Acetylation of Stat1 modulates NF-κB activity

Histone deacetylases and the immunological network: implications in cancer and inflammation

“…STAT1 is phosphorylated in response to cytokine and growth factor stimulation. This event could be counteracted by dephosphorylation or CBP acetylation, which promotes STAT1 nuclear export (Kra¨mer et al, 2006). Once acetylated, STAT1 can be deacetylated by HDAC3, as well as HDAC1 and 2, thus permitting its phosphorylation and reactivation (Klampfer et al, 2004;Kra¨mer et al, 2009).…”

Induction of inducible NO synthase in bystander human T cells increases allogeneic responses in the vasculature

“…On the other hand, JAK/STAT signaling can inhibit the immune response under certain circumstances. STAT1, STAT3, and STAT5 have all been shown to inhibit the expression of certain NF-B-controlled inflammatory genes (24)(25)(26). STAT1 also inhibits cytokineinduced iNOS expression in the human fibroblast cell line 2fTGH through the inhibition of NF-B-mediated gene transcription (27).…”

Modulation of Gene Expression Regulated by the Transcription Factor NF-κB/RelA

“…Acetylated STAT1 will repress the expression of antiapoptosis NF-B target genes via binding RelA and nuclear export (38) as revealed by in situ immunofluorescence analysis. To verify the interaction between RelA and STAT1 in the nucleus, we used immunoprecipitation and quantitative stable isotope dilution-SRM-MS (31) in the samples obtained from the immunoprecipitation by anti-RelA antibody and nonspecific IgG (negative control) from the nuclear extract of A549 cells.…”

“…An interaction between STAT1 and RelA has been previously implicated by co-localization experiments based on confocal fluorescence microscopy (38). To verify the interaction between RelA and STAT1, we used immunoprecipitation and quantitative stable isotope dilution-SRM-MS to measure the enrichment of STAT1 in the sample obtained from the immunoprecipitation of anti-RelA antibody.…”