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Histone acetyltransferase KAT6B (KAT6B) is an enzyme in the MYST family of lysine acetyltransferases that catalyzes the acetylation of lysine residues on histone proteins, particularly histone H3, thereby regulating gene activation and chromatin accessibility[1][2][3]. KAT6B forms stable complexes with other nuclear proteins, such as ING5, BRPF1, and KAT6A, and it plays a central role in the epigenetic control of gene expression during embryonic development, neurogenesis, and osteogenesis[2]. Germline loss-of-function or gain-of-function mutations in KAT6B are associated with rare congenital syndromes such as genitopatellar syndrome and the Say-Barber-Biesecker-Young-Simpson variant of Ohdo syndrome, characterized by skeletal, neurological, and genital abnormalities[1][2]. Somatic chromosomal rearrangements involving KAT6B are linked to acute myeloid leukemia, therapy-related myelodysplastic syndrome, and uterine leiomyoma, suggesting a role in tumorigenesis through dysregulation of histone acetylation and gene control[1][2]. No established drugs directly target KAT6B in the clinic, but it remains a putative therapeutic target in oncology and developmental disorders due to its critical role in chromatin modification and gene regulation.
Inhibition of KAT6B enzyme activity (for investigational agents); Disruption of histone acetylation and epigenetic gene regulation
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