Histone deacetylase 1 (HDAC1) and Histone deacetylase 2 (HDAC2) (HDAC1; HDAC2)

Histone deacetylase 1 and histone deacetylase 2 are closely related nuclear enzymes that remove acetyl groups from lysine residues on histone tails, leading to chromatin condensation and transcriptional repression. They serve as the catalytic core of numerous transcriptional co-repressor complexes, including the CoREST and NuRD complexes, and regulate gene expression, cell cycle, apoptosis, and differentiation. These enzymes also act on non-histone proteins, impacting a broad set of cellular functions. Aberrant expression or activity of HDAC1/2 is implicated in cancers, neurodegenerative diseases, and inflammatory conditions. Several HDAC inhibitors have been developed as cancer therapeutics, targeting the zinc-dependent catalytic domain of HDAC1/2, although specificity and safety remain clinical challenges. Expression levels and activity of these enzymes serve as biomarkers for some diseases and influence patient response to therapy.

Other names

HDAC1 (Histone deacetylase 1)HDAC2 (Histone deacetylase 2)Rpd3-like protein (by homology to yeast)EC 3.5.1.98 (Enzyme Commission number for HDACs)Part of CoREST complex (HDAC1/CoREST1/LSD1)

Inhibition of deacetylase activity, resulting in increased acetylation of histones and non-histone proteins. Promotion of chromatin relaxation and transcriptional activation. Induction of cell cycle arrest and apoptosis in cancer cells. Modulation of gene expression patterns.