The Crosstalk between Acetylation and Phosphorylation: Emerging New Roles for HDAC Inhibitors in the Heart

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Authors

Habibian, Justine S.
Ferguson, Bradley S.

Issue Date

2019

Type

Article

Language

en_US

Keywords

HDACs , histone deacetylases , PTMs , post-translational modifications , acetylation , lysine acetylation , heart failure , cardiac dysfunction

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Abstract

Approximately five million United States (U.S.) adults are diagnosed with heart failure (HF), with eight million U.S. adults projected to suffer from HF by 2030. With five-year mortality rates following HF diagnosis approximating 50%, novel therapeutic treatments are needed for HF patients. Pre-clinical animal models of HF have highlighted histone deacetylase (HDAC) inhibitors as efficacious therapeutics that can stop and potentially reverse cardiac remodeling and dysfunction linked with HF development. HDACs remove acetyl groups from nucleosomal histones, altering DNA-histone protein electrostatic interactions in the regulation of gene expression. However, HDACs also remove acetyl groups from non-histone proteins in various tissues. Changes in histone and non-histone protein acetylation plays a key role in protein structure and function that can alter other post translational modifications (PTMs), including protein phosphorylation. Protein phosphorylation is a well described PTM that is important for cardiac signal transduction, protein activity and gene expression, yet the functional role for acetylation-phosphorylation cross-talk in the myocardium remains less clear. This review will focus on the regulation and function for acetylation-phosphorylation cross-talk in the heart, with a focus on the role for HDACs and HDAC inhibitors as regulators of acetyl-phosphorylation cross-talk in the control of cardiac function.

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Citation

Habibian, J., & Ferguson, B. (2018). The Crosstalk between Acetylation and Phosphorylation: Emerging New Roles for HDAC Inhibitors in the Heart. International Journal of Molecular Sciences, 20(1), 102. doi:10.3390/ijms20010102

Publisher

International Journal of Molecular Sciences

License

Attribution 4.0 International

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URI

http://hdl.handle.net/11714/5802

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DOI

10.3390/ijms20010102

ISSN

1422-0067

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