The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
PINK1/Parkin-mediated mitophagy in mammalian cells
Abstract
Mitochondria-specific autophagy (mitophagy) is a fundamental process critical for maintaining mitochondrial fitness in a myriad of cell types. Particularly, mitophagy contributes to mitochondrial quality control by selectively eliminating dysfunctional mitochondria. In mammalian cells, the Ser/Thr kinase PINK1 and the E3 ubiquitin ligase Parkin act cooperatively in sensing mitochondrial functional state and marking damaged mitochondria for disposal via the autophagy pathway. Notably, ubiquitin and deubiquitinases play vital roles in modulating Parkin activity and mitophagy efficiency. In this review, we highlight recent breakthroughs addressing the key issues of how PINK1 activates Parkin in response to mitochondrial malfunction, how Parkin localizes specifically to impaired mitochondria, and how ubiquitination and deubiquitination regulate PINK1/Parkin-mediated mitophagy.
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“There are apparently several pathways to mitophagy [169,170], but the most important and the better understood one is the canonical PINK1/PARKIN pathway [171,172,173,174,175,176].”
From The mitochondrial permeability transition: Nexus of aging, disease and longevity (2021) · cites this paper as [173]
Citations
Cites
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477
Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298
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Research works printed but not linked: 1
- Fiesel, 2014, A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently, J Cell Sci, 127, 3488
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Unraveling the pyroptosis-mitophagy axis: from molecular mechanisms to therapeutic opportunities
Ban, J., 陈然兴, Ao, L., Zhao, H., Li, J., Wei, Y., & Huang, G. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1950578
Cao, S., Cheng, X., Yang, Y., Lu, B., Li, S., 黄春田, Ba, M., Luo, L., & Zhao, C. (2026) · Frontiers in Medicine · doi:10.3389/fmed.2026.1961366
Sezer, Z., Kayisli, U. A., Önder, S. Y., Çepni, İ., Timuroğlu, T., & Güzel, E. (2026) · Histochemistry and Cell Biology · doi:10.1007/s00418-026-02544-z
Wei, S., Hao, F., Zhang, W., & Xing, H. (2026) · Pharmacognosy Magazine · doi:10.1177/09731296261491136
Molecular markers of mitochondrial intoxication
Seloto, D. G., Kohori, N. A., Lima, T. D. S., & Pereira, L. C. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-45078-5.00024-5
Metadata
- Authors
- Eiyama, A., & Okamoto, K.
- Affiliations
- The University of Osaka (JP)
- Corresponding author
- Okamoto, Koji
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2015-04
- Volume
- 33
- Pages
- 95-101
- ISSN
- 0955-0674 (ISSN-L)
- OpenAlex
- W2013642338
- Cited by
- 603
- References
- 61
- Citations by year
- 2026: 45 · 2025: 66 · 2024: 71 · 2023: 74 · 2022: 83 · 2021: 68 · 2020: 57 · 2019: 36 · 2018: 38 · 2017: 22 · 2016: 29 · 2015: 14
- FWCI
- 4.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (25291045, 25650067)
- Ministry of Education, Culture, Sports, Science and Technology (26111513)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- mitophagy, PINK1, Parkin, mitochondrial quality control, mitochondrial dysfunction, ubiquitination, deubiquitination, E3 ubiquitin ligase, Ser/Thr kinase, mammalian cells
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, Enzyme Activation, Humans, Mammals, Mitochondria, Phosphorylation, Protein Kinases, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination, Mitophagy, Ubiquitin-Specific Proteases
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