SummaryNF-kB regulates the expression of a large number of target genes involved in the immune and inflammatory response, apoptosis, cell proliferation, differentiation and survival. In this study, we identified SIRT2 as a deacetylase of the transcription factor p65. SIRT2 is a member of the family of sirtuins, which are NAD + -dependent deacetylases involved in several cellular processes. SIRT2 interacts with p65 in the cytoplasm and deacetylates p65 in vitro and in vivo at Lys310. Moreover, p65 is hyperacetylated at Lys310 in Sirt2 -/-cells after TNFa stimulation, which results in the increase in expression of a subset of p65 acetylation-dependent target genes. Our work provides evidence that p65 is deacetylated by SIRT2 in the cytoplasm to regulate the expression of specific NF-kBdependent genes.

The authors explained that the data in the two figures validate the specificity of antibodies generated against different acetylated lysines of p65 and originate from the same experiment, meaning that use of the same controls is justified. Although the BMC Genomics paper was referenced and discussed, the authors should have stated in the legend for Fig. 1 that these control blots were reproduced from their earlier paper. The corrected and original legends are shown below and the online full-text and PDF versions of the paper have been updated.