GAPDH mediates nitrosylation of nuclear proteins

The activity of myriad nuclear proteins is regulated by S -nitrosylation, but a nuclear nitrosylase has remained elusive. GAPDH is now shown to be nitrosylated in the cytoplasm, which promotes its import into the nucleus, where it then transnitrosylates nuclear proteins. S -nitrosylation of proteins...

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Veröffentlicht in:	Nature cell biology 2010-11, Vol.12 (11), p.1094-1100
Hauptverfasser:	Kornberg, Michael D., Sen, Nilkantha, Hara, Makoto R., Juluri, Krishna R., Nguyen, Judy Van K., Snowman, Adele M., Law, Lindsey, Hester, Lynda D., Snyder, Solomon H.
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/612 631/80/458/2386 Biomedical and Life Sciences Cancer Research Cell Biology Cells, Cultured Cellular proteins Cellular signal transduction Dehydrogenase Deoxyribonucleic acid Developmental Biology DNA DNA-Activated Protein Kinase - metabolism Genetic aspects Glyceraldehyde 3-phosphate dehydrogenase Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism Health aspects Histone Deacetylase 2 - metabolism Humans Insects Kinases letter Life Sciences Medicine Mutation Nitric oxide Nitric Oxide - metabolism Nitric Oxide Donors - pharmacology Nuclear Proteins - metabolism Peptides Properties Proteins Signal Transduction Sirtuin 1 - antagonists & inhibitors Sirtuin 1 - metabolism Stem Cells
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