Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2022 Aug 29;23(17):9790.
doi: 10.3390/ijms23179790.

Histone Deacetylases Function in the Control of Early Hematopoiesis and Erythropoiesis

Pascal Vong  1 , Hakim Ouled-Haddou  1 , Loïc Garçon  1   2   3
Affiliations
Review

Histone Deacetylases Function in the Control of Early Hematopoiesis and Erythropoiesis

Pascal Vong et al. Int J Mol Sci. .

Abstract

Numerous studies have highlighted the role of post-translational modifications in the regulation of cell proliferation, differentiation and death. Among these modifications, acetylation modifies the physicochemical properties of proteins and modulates their activity, stability, localization and affinity for partner proteins. Through the deacetylation of a wide variety of functional and structural, nuclear and cytoplasmic proteins, histone deacetylases (HDACs) modulate important cellular processes, including hematopoiesis, during which different HDACs, by controlling gene expression or by regulating non-histone protein functions, act sequentially to provide a fine regulation of the differentiation process both in early hematopoietic stem cells and in more mature progenitors. Considering that HDAC inhibitors represent promising targets in cancer treatment, it is necessary to decipher the role of HDACs during hematopoiesis which could be impacted by these therapies. This review will highlight the main mechanisms by which HDACs control the hematopoietic stem cell fate, particularly in the erythroid lineage.

Keywords: HDAC; erythropoiesis; hematopoiesis.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

References

    1. Allfrey V.G., Faulkner R., Mirsky A.E. Acetylation and Methylation of Histones and Their Possible role in the Regulation of RNA Synthesis. Proc. Natl. Acad. Sci. USA. 1964;51:786–794. doi: 10.1073/pnas.51.5.786. - DOI - PMC - PubMed
    1. Dowling D.P., Di Costanzo L., Gennadios H.A., Christianson D.W. Evolution of the arginase fold and functional diversity. Cell. Mol. Life Sci. 2008;65:2039–2055. doi: 10.1007/s00018-008-7554-z. - DOI - PMC - PubMed
    1. Eberharter A., Becker P.B. Histone acetylation: A switch between repressive and permissive chromatin. EMBO Rep. 2002;3:224–229. doi: 10.1093/embo-reports/kvf053. - DOI - PMC - PubMed
    1. Eberharter A., Ferreira R., Becker P. Dynamic chromatin: Concerted nucleosome remodelling and acetylation. Biol. Chem. 2005;386:745–747. doi: 10.1515/BC.2005.087. - DOI - PubMed
    1. Kuo M.H., Allis C.D. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays. 1998;20:615–626. doi: 10.1002/(SICI)1521-1878(199808)20:8<615::AID-BIES4>3.0.CO;2-H. - DOI - PubMed

MeSH terms

Substances

LinkOut - more resources