Histone deacetylase 1, 2, 3, and 8 (HDAC1, HDAC2, HDAC3, HDAC8)

Histone deacetylases 1, 2, 3, and 8 are zinc-dependent enzymes belonging to Class I histone deacetylases. They catalyze the removal of acetyl groups from the lysine residues on the N-terminal tails of core histones, leading to chromatin condensation and transcriptional repression. These enzymes play a pivotal role in the regulation of gene expression, epigenetic silencing, and cellular differentiation. Their dysregulation is implicated in various diseases, notably cancer, making them important targets for small-molecule inhibitors. In addition to histone substrates, Class I HDACs also deacetylate several non-histone proteins, influencing diverse cellular processes including cell cycle, apoptosis, and DNA repair.

Other names

For HDAC1: RPD3For HDAC1: GON-10For HDAC2: RPD3For HDAC2: YAF1For HDAC2: YAF2For HDAC3: SMAP45For HDAC3: SMAPFor HDAC8: null (HDAC8 is the standard name)HDAC family members may also be referred to as Class I histone deacetylases

Inhibition of histone deacetylase activity Induction of histone hyperacetylation Reactivation of silenced genes (including tumor suppressors) Promotion of cell cycle arrest and apoptosis in cancer cells Modulation of immune response