Source:http://linkedlifedata.com/resource/pubmed/id/21268071
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
2011-1-26
|
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
1097-4644
|
| pubmed:author | |
| pubmed:copyrightInfo |
Copyright © 2010 Wiley-Liss, Inc.
|
| pubmed:issnType |
Electronic
|
| pubmed:volume |
112
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
498-508
|
| pubmed:meshHeading |
pubmed-meshheading:21268071-Animals,
pubmed-meshheading:21268071-Blotting, Western,
pubmed-meshheading:21268071-COS Cells,
pubmed-meshheading:21268071-Cell Line,
pubmed-meshheading:21268071-Cercopithecus aethiops,
pubmed-meshheading:21268071-Computational Biology,
pubmed-meshheading:21268071-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:21268071-HeLa Cells,
pubmed-meshheading:21268071-Humans,
pubmed-meshheading:21268071-Immunoprecipitation,
pubmed-meshheading:21268071-Mitochondria,
pubmed-meshheading:21268071-Protein Binding,
pubmed-meshheading:21268071-Protein Stability,
pubmed-meshheading:21268071-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:21268071-Superoxide Dismutase,
pubmed-meshheading:21268071-Two-Hybrid System Techniques,
pubmed-meshheading:21268071-Ubiquitin Thiolesterase,
pubmed-meshheading:21268071-Ubiquitination
|
| pubmed:year |
2011
|
| pubmed:articleTitle |
Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36.
|
| pubmed:affiliation |
Department of Biomedical Science, CHA General Hospital, CHA University, Seoul, Republic of Korea.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|