STAT1 signaling is not regulated by a phosphorylation-acetylation switch.

ABSTRACT: The treatment of cells with histone deacetylase inhibitors (HDACi) was reported to reveal the acetylation of STAT1 at lysine 410 and lysine 413 (O. H. Krämer et al., Genes Dev. 20:473-485, 2006). STAT1 acetylation was proposed to regulate apoptosis by facilitating binding to NF-κB and to control immune responses by suppressing STAT1 tyrosine phosphorylation, suggesting that STAT1 acetylation is a central mechanism by which histone deacetylase inhibitors ameliorate inflammatory diseases (O. H. Krämer et al., Genes Dev. 23:223-235, 2009). Here, we show that the inhibition of deacetylases had no bearing on STAT1 acetylation and did not diminish STAT1 tyrosine phosphorylation. The glutamine mutation of the alleged acetylation sites, claimed to mimic acetylated STAT1, similarly did not diminish

SUBMITTER: Antunes F 

PROVIDER: S-EPMC3133404 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature