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Protein arginine methyltransferase 8 (PRMT8) is a type I enzyme of the PRMT family, distinguished by its exclusive expression in the central nervous system and its dual catalytic activities—protein arginine methylation and phospholipase activity. PRMT8 anchors to the plasma membrane via a unique N-terminal myristoylation motif and regulates key neuronal processes such as dendritic growth, synapse maturation, and synaptic plasticity. In addition to these neural functions, PRMT8 has roles in embryonic stem cell pluripotency, PI3K/AKT signaling, and possibly lipid metabolism and cancer progression. Altered PRMT8 expression is linked to neurological diseases, glioblastoma, and may contribute to disease outside the brain via mutations or dysregulation. Structural studies show PRMT8 can form oligomeric assemblies, and while it shares similarities with PRMT1, its tissue localization and dual enzymatic functions set it apart within the PRMT family[1][2][3].
Experimental allosteric inhibition (the “hinge region” conformation described in structural studies may offer a future target for inhibitors, but none are currently available[2])
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