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MBC in Press, published online ahead of print February 20, 2008
Mol. Biol. Cell 10.1091/mbc.E07-11-1103

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Submitted on November 5, 2007
Revised on January 2, 2008
Accepted on February 8, 2008

Regulation of Mitochondrial Morphology by Usp30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane

Nobuhiro Nakamura and Shigehisa Hirose

Department of Biological Sciences, Tokyo Institute of Technology, Yokohama 226-8501, Japan

Monitoring Editor: Janet Shaw

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, which finding provides a new insight into the cellular function of deubiquitination.

Address correspondence to: Nobuhiro Nakamura (nnakamur{at}bio.titech.ac.jp)






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