PRMT1

PRMT1, or protein arginine N-methyltransferase 1, is a member of the protein arginine methyltransferase (PRMT) family that catalyzes the transfer of methyl groups to arginine residues on target proteins. It is a type I PRMT that generates asymmetric dimethylarginine (ADMA) from arginine, using S-adenosyl-L-methionine as the methyl donor.

PRMT1 methylates a broad spectrum of substrates, including histones such as histone H4 at arginine 3 (H4R3), contributing to the regulation of chromatin structure and transcription. It also methylates many non-histone proteins, including transcription factors and RNA-binding proteins such as p53, MBP (myelin basic protein), and FMRP, influencing processes from gene expression to signaling and RNA metabolism.

PRMT1 functions as a key regulator of gene expression, RNA processing, and signal transduction. It localizes to both nucleus and cytoplasm and is expressed broadly across tissues. Its activity is modulated by expression levels and post-translational modifications, and it can be inhibited by selective type I PRMT inhibitors such as MS023 and GSK3368715.

Increased or aberrant PRMT1 activity has been linked to multiple diseases, notably cancer, where it can promote transcriptional programs that support proliferation and survival. Because of its central role in epigenetic and post-transcriptional regulation, PRMT1 is studied as a potential therapeutic target, with inhibitors used in research to dissect its functions and assess therapeutic potential.