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Plays an Essential Role in the Phosphorylation of RelA/p65 on Serine 536 Induced by Lipopolysaccharide1
,
* Laboratory of Molecular Signaling and Apoptosis, Department of Biologic and Materials Sciences,
Department of Biological Chemistry, and
Program in Cellular and Molecular Biology, University of Michigan, Ann Arbor, MI 48109
Activation of the I
B kinase (IKK) complex by LPS induces phosphorylation and degradation of IB
, leading to the nuclear translocation of NF-B. Although it is essential for NF-B activation, emerging evidence has indicated that the nuclear translocation of NF-B is not sufficient to activate NF-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 or IKK
, we found that IKK played an essential role in LPS-induced p65 phosphorylation on serine 536, while IKK 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 plays an essential role in the LPS-induced p65 phosphorylation on serine 536, which may represent a mechanism to regulate the NF-B transcription activity by LPS.
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