Protein arginine N-methyltransferase 5 (PRMT5)

Protein arginine N-methyltransferase 5 (PRMT5) is a highly conserved enzyme encoded by the PRMT5 gene. It belongs to the type II protein arginine methyltransferase family and catalyzes the symmetric dimethylation of arginine residues on various protein substrates, including histones and transcription factors. PRMT5 has a characteristic TIM barrel domain and is found in both the cytoplasm and nucleus, with dynamic translocation. Its activity is crucial for numerous biological processes including epigenetic regulation, transcription, cell cycle control, DNA damage response, RNA splicing, and cellular development/differentiation. PRMT5's activity is regulated by protein-protein interactions with adaptor proteins (e.g., CLNS1A, RIOK1, COPR5), complex formation (especially with MEP50), phosphorylation, and C-terminal interactions. Due to its overexpression and critical roles in cancer and other diseases, PRMT5 is considered an important therapeutic target, with strategies including direct enzymatic inhibitors and PPI inhibitors.

Inhibiting the enzyme's symmetric dimethylation activity or blocking its interaction with adaptor proteins like MEP50.