Fig. 7
From: METTL3 drives NSCLC metastasis by enhancing CYP19A1 translation and oestrogen synthesis
METTL3 binds to CYP19A1 mRNA and interact with eIFs to regulates translation efficiency of CYP19A1. (A) Immunoprecipitation using anti-METTL3 followed by mass spectrometry analysis was performed to identify proteins that interact with METTL3. A total of 218 proteins were identified as specific binding proteins of METTL3, which are presented in a Venn diagram. GO analysis of the 218 proteins revealed enrichment in the translation initiation process. (B) Co-IP to confirm the interaction between METTL3 and translation initiation molecules identified by mass spectrometry, including eIF3e, eIF3i, and eIF4E. (C-D) RNA immunoprecipitation using anti-METTL3 antibody followed by qPCR validation showing direct binding of METTL3 to CYP19A1 mRNA in A549 and H1975 cells. Agarose gel electrophoresis of qPCR samples confirmed the enrichment of CYP19A1 mRNA in the anti-METTL3 group, confirming the binding between METTL3 and CYP19A1 mRNA. (E) Treatment with the eIF4E inhibitor 4EGI-1 significantly downregulated the protein expression of CYP19A1. (F) Administration of 4EGI-1 abolished the effect of METTL3 overexpression in promoting CYP19A1 expression