Bararia, DeepakKwok, Hui SiWelner, Robert S.Numata, AkihikoSárosi, Menyhárt B.Yang, HenryWee, SheenaTschuri, SebastianRay, DebleenaWeigert, OliverLevantini, ElenaEbralidze, AlexanderGunaratne, JayanthaTenen, Daniel2016-11-182016Bararia, D., H. S. Kwok, R. S. Welner, A. Numata, M. B. Sárosi, H. Yang, S. Wee, et al. 2016. “Acetylation of C/EBPα inhibits its granulopoietic function.” Nature Communications 7 (1): 10968. doi:10.1038/ncomms10968. http://dx.doi.org/10.1038/ncomms10968.2041-1723http://nrs.harvard.edu/urn-3:HUL.InstRepos:29407765CCAAT/enhancer-binding protein alpha (C/EBPα) is an essential transcription factor for myeloid lineage commitment. Here we demonstrate that acetylation of C/EBPα at lysine residues K298 and K302, mediated at least in part by general control non-derepressible 5 (GCN5), impairs C/EBPα DNA-binding ability and modulates C/EBPα transcriptional activity. Acetylated C/EBPα is enriched in human myeloid leukaemia cell lines and acute myeloid leukaemia (AML) samples, and downregulated upon granulocyte-colony stimulating factor (G-CSF)- mediated granulocytic differentiation of 32Dcl3 cells. C/EBPα mutants that mimic acetylation failed to induce granulocytic differentiation in C/EBPα-dependent assays, in both cell lines and in primary hematopoietic cells. Our data uncover GCN5 as a negative regulator of C/EBPα and demonstrate the importance of C/EBPα acetylation in myeloid differentiation.en-USJournal Article2016-11-1810.1038/ncomms10968