Acetylation of nuclear receptors in health and disease: an update

Anthony W. Ashton, Harpreet K. Dhanjal, Benjamin Rossner, Huma Mahmood, Vivek Patel, Mohammad Nadim, Manpreet Lota, Farhan Shahid, Zhiping Li, David Joyce, Matyas Pajkos, Zsuzsanna Dosztanyi, Xuanmao Jiao, Richard G. Pestell

Research output: Contribution to journalReview articlepeer-review

4 Citations (Scopus)


Lysine acetylation is a common reversible post-translational modification of proteins that plays a key role in regulating gene expression. Nuclear receptors (NRs) include ligand-inducible transcription factors and orphan receptors for which the ligand is undetermined, which together regulate the expression of genes involved in development, metabolism, homeostasis, reproduction and human diseases including cancer. Since the original finding that the ER alpha, AR and HNF4 are acetylated, we now understand that the vast majority of NRs are acetylated and that this modification has profound effects on NR function. Acetylation sites are often conserved and involve both ordered and disordered regions of NRs. The acetylated residues function as part of an intramolecular signalling platform intersecting phosphorylation, methylation and other modifications. Acetylation of NR has been shown to impact recruitment into chromatin, co-repressor and coactivator complex formation, sensitivity and specificity of regulation by ligand and ligand antagonists, DNA binding, subcellular distribution and transcriptional activity. A growing body of evidence in mice indicates a vital role for NR acetylation in metabolism. Additionally, mutations of the NR acetylation site occur in human disease. This review focuses on the role of NR acetylation in coordinating signalling in normal physiology and disease.

Original languageEnglish
Pages (from-to)217-236
Number of pages20
JournalFEBS Journal
Issue number2
Early online date19 Dec 2022
Publication statusPublished - Jan 2024


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