PINK1 genes, which play major roles in mitochondrial quality control and mitophagy, are frequently associated with Parkinson's disease. PARKIN is an E3 ubiquitin ligase that translocates to mitochondria during loss of mitochondrial membrane potential to increase mitophagy. Although muscle dysfunction is noted in Parkinson's disease, little is known about the involvement of PARKIN in the muscle phenotype of Parkinson's disease. In this study, we report that the mitochondrial uncoupler CCCP promotes PINK1/PARKIN-mediated mitophagy in myogenic C2C12 cells. As a result of this excess mitophagy, we show that CCCP treatment of myotubes leads to the development of myotube atrophy in vitro. Surprisingly, we also found that siRNA-mediated knockdown of Parkin results in impaired mitochondrial turnover. In addition, knockdown of Parkin led to myotubular atrophy in vitro. Consistent with these in vitro results, Parkin knockout muscles showed impaired mitochondrial function and smaller myofiber area, suggesting that Parkin function is required for post-natal skeletal muscle growth and development.
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Muscles of Parkin-deficient mice display impaired mitochondrial energetics.
“We and others have reported that muscles of Parkin-deficient mice display several aging-like features, including contractile dysfunction [154] and impaired mitochondrial energetics [147,153,154,155].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [155]
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Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging
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- Authors
- Peker, N., Donipadi, V., Sharma, M., McFarlane, C., & Kambadur, R.
- Affiliations
- Nanyang Technological University (SG)
- Singapore Institute for Clinical Sciences (SG)
- National University of Singapore (SG)
- Corresponding author
- Kambadur, Ravi
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2018-08-01
- Volume
- 315
- Issue
- 2
- Pages
- C164-C185
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2793058965
- Cited by
- 68
- References
- 79
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 9 · 2023: 5 · 2022: 12 · 2021: 12 · 2020: 13 · 2019: 4
- FWCI
- 4.91
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- ResearchOnline at James Cook University (James Cook University) (submittedVersion)
- DR-NTU (Nanyang Technological University) (submittedVersion)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- Parkin, PINK1, mitophagy, mitochondrial quality control, muscle atrophy, skeletal muscle development, mitochondrial turnover, E3 ubiquitin ligase, myotube atrophy, Parkin knockout mice, Parkinson's disease
- MeSH terms
- Animals, Cells, Cultured, Mice, Inbred C57BL, Mitochondria, Muscular Atrophy, Parkinson Disease, Protein Kinases, Muscle, Skeletal, Mitochondrial Proteins, Ubiquitin-Protein Ligases, Mice, Membrane Potential, Mitochondrial, Mitophagy
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