Histone deacetylase 3 (HDAC3) (HDAC3)

Histone deacetylase 3 (HDAC3) is a Class I enzyme that plays a pivotal role in the epigenetic regulation of gene expression by removing acetyl groups from lysine residues on histones and various non-histone proteins (UniProt O15379). It is unique among Class I HDACs because its enzymatic activity is strictly dependent on its association with the NCoR (nuclear receptor corepressor) and SMRT (silencing mediator for retinoid and thyroid receptors) complexes, as well as the presence of the signaling molecule inositol tetraphosphate (Lahm et al., 2007). HDAC3 is involved in a wide array of biological processes, including cell cycle progression, apoptosis, and metabolic regulation, particularly in the liver and heart (Sun et al., 2013). Dysregulation or overexpression of HDAC3 is frequently observed in various malignancies, where it contributes to the silencing of tumor suppressor genes and promotes oncogenic pathways (NCBI Gene 8841). Sodium butyrate is a short-chain fatty acid that acts as a non-selective inhibitor of HDAC3 and other Class I and II HDACs, and it is often used in research to study the effects of histone hyperacetylation on cell differentiation and growth arrest (PubChem CID 522249). Therapeutic targeting of HDAC3 aims to reverse aberrant epigenetic silencing, though achieving isoform selectivity remains a significant challenge in drug development.

Other names

HD3RPD3-2SMAP45Histone deacetylase 3

HDAC3 catalyzes the deacetylation of lysine residues on histone tails (H3 and H4) and non-histone proteins, facilitating a condensed chromatin state that generally represses transcription (UniProt O15379).