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Different enzymatic activities recruitme ... ed in NF-kappaB transactivation
Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-kappaB transactivation
7350
We have previously shown that nuclear receptor coactivator overexpression significantly enhanced NF-kappaB activity in a dose response manner. We studied the mechanism by which TIF2 regulates NF-kappaB activity. We determined that: 1) the p38 specific inhibitor reduces 50% NF-kappaB transcriptional activity, even in cells that overexpress distinct TIF2 deletions; 2) there is a physical interaction between TIF2 and p38 and RelA determined through in vitro translated protein binding assays; 3) TIF2 is a p38 substrate; 4) there is a physical interaction between TIF2 and IKK in TNF-alpha 20 ng/ml stimulated or not HEK 293 cell protein extract, and IkappaB only in basal conditions, determined by binding pull down assays. This NF-kappaB complex regulates its activity and targets gene expression in a determined physiologic context depending on the coactivator complex content.
Nojek IM, Werbajh SE, Colo GP, Rubio FM, Franco LD, Nahmod VE, Costas MA
Medicina
2004-01-01 00:00
64
2
135-8
Cell Nucleus,Cytoplasm,Enzyme Activation,Humans,NF-kappa B,Nuclear Receptor Coactivator 2,Phosphorylation,Trans-Activation (Genetics),Transcription Factors,p38 Mitogen-Activated Protein Kinases,NCOA2 protein, human,NF-kappa B,Nuclear Receptor Coactivator 2,Transcription Factors,p38 Mitogen-Activated Protein Kinases
Instituto de Investigaciones Médicas Alfredo Lanari, Buenos Aires, Argentina.
Medicina (B Aires)
0025-7680
0
False
15628300
