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• W1555980866 endingPage "5635" @default.
• W1555980866 startingPage "5630" @default.
• W1555980866 abstract "Activation of the I kappa B kinase (IKK) complex by LPS induces phosphorylation and degradation of I kappa B alpha, leading to the nuclear translocation of NF-kappa B. Although it is essential for NF-kappa B activation, emerging evidence has indicated that the nuclear translocation of NF-kappa B is not sufficient to activate NF-kappa B-dependent transcription. Here, we reported that LPS induced the phosphorylation of the p65 trans-activation domain on serine 536 in monocytes/macrophages. Using mouse embryonic fibroblasts lacking either IKK alpha or IKK beta, we found that IKK beta played an essential role in LPS-induced p65 phosphorylation on serine 536, while IKK alpha was partially required for the p65 phosphorylation. The LPS-induced p65 phosphorylation on serine 536 was independent of the phosphatidylinositol 3'-kinase/Akt signaling pathway. Furthermore, we found that the phosphorylation on serine 536 increased the p65 transcription activity. In summary, our results demonstrate that IKK beta plays an essential role in the LPS-induced p65 phosphorylation on serine 536, which may represent a mechanism to regulate the NF-kappa B transcription activity by LPS." @default.
• W1555980866 created "2016-06-24" @default.
• W1555980866 creator A5016834516 @default.
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• W1555980866 date "2003-06-01" @default.
• W1555980866 modified "2023-10-08" @default.
• W1555980866 title "IKKβ Plays an Essential Role in the Phosphorylation of RelA/p65 on Serine 536 Induced by Lipopolysaccharide" @default.
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• W1555980866 doi "https://doi.org/10.4049/jimmunol.170.11.5630" @default.
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