Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation
We have previously shown that nuclear receptor coactivator overexpression significantly enhanced NF-κB activity in a dose response manner. We studied the mechanism by which TIF2 regulates NF-κB activity. We determined that: 1) the p38 specific inhibitor reduces 50% NF-κB transcriptional activity, ev...
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| Autores principales: | , , , , , , |
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| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00257680_v64_n2_p135_Nojek |
| Aporte de: |
| Sumario: | We have previously shown that nuclear receptor coactivator overexpression significantly enhanced NF-κB activity in a dose response manner. We studied the mechanism by which TIF2 regulates NF-κB activity. We determined that: 1) the p38 specific inhibitor reduces 50% NF-κB 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 bindind assays; 3) TIF2 is a p38 substrate; 4) there is a physical interaction between TIF2 and IKK in TNF-α 20 ng/ml stimulated or not HEK 293 cell protein extract, and IκB only in basal conditions, determined by binding pull down assays. This NF-κ B complex regulates its activity and targets gene expression in a determined physiologic context depending on the coactivator complex content. |
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