共查询到20条相似文献,搜索用时 31 毫秒
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Imamura T Imamura C Iwamoto Y Sandell LJ 《The Journal of biological chemistry》2005,280(17):16625-16634
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Cooperative interactions between CBP and TORC2 confer selectivity to CREB target gene expression 总被引:2,自引:0,他引:2
Ravnskjaer K Kester H Liu Y Zhang X Lee D Yates JR Montminy M 《The EMBO journal》2007,26(12):2880-2889
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Sen N Hara MR Kornberg MD Cascio MB Bae BI Shahani N Thomas B Dawson TM Dawson VL Snyder SH Sawa A 《Nature cell biology》2008,10(7):866-873
Besides its role in glycolysis, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) initiates a cell death cascade. Diverse apoptotic stimuli activate inducible nitric oxide synthase (iNOS) or neuronal NOS (nNOS), with the generated nitric oxide (NO) S-nitrosylating GAPDH, abolishing its catalytic activity and conferring on it the ability to bind to Siah1, an E3-ubiquitin-ligase with a nuclear localization signal (NLS). The GAPDH-Siah1 protein complex, in turn, translocates to the nucleus and mediates cell death; these processes are blocked by procedures that interfere with GAPDH-Siah1 binding. Nuclear events induced by GAPDH to kill cells have been obscure. Here we show that nuclear GAPDH is acetylated at Lys 160 by the acetyltransferase p300/CREB binding protein (CBP) through direct protein interaction, which in turn stimulates the acetylation and catalytic activity of p300/CBP. Consequently, downstream targets of p300/CBP, such as p53 (Refs 10,11,12,13,14,15), are activated and cause cell death. A dominant-negative mutant GAPDH with the substitution of Lys 160 to Arg (GAPDH-K160R) prevents activation of p300/CBP, blocks induction of apoptotic genes and decreases cell death. Our findings reveal a pathway in which NO-induced nuclear GAPDH mediates cell death through p300/CBP. 相似文献
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