Abstract

NOJEK, Ignacio M. et al. Different  enzymatic activities recruitment by specific  domains of TIF2  are involved  in NF-kB transactivation. Medicina (B. Aires) [online]. 2004, vol.64, n.2, pp.135-138. ISSN 0025-7680.

We have previously shown that nuclear receptor coactivator overexpression significantly enhanced NF-kB activity in a dose response manner. We studied the mechanism  by which TIF2 regulates NF-kB activity. We determined that: 1) the p38 specific inhibitor reduces 50% NF-kB 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-a 20 ng/ml stimulated or not HEK 293 cell protein extract, and IkB only in  basal conditions, determined by binding pull down assays. This NF-kB complex regulates its activity and targets gene expression in a determined physiologic context depending on the coactivator complex content.

Keywords : Nuclear receptor coactivators; NF-kB; MAPK; TIF2.

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