p38-dependent marking of inflammatory genes for increased NF-κB recruitment

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-kappaB binding sites contained in H3 phosphorylated promoters, which indicated that p38-dependent H3 phosphorylation may mark promoters for increased NF-kappaB recruitment. These results show that p38 plays an additional role in the induction of the inflammatory and immune response: the regulation of NF-kappaB recruitment to selected chromatin targets.