期刊
JOURNAL OF CELL BIOLOGY
卷 154, 期 6, 页码 1111-1116出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200104008
关键词
nitric oxide; caspase-3; caspase-9; mitochondria; S-nitrosylation
类别
资金
- NHLBI NIH HHS [R56 HL059337, HL59337, R01 HL059337] Funding Source: Medline
- NIGMS NIH HHS [GM57601] Funding Source: Medline
Caspase-3 is a cysteine protease located in both the cytoplasm and mitochondrial intermembrane space that is a central effector of many apoptotic pathways. In resting cells, a subset of caspase-3 zymogens is S-nitrosylated at the active site cysteine, inhibiting enzyme activity. During Fas-induced apoptosis, caspases are denitrosylated, allowing the catalytic site to function. In the current studies, we sought to identify the subpopulation of caspases that is regulated by S-nitrosylation. We report that the majority of mitochondrial, but not cytoplasmic, caspase-3 zymogens contain this inhibitory modification. In addition, the majority of mitochondrial caspase-9 is S-nitrosylated. These studies suggest that S-nitrosylation plays an important role in regulating mitochondrial caspase function and that the S-nitrosylation state of a given protein depends on its subcellular localization.
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