A central role for s-nitrosylation in apoptosis

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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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of Medicine, Howard Hughes Medical Institute, Room 321 MSRB, Box 2612, Duke University Medical Center, Durham, 27710, NC, USA Moran Benhar & Jonathan S. Stamler Authors * Moran Benhar


View author publications You can also search for this author inPubMed Google Scholar * Jonathan S. Stamler View author publications You can also search for this author inPubMed Google


Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Benhar, M., Stamler, J. A central role for _S_-nitrosylation in apoptosis. _Nat Cell Biol_ 7,


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