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WIZ zinc finger protein (WIZ) is a chromatin-associated factor characterized by its widely interspaced C2H2-type zinc finger motifs. WIZ forms a complex with the histone methyltransferases G9a (EHMT2) and GLP (EHMT1), where it is critical for the recruitment and stabilization of these enzymes on chromatin, thus facilitating mono- and di-methylation of histone H3 at lysine 9 (H3K9me1/me2). It possesses DNA sequence-specific binding activity and functions as a transcriptional corepressor, potentially bridging the G9a/GLP complex to the CTBP corepressor machinery. WIZ is involved in the positive regulation of cell cycle DNA replication and protein stabilization and has been identified as a biomarker in atherosclerosis and is linked to rare developmental diseases such as giant axonal neuropathy 2 and bladder exstrophy. Currently, WIZ is not regarded as a classical therapeutic target (such as a receptor, transporter, enzyme, or channel), and no direct small molecule drugs targeting WIZ have been reported.
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