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Review
. 2016 Dec;1862(12):2221-2231.
doi: 10.1016/j.bbadis.2016.08.011. Epub 2016 Aug 17.

Mechanisms of transcription factor acetylation and consequences in hearts

Devi Thiagarajan  1 , Srinivasan Vedantham  2 , Radha Ananthakrishnan  1 , Ann Marie Schmidt  1 , Ravichandran Ramasamy  3
Affiliations
Review

Mechanisms of transcription factor acetylation and consequences in hearts

Devi Thiagarajan et al. Biochim Biophys Acta. 2016 Dec.

Abstract

Acetylation of proteins as a post-translational modification is gaining rapid acceptance as a cellular control mechanism on par with other protein modification mechanisms such as phosphorylation and ubiquitination. Through genetic manipulations and evolving proteomic technologies, identification and consequences of transcription factor acetylation is beginning to emerge. In this review, we summarize the field and discuss newly unfolding mechanisms and consequences of transcription factor acetylation in normal and stressed hearts. This article is part of a Special Issue entitled: The role of post-translational protein modifications on heart and vascular metabolism edited by Jason R.B. Dyck & Jan F.C. Glatz.

Keywords: Acetylation; Cardiovascular diseases; Heart; Histone acetyl transferases; Histone deacetylases; Transcription factors.

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Figures

Figure 1
Figure 1
Figure 1 illustrates the various histone acetyltransferases (top) and Zinc dependent and NAD+ dependent histone deacetylases and their subcellular localization in cells (bottom).
Figure 2
Figure 2
Figure 2 depicts an emerging mechanism of HDAC3 regulation in cells. This mechanism scheme adapted from [181] shows that polyol pathway enzyme aldose reductase (AR) competes with HDAC3 for corepressor complex binding leading to HDAC3 degradation and derepression of the PPARg and RAR pathways.
Figure 3
Figure 3
Figure 3 adapted from [74] depicts post-translational activation mechanism of HDAC2 that involves acetylation of HDAC2 mediated by p300/CBP-associated factor/HDAC5. Cardiac stress induces phosphorylation of HDAC5 and subsequent export to the cytoplasm. Casein kinase 2α1 (CK2α1) phosphorylates HDAC2, and p300/CBP-associated factor (pCAF) binds to HDAC2 and induces acetylation. “P’ indicates phosphorylation, “Ac” indicates acetylation.
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