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Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36

Title
Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36
Author
Ramakrishna Suresh
Keywords
deubiquitination; oxidative stress; ROS
Issue Date
2011-02
Publisher
WILEY-LISS
Citation
JOURNAL OF CELLULAR BIOCHEMISTRY, Page. 498-508
Abstract
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. J. Cell. Biochem. 112: 498?508, 2011. ⓒ 2010 Wiley?Liss, Inc.
URI
http://onlinelibrary.wiley.com/doi/10.1002/jcb.22940/abstract;jsessionid=934C8DF6923D6A41ED8E0685BE828C65.f02t03
ISSN
0730-2312
DOI
10.1002/jcb.22940
Appears in Collections:
GRADUATE SCHOOL OF BIOMEDICAL SCIENCE AND ENGINEERING[S](의생명공학전문대학원) > ETC
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