西亚试剂：Negative Regulation of Interferon-Induced Transmembrane

Zhao Shan1， Qinglin Han1， Jia Nie1， Xuezhi Cao1， Zuojia Chen1， Shuying Yin1， Yayi Gao1， Fang Lin1， Xiaohui Zhou2， Ke Xu1， Huimin Fan2， Zhikang Qian1， Bing Sun1， Jin Zhong1， Bin Li3* and Andy Tsun1

Although lysine methylation is classically known to regulate histone function， its role in modulating antiviral restriction factor activity remains uncharacterized. Interferon-induced transmembrane protein 3 (IFITM3) was found monomethylated on its lysine-88 residue (IFITM3-K88me1) to reduce its antiviral activity， mediated by the lysine methyltransferase SET7. Vesicular Stomatitis virus (VSV) and Influenza A virus (IAV) infection increased IFITM3-K88me1 levels by promoting the interaction between IFITM3 and SET7， suggesting that this pathway could be hijacked to support infection； conversely， IFN-α reduced IFITM3-K88me1 levels. These findings may have important implications in the design of therapeutics targeting protein methylation against infectious diseases.

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