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Review
. 2014 Feb;6(1):139-50.
doi: 10.2217/epi.13.73.

HDAC4: mechanism of regulation and biological functions

Affiliations
Review

HDAC4: mechanism of regulation and biological functions

Zhengke Wang et al. Epigenomics. 2014 Feb.

Abstract

The acetylation and deacetylation of histones plays an important role in the regulation of gene transcriptions. Histone acetylation is mediated by histone acetyltransferase; the resulting modification in the structure of chromatin leads to nucleosomal relaxation and altered transcriptional activation. The reverse reaction is mediated by histone deacetylase (HDAC), which induces deacetylation, chromatin condensation and transcriptional repression. HDACs are divided into three distinct classes: I, II, and III, on the basis of size and sequence homology, as well as formation of distinct complexes. Among class II HDACs, HDAC4 is implicated in controlling gene expression important for diverse cellular functions. Basic and clinical experimental evidence has established that HDAC4 performs a wide variety of functions. Understanding the biological significance of HDAC4 will not only provide new insight into the mechanisms of HDAC4 involved in mediating biological response, but also form a platform to develop a therapeutic strategy to achieve clinical implications.

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Conflict of interest statement

Conflict of interest

None

Figures

Figure 1
Figure 1. microRNAs target sites localized in the 3′UTR of HDAC4
Schematic representation of microRNAs target sites localized in the 4.5kb 3′UTR of HDAC4.
Figure 2
Figure 2. Domain organization and known post-translational modifications of HDAC4
Schematic representation of HDAC4 is shown below. The total number of amino ac id residues (aa) is depicted on the left, and the deacetylase domains are highlighted in gray. Phosphorylated (P), Sumoylated residues (S) and acetylated (A) residues are marked with a circle. Polyubiquitylation (U) is illustrated by multiple hexagons. The positions of modified amino acids are indicated next to each modification. Post-translational modifications that were detected without identification of the exact position are shown on the right and are marked by !?. NLS: nuclear localization

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