Class I and IV Histone Deacetylases (HDACs) (HDAC Class I and IV)

Class I and IV Histone Deacetylases (HDACs) are a subset of zinc-dependent enzymes that catalyze the removal of acetyl groups from lysine residues on both histone and non-histone proteins (UniProt). Class I HDACs, comprising HDAC1, 2, 3, and 8, are predominantly located in the nucleus and are integral components of multi-protein transcriptional co-repressor complexes that regulate cell cycle progression and survival (PMID: 22421968). Class IV consists of a single member, HDAC11, which is the smallest HDAC and plays specialized roles in immune cell function and metabolic regulation (PMID: 28233118). In many pathological states, particularly oncology, these enzymes are overexpressed or aberrantly recruited, leading to the epigenetic silencing of tumor suppressor genes and promoting tumorigenesis (PubMed). Therapeutic targeting of these HDACs with small molecule inhibitors, such as Vorinostat and Romidepsin, has proven effective in treating certain hematological malignancies (NIH). Ongoing research also explores their potential in treating solid tumors, neurodegenerative conditions, and inflammatory diseases by modulating gene expression patterns and cellular signaling pathways (PubMed).

Other names

Histone deacetylase Class IHistone deacetylase Class IVHistone deacetylase 1Histone deacetylase 2Histone deacetylase 3Histone deacetylase 8Histone deacetylase 11Zinc-dependent histone deacetylases (UniProt)RPD3-like histone deacetylases (PubMed)

Inhibition of the catalytic activity of zinc-dependent histone deacetylases, resulting in hyperacetylation of histones and non-histone proteins, which promotes an open chromatin configuration and modulates the transcription of genes involved in cell cycle arrest and apoptosis (PMID: 22421968, NIH).