Publication:

Acetylation of C/EBPα inhibits its granulopoietic function

Thumbnail Image

Open/View Files

4814574.pdf (1.34 MB)

Date

2016

Authors

Published Version

10.1038/ncomms10968

Journal Title

Journal ISSN

Volume Title

Publisher

Nature Publishing Group
The Harvard community has made this article openly available. Please share how this access benefits you.

Research Projects

Organizational Units

Journal Issue

Citation

Bararia, 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.

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.

Description

Other Available Sources

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4814574/pdf/

Research Data

Keywords

Terms of Use

This article is made available under the terms and conditions applicable to Other Posted Material (LAA), as set forth at Terms of Service

URI

http://nrs.harvard.edu/urn-3:HUL.InstRepos:29407765

Collections

HMS Scholarly Articles

Endorsement

Review

Supplemented By

Related Stories