Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36.
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.
Mesh Terms:
Animals, Blotting, Western, COS Cells, Cell Line, Cercopithecus aethiops, Computational Biology, Electrophoresis, Gel, Two-Dimensional, Hela Cells, Humans, Immunoprecipitation, Mitochondria, Protein Binding, Protein Stability, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Superoxide Dismutase, Two-Hybrid System Techniques, Ubiquitin Thiolesterase, Ubiquitination
Animals, Blotting, Western, COS Cells, Cell Line, Cercopithecus aethiops, Computational Biology, Electrophoresis, Gel, Two-Dimensional, Hela Cells, Humans, Immunoprecipitation, Mitochondria, Protein Binding, Protein Stability, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Superoxide Dismutase, Two-Hybrid System Techniques, Ubiquitin Thiolesterase, Ubiquitination
J. Cell. Biochem.
Date: Feb. 01, 2011
PubMed ID: 21268071
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- Interactions 3
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