PRMT8 is a membrane-associated protein arginine methyltransferase that catalyzes the formation of monomethylarginine and asymmetric dimethylarginine in various protein substrates 1234. The enzyme demonstrates neuron-specific expression and plays critical roles in neuronal development and function 56. PRMT8 regulates dendritic spine maturation through methylation of G3BP1 and suppression of Rac1-PAK1 signaling to control synaptic actin dynamics 6. In Purkinje cells, PRMT8 functions as both an arginine methyltransferase and phospholipase, directly hydrolyzing phosphatidylcholine to generate choline and phosphatidic acid, which is essential for proper dendritic arborization and motor coordination 7. The protein also maintains pluripotency in human embryonic stem cells by enhancing PI3K/AKT/SOX2 signaling through direct interaction with the PI3K regulatory subunit p85 8. Additionally, PRMT8 serves as a transcriptional coactivator of retinoid signaling during neuronal differentiation 5. Dysregulation of PRMT8 is implicated in various cancers, with expression levels correlating with patient survival outcomes in breast, ovarian, and gastric cancers 9. Loss of PRMT8 expression is notably observed in glioblastoma tissues 5.