Article
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding.
Nature cell biology - 1 Jul 2005
Hara Makoto R, Agrawal Nishant, Kim Sangwon F, Cascio Matthew B, Fujimuro Masahiro, Ozeki Yuji, Takahashi Masaaki, Cheah Jaime H, Tankou Stephanie K, Hester Lynda D, Ferris Christopher D, Hayward S Diane, Snyder Solomon H, Sawa Akira
Abstract excerpt
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) influences cytotoxicity, translocating to the nucleus during apoptosis. Here we report a signalling pathway in which nitric oxide (NO) generation that follows apoptotic stimulation elicits S-nitrosylation of GAPDH, which triggers binding to Siah1 (an E3 ubiquitin ligase), nuclear translocation and apoptosis. S-nitrosylation of GAPDH augments its binding to Siah1,...
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