Lysine-specific histone demethylase 5B (KDM5B)

Lysine-specific histone demethylase 5B (KDM5B), also known as JARID1B or PLU-1, is a chromatin-modifying enzyme that specifically demethylates tri-, di-, and mono-methylated lysine 4 on histone H3 (H3K4) via an oxidative reaction requiring Fe²⁺ and α-ketoglutarate as cofactors[1][7][9]. KDM5B contains a catalytic jumonji C (JmjC) domain, an ARID DNA-binding domain, plant homeodomain fingers, and a zinc-finger motif, reflecting its multifaceted role in interpreting and modifying chromatin states[1][5]. By removing H3K4 methylation, KDM5B typically represses transcription and has essential roles in cell cycle progression, differentiation, and stem cell renewal. It is overexpressed in multiple cancers, where it contributes to tumor initiation, progression, invasion, and metastasis. Its status as an epigenetic modifier and emerging cancer target has led to the development of experimental inhibitors as potential anticancer agents[1][5][7][9].

Other names

JARID1BPLU-1histone demethylase JARID1Bhistone H3 lysine-4 demethylaseKDM5B

Inhibition of demethylase activity on H3K4me3/me2 marks leading to altered transcription and potential re-expression of tumor suppressor genes