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Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36.

Authors
  • 1
  • 1 Department of Biomedical Science, CHA General Hospital, CHA University, Seoul, Republic of Korea. , (North Korea)
Type
Published Article
Journal
Journal of Cellular Biochemistry
1097-4644
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
112
Issue
2
Pages
498–508
Identifiers
DOI: 10.1002/jcb.22940
PMID: 21268071
Source
Medline
License
Unknown

Abstract

SOD2 is a key mitochondrial antioxidant enzyme and its perturbation leads to oxidative cell death, which results in various disorders. In this study, we identified a deubiquitinating enzyme USP36 that regulates the protein stability of SOD2. The regulatory effect of USP36 on SOD2 was initially identified by 2-DE and MALDI-TOF/MS analyses. In addition, endogenous USP36 and SOD2 were shown to interact in an immunoprecipitation assay, which was verified using the yeast two-hybrid system. Furthermore, we demonstrated that SOD2 binds with ubiquitin molecules to form polyubiquitination chains and undergoes degradation through the ubiquitin-proteasomal pathway. Finally, USP36 was shown to be a specific deubiquitinating enzyme that reduces the ubiquitination level of SOD2 and was involved in SOD2 protein stability by extending its half-life.

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