Interleukin-1 receptor-associated kinase (IRAK)-1-mediated NF-κB activation requires cytosolic and nuclear activity
Interleukin-1 receptor-associated kinase (IRAK)-1-mediated NF-κB activation requires cytosolic and nuclear activity
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DOI:
10.1096/fj.07-101816
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发表时间:
2008-07-01
期刊:
影响因子:
4.8
通讯作者:
Abraham, Edward
中科院分区:
文献类型:
--
作者:
Liu, Gang;Park, Young-Jun;Abraham, Edward
Interleukin-1 receptor-associated kinase (IRAK) -1 plays an essential role in Toll-like receptor/interleukin-1 receptor (TLR/IL-1R) -associated NF-kappa B activation through its involvement in IKK activation, which then leads to subsequent I kappa B degradation and NF-kappa B nuclear translocation. In the present studies, we demonstrate a novel pathway in which IRAK-1 present in the nucleus participates in NF-kappa B-dependent gene expression. Nuclear localization of IRAK-1 is increased on cellular stimulation with IL-1 and LPS, or CRM-1-dependent nuclear export blockade. Induction of IRAK-1 produces enhanced NF-kappa B transcriptional activity that precedes I kappa B-alpha degradation and nuclear translocation of NF-kappa B. IRAK-1 binds to the promoter of NF-kappa B-regulated gene, I kappa B-alpha, and enhances binding of the NF-kappa B p65 subunit to NF-kappa B responsive elements within the I kappa B-alpha promoter. IRAK-1 phosphorylates histone H3 in vitro and is required for IL-1-induced phosphorylation of histone H3 at serine 10 in vivo. These data indicate that both cytosolic and nuclear actions of IRAK-1 participate in the activation of NF kappa B-dependent transcriptional events.