PRMT1 is a protein arginine methyltransferase that catalyzes mono- and asymmetric dimethylation of arginine residues on target proteins, functioning primarily as an epigenetic regulator 1. Its primary function involves methylating histone H4 at arginine 3 (H4R3me1/me2a), a mark associated with transcriptional activation, while also modifying diverse substrates including transcription factors, RNA-binding proteins, and metabolic enzymes 1. Mechanistically, PRMT1 regulates multiple cellular pathways. It methylates PHGDH to enhance serine synthesis in hepatocellular carcinoma 2, methylates PGK1 to promote glycolysis in colorectal cancer 3, and methylates PTX3 to regulate ferritinophagy in glioma 4. PRMT1 expression is tightly controlled; the E3 ubiquitin ligase FBXO7 promotes PRMT1 degradation to suppress serine synthesis in hepatocellular carcinoma 5. Dysregulated PRMT1 expression significantly impacts cancer development and progression. PRMT1 is highly upregulated in pancreatic cancer, where it promotes glycolysis and tumorigenesis; deletion impairs cancer development in KRAS-dependent models 6. PRMT1 inhibition synergizes with gemcitabine against pancreatic tumors 6. In gastric cancer, PRMT1 acts within the PRMT1/BTG2 axis 7, while LPCAT2 suppresses colorectal cancer by inhibiting PRMT1 nuclear localization and downstream SLC7A11 expression 8. These findings establish PRMT1 as a promising therapeutic target across multiple cancer types.