Lysine-specific demethylase 2A (KDM2A)

Lysine-specific demethylase 2A (KDM2A) is a Jumonji C (JmjC) domain-containing enzyme that demethylates mono- and dimethylated lysine 36 on histone H3 (H3K36me1/2)[1][2][4]. It also contains F-box and leucine-rich repeat motifs, and forms part of SCF (SKP1-cullin-F-box) ubiquitin-ligase complexes that regulate protein stability. KDM2A is a key epigenetic regulator, involved in chromatin remodeling, gene transcription, cell proliferation, and differentiation[1][2]. It is essential for maintaining heterochromatin stability, DNA damage repair, and proper gene expression. Dysregulation of KDM2A contributes to tumorigenesis and cancer progression, particularly in breast and lung cancers, by promoting stemness and angiogenesis[6][5]. KDM2A has been proposed as a prognostic biomarker and a potential therapeutic target, but its broad role in chromatin biology highlights the need for caution in targeting it pharmacologically.

Other names

F-box and leucine-rich repeat protein 11 (FBXL11)Histone lysine demethylase KDM2AKDM2A

Demethylation of histone H3 at lysine 36 (H3K36), leading to regulation of gene transcription[1][2][4]. Modulation of chromatin accessibility and structure. Interaction with ubiquitin-ligase complexes (SCF), promoting ubiquitination and degradation of target proteins[2][1].