VIRMA (vir like m6A methyltransferase associated) functions as a critical component and the largest structural unit of the m6A methyltransferase complex 1, mediating N6-methyladenosine (m6A) modification of cellular RNAs. As a "writer" in the m6A regulatory system, VIRMA recruits catalytic components METTL3 and METTL14 to guide m6A methylation at specific sites in the 3'-UTR near stop codons, thereby regulating mRNA splicing, processing, and polyadenylation 2. VIRMA is essential for active ribosome biogenesis and protein synthesis adaptation; its depletion impairs ribosomal RNA stability and triggers p53-dependent stress responses 3. Dysregulation of VIRMA promotes multiple cancer types through m6A-dependent mechanisms. VIRMA is upregulated in breast cancer, hepatocellular carcinoma, and intrahepatic cholangiocarcinoma, where elevated expression correlates with poor survival 14. In breast cancer, VIRMA interacts with m6A reader IGF2BP3 to stabilize HAS2 mRNA, promoting cell proliferation and migration 4. In cholangiocarcinoma, VIRMA stabilizes TMED2 and PARD3B mRNAs through m6A modification, activating oncogenic Akt/GSK/β-catenin and MEK/ERK/Slug pathways 5. These mechanisms underscore VIRMA's dual role in normal development and cancer pathogenesis, suggesting therapeutic potential for targeting this m6A modification pathway.