Authors
Mannick, Joan B.Schonhoff, Christopher M.
Papeta, Natalia
Ghafourifar, Pedram
Szibor, Marten
Fang, Kezhong
Gaston, Benjamin M.
UMass Chan Affiliations
Department of Medicine, Division of Infectious Diseases and ImmunologyDocument Type
Journal ArticlePublication Date
2001-09-12Keywords
Antigens, CD95Caspase 3
Caspase 9
Caspases
Enzyme Precursors
Humans
Mitochondria
Nitric Oxide Synthase
Protein Sorting Signals
Protein Transport
Subcellular Fractions
Tumor Cells, Cultured
Cell Biology
Immunology and Infectious Disease
Metadata
Show full item recordAbstract
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.Source
J Cell Biol. 2001 Sep 17;154(6):1111-6. Epub 2001 Sep 10. Link to article on publisher's siteDOI
10.1083/jcb.200104008Permanent Link to this Item
http://hdl.handle.net/20.500.14038/42592PubMed ID
11551979Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1083/jcb.200104008