Saccani Simona, Pantano Serafino, Natoli Gioacchino
Institute for Research in Biomedicine, Via Vela 6, CH 6501, Bellinzona, Switzerland.
Nat Immunol. 2002 Jan;3(1):69-75. doi: 10.1038/ni748. Epub 2001 Dec 17.
We found that inflammatory stimuli induce p38 mitogen-activated protein kinase-dependent phosphorylation and phosphoacetylation of histone H3; this selectively occurred on the promoters of a subset of stimulus-induced cytokine and chemokine genes. p38 activity was required to enhance the accessibility of the cryptic NF-kappa B binding sites contained in H3 phosphorylated promoters, which indicated that p38-dependent H3 phosphorylation may mark promoters for increased NF-kappa B recruitment. These results show that p38 plays an additional role in the induction of the inflammatory and immune response: the regulation of NF-kappa B recruitment to selected chromatin targets.
我们发现，炎性刺激可诱导p38丝裂原活化蛋白激酶依赖性组蛋白H3的磷酸化和磷酸乙酰化；这种情况选择性地发生在刺激诱导的细胞因子和趋化因子基因亚群的启动子上。增强H3磷酸化启动子中隐藏的NF-κB结合位点的可及性需要p38活性，这表明p38依赖性H3磷酸化可能标记启动子以增加NF-κB的募集。这些结果表明，p38在炎症和免疫反应的诱导中发挥额外作用：调节NF-κB募集到选定的染色质靶点。
