Glutathione Depletion in CYP2E1-Expressing Liver Cells Induces Toxicity Due to the Activation of p38 Mitogen-Activated Protein Kinase and Reduction of Nuclear Factor-κB DNA Binding Activity

2004 ◽  
Vol 66 (3) ◽  
pp. 749-760 ◽  
Author(s):  
Defeng Wu ◽  
Arthur Cederbaum
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Nuclear Factor Κb ◽  
Liver Cells ◽  
Binding Activity ◽  
Mitogen Activated Protein Kinase ◽  
Glutathione Depletion ◽  
Nuclear Factor ◽  
Dna Binding Activity ◽  
Mitogen Activated Protein

scholarly journals Tobacco Transcription Factor WRKY1 Is Phosphorylated by the MAP Kinase SIPK and Mediates HR-Like Cell Death in Tobacco

2005 ◽  
Vol 18 (10) ◽  
pp. 1027-1034 ◽  
Author(s):  
Frank L. H. Menke ◽  
Hong-Gu Kang ◽  
Zhixiang Chen ◽  
Jeong Mee Park ◽  
Dhirendra Kumar ◽  
...  
Keyword(s):  
Cell Death ◽  
Transcription Factor ◽  
Protein Kinase ◽  
Dna Binding ◽  
Kinase Inhibitor ◽  
Hybrid Approach ◽  
Binding Activity ◽  
Mitogen Activated Protein Kinase ◽  
Dna Binding Activity ◽  
Mitogen Activated Protein

The salicylic acid-induced protein kinase (SIPK) of tobacco, which is a mitogen-activated protein kinase (MAPK), is activated by various biotic and abiotic treatments. Overexpression of SIPK has been shown to trigger cell death. In this study, a targeted yeast two-hybrid approach identified the tobacco transcription factor WRKY1 as a potential substrate. SIPK phosphorylated WRKY1, which resulted in enhanced DNA-binding activity of WRKY1 to its cognate binding site, a W box sequence from the tobacco chitinase gene CHN50. SIPK-mediated enhancement of WRKY1 DNA-binding activity was inhibited by staurosporine, a general kinase inhibitor. Co-expression of SIPK and WRKY1 in Nicotiana benthamiana led to more rapid cell death than expression of SIPK alone, suggesting that WRKY1 is involved in the formation of hypersensitive response-like cell death and may be a component of the signaling cascade downstream of SIPK.

UV stimulation induces nuclear factor κB (NF-κB) DNA-binding activity but not transcriptional activation

2001 ◽  
Vol 29 (6) ◽  
pp. 688-691 ◽  
Author(s):  
K. J. Campbell ◽  
N. R. Chapman ◽  
N. D. Perkins
Keyword(s):  
Dna Binding ◽  
Transcriptional Activation ◽  
Cellular Response ◽  
Uv Light ◽  
Binding Protein ◽  
Nuclear Factor Κb ◽  
Camp Response Element Binding ◽  
Binding Activity ◽  
Nuclear Factor ◽  
Dna Binding Activity

The cellular response to DNA-damaging agents is partly mediated by DNA-binding transcription factors such as p53 and nuclear factor κB (NF-κB). Typically NF-κB activation is associated with resistance to apoptosis. Following stimulation with UV light however, NF-κB activation has been shown to be required for programmed cell death. To study this effect further and to determine the relationship between NF-κB and p53 function, we have examined the effect of UV light on U2OS cells. UV stimulation resulted in the activation of NF-κB DNA-binding and the induction of p53. Surprisingly, and in contrast with tumour necrosis factor α stimulation, this UV-induced NF-κB was transcriptionally inert. These observations suggest a model in which the NF-κB switch from an anti-apoptotic to a pro-apoptotic role within the cell results from modulation of its ability to stimulate gene expression, possibly as a result of the ability of p53 to sequester transcriptional co-activator proteins such as p300/CREB (cAMP-response-element-binding protein)-binding protein.

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