PRMT3

PRMT3 (protein arginine methyltransferase 3) is a type I protein arginine methyltransferase that catalyzes asymmetric dimethylation of arginine residues and functions as a ribosomal protein methyltransferase involved in ribosome biogenesis and cellular protein synthesis regulation^[1][2]. Mechanistically, PRMT3 is distinguished within the PRMT family by the presence of a zinc-finger domain that mediates substrate interaction, enabling regulation of diverse proteins involved in transcriptional control, post-transcriptional regulation, translation, and metabolic signaling pathways^[3]. Through these activities, PRMT3 contributes to the control of gene expression and cellular metabolism, linking arginine methylation to fundamental biological processes^[3]. In disease contexts, accumulating evidence indicates that PRMT3 participates in oncogenic programs by promoting metabolic reprogramming and gene expression changes associated with tumorigenesis^[3]. Experimental studies further demonstrate that PRMT3 can influence cellular metabolism through regulation of glycolytic pathways and other metabolic processes relevant to cancer progression^[3]. Compared with related PRMT isoforms, PRMT3 exhibits distinct substrate recognition, subcellular functions, and regulatory mechanisms, highlighting its nonredundant biological role^[1][3]. For experimental applications, the allosteric inhibitor SGC707 provides a highly selective chemical probe for PRMT3, exhibiting nanomolar potency and substantial selectivity over other methyltransferases, thereby enabling mechanistic studies of PRMT3-dependent signaling and metabolic regulation^[4]. Pharmacological inhibition of PRMT3 has also shown effects on hepatic triglyceride metabolism in preclinical models, supporting its utility for pathway interrogation and therapeutic target validation studies^[5].