Drosophila Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin
Open accessAbstract
Loss of the E3 ubiquitin ligase Parkin causes early onset Parkinson's disease, a neurodegenerative disorder of unknown etiology. Parkin has been linked to multiple cellular processes including protein degradation, mitochondrial homeostasis, and autophagy; however, its precise role in pathogenesis is unclear. Recent evidence suggests that Parkin is recruited to damaged mitochondria, possibly affecting mitochondrial fission and/or fusion, to mediate their autophagic turnover. The precise mechanism of recruitment and the ubiquitination target are unclear. Here we show in Drosophila cells that PINK1 is required to recruit Parkin to dysfunctional mitochondria and promote their degradation. Furthermore, PINK1 and Parkin mediate the ubiquitination of the profusion factor Mfn on the outer surface of mitochondria. Loss of Drosophila PINK1 or parkin causes an increase in Mfn abundance in vivo and concomitant elongation of mitochondria. These findings provide a molecular mechanism by which the PINK1/Parkin pathway affects mitochondrial fission/fusion as suggested by previous genetic interaction studies. We hypothesize that Mfn ubiquitination may provide a mechanism by which terminally damaged mitochondria are labeled and sequestered for degradation by autophagy.
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Once activated, Parkin facilitates ubiquitination of numerous outer mitochondrial membrane proteins, including Mfn1, Mfn2, VDAC, Tom20, and Miro.
“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 [128]
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Shen, J. L., Fortier, T. M., Zhao, Y. G., Wang, R., Burmeister, M., & Baehrecke, E. H. (2021) · Current Biology · doi:10.1016/j.cub.2021.04.062 · Cited by 36 · see citing works
A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling
Shiba-Fukushima, K., Inoshita, T., Sano, O., Iwata, H., Ishikawa, K.-I., Okano, H., Akamatsu, W., Imai, Y., & Hattori, N. (2020) · iScience · doi:10.1016/j.isci.2020.101048 · Cited by 37 · see citing works
- Authors
- Ziviani, E., Tao, R. N., & Whitworth, A. J.
- Affiliations
- Medical Research Council (GB)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-03
- Volume
- 107
- Issue
- 11
- Pages
- 5018-5023
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2841909
- OpenAlex
- W1979645469
- Cited by
- 735
- References
- 46
- Citations by year
- 2026: 12 · 2025: 17 · 2024: 23 · 2023: 29 · 2022: 27 · 2021: 42 · 2020: 54 · 2019: 38 · 2018: 35 · 2017: 40 · 2016: 46 · 2015: 61 · 2014: 61 · 2013: 71 · 2012: 75
- FWCI
- 47.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by-nc-nd)
- Funders
- Wellcome Trust (081987, GR077544AIA)
- Parkinson's UK (G-0713)
- Medical Research Council (GR077544AIA)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- Parkin, PINK1, mitofusins, mitochondrial fission, mitochondrial fusion, ubiquitination, E3 ubiquitin ligase, Parkinson's disease, mitophagy, mitochondrial translocation, mitochondrial homeostasis, Drosophila
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, Autophagy, Drosophila melanogaster, Membrane Proteins, Mitochondria, Mutation, Protein Serine-Threonine Kinases, Protein Transport, Drosophila Proteins, Ubiquitin-Protein Ligases, Ubiquitination, Gene Knockdown Techniques
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