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Originally published as MBC in Press, 10.1091/mbc.E07-11-1103 on February 20, 2008

Vol. 19, Issue 5, 1903-1911, May 2008

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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

Submitted November 5, 2007; Revised January 2, 2008; Accepted February 8, 2008
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, a finding that provides new insight into the cellular function of deubiquitination.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-11-1103) on February 20, 2008.

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

Abbreviations used: Drp1, dynamin-related protein 1; DUB, deubiquitinating enzyme; GST, glutathione transferase; Mfn, mitofusin; MOM, mitochondrial outer membrane; RNAi, RNA interference; shRNA, short-hairpin RNA; TM, transmembrane; Ub, ubiquitin; USP, ubiquitin-specific protease.






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