Histone acetyltransferase KAT8 (KAT8)

Histone acetyltransferase KAT8 (KAT8), also known as MOF or MYST1, is a highly conserved enzyme of the MYST family, primarily responsible for acetylating histone H4 at lysine 16 (H4K16), a key epigenetic mark that regulates chromatin structure and gene accessibility[1][2][4][7]. KAT8 acts as part of the multiprotein MSL and NSL complexes, which target chromatin to modify transcription of essential and developmental genes[2][3]. Its function is critical for maintaining genomic stability, cell identity, cell cycle regulation, and proper DNA repair, as well as modulating antiviral and inflammatory responses by acetylating non-histone proteins[1][2][4][6]. Genetic variation or abnormal activity of KAT8 is implicated in cancer, infertility, immune, and neurological diseases, and KAT8 is widely considered a potential therapeutic target, though drug development is still preclinical[1][5][6][7].

Other names

MOFMYST1hMOFZC2HC8Protein acetyltransferase KAT8Protein propionyltransferase KAT8Males-absent on the first protein homologLysine acetyltransferase 8Histone acetyltransferase MYST1Probable histone acetyltransferase MYST1

Inhibition of acetyltransferase activity (e.g., MG149 inhibits KAT8, reducing acetylation of histone and non-histone substrates) Modulation of chromatin structure (compounds affecting KAT8 modify histone acetylation, affecting gene expression) Altered immune signaling (modulation of IRF3 acetylation impacts antiviral responses) Potential restoration of DNA damage repair (experimental approaches focus on KAT8’s role in double-strand break repair)