Protein arginine methyltransferase 7 (PRMT7)

Protein arginine methyltransferase 7 (PRMT7) is an evolutionarily conserved enzyme that catalyzes the mono-methylation of arginine residues on a variety of substrate proteins, including histones and select non-histone proteins such as eukaryotic translation initiation factor 2α (eIF2α). As the only known type III PRMT in mammals, PRMT7 plays key roles in epigenetic regulation, transcriptional control, RNA metabolism, and the cellular response to stress. PRMT7-driven substrate methylation is involved in gene expression, maintenance of cellular stemness, stress granule formation, muscle development, immune function, and nervous system development. Altered PRMT7 expression or function has been associated with cancer aggressiveness and metastasis, as well as neurodevelopmental and immune-related disorders. Pharmacological inhibition of PRMT7 has emerged as a promising therapeutic strategy in preclinical research, but the full extent of its biological and safety implications remains under investigation[1][2][3][4].

Other names

Protein arginine N-methyltransferase 7KIAA1933FLJ10640Histone-arginine N-methyltransferase PRMT7[Myelin basic protein]-arginine N-methyltransferase PRMT7SBIDDS

Inhibition of PRMT7 catalytic activity leads to altered arginine methylation on target proteins, affecting stress response, gene expression, and disease phenotypes[1][4]