The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane
Open accessAbstract
Recent studies have suggested that ubiquitination of mitochondrial proteins participates in regulating mitochondrial dynamics in mammalian cells, but it is unclear whether deubiquitination is involved in this process. Here, we identify human ubiquitin-specific protease 30 (USP30) as a deubiquitinating enzyme that is embedded in the mitochondrial outer membrane. Depletion of USP30 expression by RNA interference induced elongated and interconnected mitochondria, depending on the activities of the mitochondrial fusion factors mitofusins, without changing the expression levels of the key regulators for mitochondrial dynamics. Mitochondria were rescued from this abnormal phenotype by ectopic expression of USP30 in a manner dependent on its enzymatic activity. Our findings reveal that USP30 participates in the maintenance of mitochondrial morphology, a finding that provides new insight into the cellular function of deubiquitination.
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Cites
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Functions and dysfunctions of mitochondrial dynamics
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Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
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Control of mitochondrial morphology by a human mitofusin
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The Machines that Divide and Fuse Mitochondria
Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790
Henry, K. W., Wyce, A., Lo, W.-S., Duggan, L. J., Emre, N. C. T., Kao, C.-F., Pillus, L., Shilatifard, A., Osley, M. A., & Berger, S. L. (2003) · Genes & Development · doi:10.1101/gad.1144003 · Cited by 714
Mitochondrial filaments and clusters as intracellular power-transmitting cables
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“The target sequences for Drp1 (Parone et al., 2006) and Mfn1 (Eura et al., 2003) RNAi were reported previously.”
BackgroundInfluentialSuzuki, A., Ishiyama, C., Hashiba, K., Shimizu, M., Ebnet, K., & Ohno, S. (2002) · Journal of Cell Science · doi:10.1242/jcs.00032 · Cited by 251
Cited by
Breaking the chains: structure and function of the deubiquitinases
Komander, D., Clague, M. J., & Urbé, S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2731 · Cited by 1,969
Deubiquitylating enzymes and drug discovery: emerging opportunities
Harrigan, J. A., Jacq, X., Martin, N. M., & Jackson, S. P. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.152 · Cited by 940
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy
Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., Foreman, O., Kirkpatrick, D. S., & Sheng, M. (2014) · Nature · doi:10.1038/nature13418 · Cited by 855
Shi, C.-S., Qi, H.-Y., Boularan, C., Huang, N.-N., Abu-Asab, M., Shelhamer, J. H., & Kehrl, J. H. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1303196 · Cited by 473
Deubiquitylases From Genes to Organism
Clague, M. J., Barsukov, I., Coulson, J. M., Liu, H., Rigden, D. J., & Urbé, S. (2013) · Physiological Reviews · doi:10.1152/physrev.00002.2013 · Cited by 425
Metadata
- Authors
- Nakamura, N., & Hirose, S.
- Venue
- Molecular Biology of the Cell
- Published
- 2008-05
- Volume
- 19
- Issue
- 5
- Pages
- 1903-1911
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2096216483
- Cited by
- 179
- References
- 10
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane. https://app.cochat.ai/papers/10.1091/mbc.e07-11-1103
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- Nakamura, N., & Hirose, S. (2008). Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e07-11-1103
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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