title: Negative regulation of interferon-induced transmembrane protein 3 by SET7-mediated lysine monomethylation.
abstract: 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 and influenza A virus 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.
authors.affiliation: From the Units of Molecular Immunology.
authors.forename: Zhao
authors.initials: Z
authors.lastname: Shan
authors.forename: Qinglin
authors.initials: Q
authors.lastname: Han
authors.forename: Jia
authors.initials: J
authors.lastname: Nie
authors.forename: Xuezhi
authors.initials: X
authors.lastname: Cao
authors.forename: Zuojia
authors.initials: Z
authors.lastname: Chen
authors.forename: Shuying
authors.initials: S
authors.lastname: Yin
authors.forename: Yayi
authors.initials: Y
authors.lastname: Gao
authors.forename: Fang
authors.initials: F
authors.lastname: Lin
authors.forename: Xiaohui
authors.initials: X
authors.lastname: Zhou
authors.forename: Ke
authors.initials: K
authors.lastname: Xu
authors.forename: Huimin
authors.initials: H
authors.lastname: Fan
authors.forename: Zhikang
authors.initials: Z
authors.lastname: Qian
authors.forename: Bing
authors.initials: B
authors.lastname: Sun
authors.forename: Jin
authors.initials: J
authors.lastname: Zhong
authors.forename: Bin
authors.initials: B
authors.lastname: Li
authors.forename: Andy
authors.initials: A
authors.lastname: Tsun
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D055785:Gene Knockdown Techniques; D057809:HEK293 Cells; D011495:Histone-Lysine N-Methyltransferase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009980:Influenza A virus / Q000276:immunology / Q000472:pathogenicity; D007370:Interferon Type I / Q000378:metabolism; D008239:Lysine / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008745:Methylation; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D014709:Vero Cells; D018116:Vesiculovirus / Q000276:immunology / Q000472:pathogenicity; D014777:Virus Diseases / Q000276:immunology / Q000378:metabolism / Q000517:prevention & control
chemical_list: C080082:IFITM3 protein, human; D007370:Interferon Type I; D008565:Membrane Proteins; D016601:RNA-Binding Proteins; D011495:Histone-Lysine N-Methyltransferase; C540312:SETD7 protein, human; D008239:Lysine
keywords: Antiviral Agents; Antiviral Host Restriction Factors; Host Defense; Host-pathogen Interactions; IFITM3; Lysine Methylation; Post-translational Modification; Protein Methylation; SET7