Histone-arginine methyltransferase METTL23 (METTL23)

Histone-arginine methyltransferase METTL23 is an epigenetic enzyme that specifically catalyzes the asymmetric dimethylation of arginine 17 on histone H3, forming the H3R17me2a mark[1][2][6]. This posttranslational modification is crucial for chromatin remodeling and transcriptional activation of certain estrogen receptor α target genes that are vital for the homeostasis of neuronal cells, especially retinal ganglion cells[1][3]. Loss-of-function mutations in METTL23 cause aberrant splicing, reduce enzymatic activity, and are etiologically linked to normal-tension glaucoma, with evidence for autosomal dominant inheritance[1][3]. METTL23’s methylation activity also plays a regulatory role in inflammatory signaling via NF-κB and the transcription of TNF-α and IL-1β[1]. Variants have additionally been associated with familial intellectual disabilities, suggesting broader implications for nervous system disorders[5]. No specific drugs targeting METTL23 are currently identified, and H3R17me2a status or METTL23 genotype could serve as potential biomarkers for disease risk or progression.

Other names

Methyltransferase-like protein 23C17orf95LOC124512MRT44spike binding protein 1METTL23probable methyltransferase-like protein 23