Acetylation of C/EBPα inhibits its granulopoietic function

Deepak Bararia (), Hui Si Kwok, Robert S. Welner, Akihiko Numata, Menyhárt B. Sárosi, Henry Yang, Sheena Wee, Sebastian Tschuri, Debleena Ray, Oliver Weigert, Elena Levantini, Alexander K. Ebralidze, Jayantha Gunaratne and Daniel G. Tenen ()
Additional contact information
Deepak Bararia: Cancer Science Institute, National University of Singapore
Hui Si Kwok: Cancer Science Institute, National University of Singapore
Robert S. Welner: Harvard Stem Cell Institute, Harvard Medical School
Akihiko Numata: Cancer Science Institute, National University of Singapore
Menyhárt B. Sárosi: Institute of Inorganic Chemistry, Faculty of Chemistry and Mineralogy, Universität Leipzig
Henry Yang: Cancer Science Institute, National University of Singapore
Sheena Wee: Translational Biomedical Proteomics Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research
Sebastian Tschuri: University Hospital of the Ludwig-Maximilians-University Munich
Debleena Ray: Program in Cancer and Stem Cell Biology, Duke-NUS Graduate Medical School
Oliver Weigert: University Hospital of the Ludwig-Maximilians-University Munich
Elena Levantini: Dana Farber/Harvard Cancer Center
Alexander K. Ebralidze: Dana Farber/Harvard Cancer Center
Jayantha Gunaratne: Translational Biomedical Proteomics Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research
Daniel G. Tenen: Cancer Science Institute, National University of Singapore

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract CCAAT/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.

Date: 2016
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DOI: 10.1038/ncomms10968

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