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Parkin is required for exercise-induced mitophagy in muscle: impact of aging
Abstract
The maintenance of muscle health with advancing age is dependent on mitochondrial homeostasis. While reductions in mitochondrial biogenesis have been observed with age, less is known regarding organelle degradation. Parkin is an E3 ubiquitin ligase implicated in mitophagy, but few studies have examined Parkin’s contribution to mitochondrial turnover in muscle. Wild-type (WT) and Parkin knockout (KO) mice were used to delineate a role for Parkin-mediated mitochondrial degradation in aged muscle, in concurrence with exercise. Aged animals exhibited declines in muscle mass and mitochondrial content, paralleled by a nuclear environment endorsing the transcriptional repression of mitochondrial biogenesis. Mitophagic signaling was enhanced following acute endurance exercise in young WT mice but was abolished in the absence of Parkin. Basal mitophagy flux of the autophagosomal protein lipidated microtubule-associated protein 1A/1B-light chain 3 was augmented in aged animals but did not increase additionally with exercise when compared with young animals. In the absence of Parkin, exercise increased the nuclear localization of Parkin-interacting substrate, corresponding to a decrease in nuclear peroxisome proliferator gamma coactivator-1α. Remarkably, exercise enhanced mitochondrial ubiquitination in both young WT and KO animals. This suggested compensation of alternative ubiquitin ligases that were, however, unable to restore the diminished exercise-induced mitophagy in KO mice. Under basal conditions, we demonstrated that Parkin was required for mitochondrial mitofusin-2 ubiquitination. We also observed an abrogation of exercise-induced mitophagy in aged muscle. Our results demonstrate that acute exercise-induced mitophagy is dependent on Parkin and attenuated with age, which likely contributes to changes in mitochondrial content and quality in aging muscle.
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“Although conflicting data exist [54,145,146,147], several studies reported that mitophagy-related proteins are decreased in the skeletal muscle of old rodents [46,120,148,149,150,151,152].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [147]
In the citing paper
“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 [147]
In the citing paper
“Importantly, the majority of studies that reported an increase in Parkin content in aged muscles also reported that mitophagy was impaired/insufficient in aged skeletal muscles [145,146,147].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [147]
In the citing paper
“For instance, it has been reported that muscles from Parkin-deficient mice display lower mitophagy flux in response to acute exercise [147] and endurance training [153].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [147]
In the citing paper
“Under the conditions of stress, injury or aging, mitochondrial kinase PINK1 can gather outside the membrane of dysfunctional mitochondria and translocate them into it selectively by phosphorylating and recruiting Parkin, and then ubiquitinate outer mitochondrial membrane proteins such as mitochondrial fusion key proteins Mfn1/2 and fission key protein Drp1 to participate in mitophagy [48].”
From Lifelong Aerobic Exercise Alleviates Sarcopenia by Activating Autophagy and Inhibiting Protein Degradation via the AMPK/PGC-1α Signaling Pathway (2021) · cites this paper as [48]
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Metadata
- Authors
- Chen, C. C. W., Erlich, A. T., Crilly, M. J., & Hood, D. A.
- Affiliations
- York University (CA)
- Corresponding author
- Hood, David A.
- ORCID
- Hood, David A.
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2018-09-01
- Volume
- 315
- Issue
- 3
- Pages
- E404-E415
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2807114871
- Semantic Scholar
- 4601835e866b1f7b1dd68edc05405eb6f445e786
- Cited by
- 108
- References
- 67
- Citations by year
- 2026: 11 · 2025: 9 · 2024: 13 · 2023: 14 · 2022: 19 · 2021: 19 · 2020: 11 · 2019: 7 · 2018: 5
- FWCI
- 8.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (Conseil de Recherches en Sciences Naturelles et en Génie du Canada)
- Canada Research Chairs (Chaires de recherche du Canada)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- Parkin, mitophagy, physical activity, muscle aging, mitochondrial homeostasis, mitochondrial biogenesis, PGC-1α, mitofusin 2, mitochondrial ubiquitination, E3 ubiquitin ligase, skeletal muscle, autophagy
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Aging, Animals, Electron Transport Complex IV, Mice, Inbred C57BL, Mitochondria, Muscle, Physical Conditioning, Animal, Repressor Proteins, Mice, Knockout, Muscle, Skeletal, GTP Phosphohydrolases, Ubiquitin-Protein Ligases, Mice, Ubiquitination, Mitophagy
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