News and Views
Nature Cell Biology 7, 645 - 646 (2005)
doi:10.1038/ncb0705-645
A central role for S-nitrosylation in apoptosis
Moran Benhar1 & Jonathan S. Stamler1
- Moran Benhar and Jonathan S. Stamler are at the Howard Hughes Medical Institute, Department of Medicine, Room 321 MSRB, Box 2612, Duke University Medical Center, Durham, NC 27710, USA. e-mail: STAML001@mc.duke.edu
Abstract
New work reveals a key signal transduction pathway through which nitric oxide (NO) regulates apoptosis induced by disparate cellular stresses. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is S-nitrosylated by NO, which initiates an interaction with the E3 ligase Siah1, leading to nuclear translocation and ubiquitin-mediated degradation of nuclear target proteins.
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