PRMT1

Protein arginine methyltransferase 1 (PRMT1) is the primary type I PRMT responsible for asymmetric dimethylation of arginine residues on histone and non-histone proteins^[1][2]. Mechanistically, PRMT1 regulates gene transcription, RNA processing, DNA replication, and signal transduction pathways critical for cell proliferation and survival^[3][2]. PRMT1 activity influences type I interferon signaling and modulates anti-tumor immunity, particularly in lung adenocarcinoma, affecting proliferation, migration, and invasion^[4]. In disease models, PRMT1 dysregulation contributes to persistence of cancer cells under EGFR- and KRAS-targeted therapies, with knockdown enhancing drug efficacy and prolonging tumor regression in xenografts^[5]. Compared with related isoforms, PRMT1 exhibits distinct substrate specificity and nuclear localization, unlike PRMT3 which is primarily cytoplasmic, or PRMT8 which has brain-specific expression^[6][7]. Functionally, PRMT1 shows sensitivity to ionic strength, temperature, and pH, allowing regulation under cellular stress conditions^[2]. Experimental applications have demonstrated that inhibition of PRMT1, alone or combined with PRMT5 blockade, sensitizes cancer cells to DNA damage and PARP inhibitors, highlighting its therapeutic potential^[8][9]. Collectively, PRMT1 is a key epigenetic regulator, distinct from other PRMT isoforms, and serves as a critical target in cancer biology and therapeutic design^[10][5].