title: Regulation of apoptosis by protein S-nitrosylation.
abstract: S-nitrosylation/denitrosylation of critical cysteine residues on proteins serves as a redox switch that regulates the function of a wide array of proteins. A key signaling pathway that is regulated by S-nitrosylation is apoptotic cell death. Here we will review the proteins in apoptotic pathways that are known to be S-nitrosylated by endogenous NO production. The targets and functional consequences of S-nitrosylation during apoptosis are multifaceted, allowing cells to fine tune their response to apoptotic signals.
authors.affiliation: Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01605, U.S.A. joan.mannick@umassmed.edu
authors.forename: J B
authors.initials: JB
authors.lastname: Mannick
mesh_terms: D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D020169:Caspases / Q000378:metabolism; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / Q000378:metabolism; D006801:Humans; D009569:Nitric Oxide / Q000378:metabolism*; D019001:Nitric Oxide Synthase / Q000378:metabolism; D013879:Thioredoxins / Q000378:metabolism
chemical_list: D009569:Nitric Oxide; D013879:Thioredoxins; D019001:Nitric Oxide Synthase; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); D020169:Caspases