PRMT1, protein arginine methyltransferase 1, is the major protein arginine methyltransferase in mammals. It catalyzes monomethylation and asymmetric dimethylation of arginine side chains in proteins, playing essential roles in numerous biological processes. Initially recognized for regulating chromatin dynamics via histone H4 arginine 3 (H4R3) methylation, it is now known to be involved in transcriptional regulation, signal transduction, DNA repair, and more [1].

In pancreatic cancer, deletion of PRMT1 in a KRAS-dependent mouse model delays cancer development. Multi-omics analyses show that PRMT1 depletion leads to global changes in chromatin accessibility and transcription, reducing glycolysis and tumorigenic capacity [3]. In hepatocellular carcinoma, FBXO7, an E3 ubiquitin ligase, binds PRMT1, induces its ubiquitination, and promotes proteosomal degradation, thus inhibiting serine synthesis and tumor growth [2]. In glioma, diminished PRMT1 expression in IDH1R132H gliomas is associated with reduced PTX3 levels, affecting ferritinophagy [4]. In colorectal cancer, PRMT1-mediated H4R3me2a recruits SMARCA4 to promote cancer progression by enhancing EGFR signaling, and knockdown or inhibition of PRMT1 attenuates tumor growth in a CRC mouse model [5].

In conclusion, PRMT1 is crucial for various biological functions including chromatin regulation, cell metabolism, and signal transduction. Studies using gene knockout and conditional knockout mouse models have revealed its significant roles in cancer development, such as in pancreatic, hepatocellular, glioma, and colorectal cancers, highlighting its potential as a therapeutic target in these disease areas.