Protein arginine N-methyltransferase 7 (PRMT7)

Protein arginine N-methyltransferase 7 (PRMT7) is a unique member of the PRMT family, primarily recognized as a Type III methyltransferase that catalyzes the formation of monomethylarginine (MMA) on various substrates. It plays a pivotal role in epigenetic regulation by methylating histones, such as H4 and H2B, and non-histone proteins like HSP70 and Sm proteins. These modifications influence critical cellular processes, including gene transcription, RNA splicing, DNA damage repair, and the maintenance of stem cell pluripotency. In the context of human disease, PRMT7 is frequently overexpressed in several malignancies, including breast, lung, and gastric cancers, where it promotes epithelial-mesenchymal transition (EMT), invasion, and metastasis. Conversely, biallelic loss-of-function mutations in PRMT7 lead to a rare syndromic neurodevelopmental disorder characterized by short stature, intellectual disability, and obesity (SBIDDS). Therapeutic targeting of PRMT7 with small-molecule inhibitors, such as SGC3027, aims to disrupt its catalytic activity by competing with the methyl donor S-adenosylmethionine. Such inhibitors have shown potential in sensitizing cancer cells to chemotherapy and proteasomal stress, making PRMT7 an emerging target for precision oncology.

Other names

PRMT7FLJ10640SBIDDS[Myelin basic protein]-arginine N-methyltransferase PRMT7Histone-arginine N-methyltransferase PRMT7

SAM-competitive inhibition of protein arginine methyltransferase activity, preventing the transfer of methyl groups to arginine residues on histone and non-histone substrates.