Histone deacetylase 1, Histone deacetylase 2, Histone deacetylase 3, and Histone deacetylase 10 (HDAC1, HDAC2, HDAC3, HDAC10)

Histone deacetylase 1, 2, and 3 (class I) and Histone deacetylase 10 (class IIb) are zinc-dependent enzymes that remove acetyl groups from histone and non-histone proteins, leading to chromatin condensation and transcriptional repression[2][3][4][7]. Class I HDACs (HDAC1, HDAC2, HDAC3) are primarily nuclear, forming large multiprotein complexes critical for gene silencing and supporting cell proliferation, differentiation, and survival[2][4]. HDAC10, classified as class IIb, has a structural domain similar to class I HDACs but also possesses unique functions in polyamine deacetylation and cytoplasmic-nuclear shuttling[3][6]. Dysfunction or overexpression of these enzymes is strongly associated with cancer and other diseases, making them validated therapeutic targets. Pharmacological inhibitors of these HDACs are approved or in development for various cancers and are being explored in other disease contexts due to their capacity to reactivate silenced genes and alter disease-relevant epigenetic states[3][5][9].

Other names

HDAC1HDAC2HDAC3HDAC10Histone deacetylase class I (for HDAC1, HDAC2, HDAC3)Histone deacetylase class IIb (for HDAC10)Lysine deacetylase 1/2/3/10 (less common)

Inhibition of deacetylation activity, leading to hyperacetylation of histones and non-histone proteins; Reactivation of silenced tumor suppressor genes; Cell cycle arrest; Induction of apoptosis in cancer cells; Modulation of inflammatory gene expression