ArticleProceedings of the National Academy of Sciences of the United States of America2025
Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Predictive bioactivity modeling and structural binding analysis for the identification of potential SMYD3 modulators.Molecular diversity · 2026Article
- TANK potentiates antiviral innate immunity by recruiting deubiquitinase USP46 to activate IKKε.PLoS pathogens · 2026Article
- Multi-omics analysis reveals that glyceryl monooleate mitigates PEDV-induced intestinal injury in piglets.BMC microbiology · 2026Article
- Canonical and Non-Canonical Functions of Histone H3K4 Methylation Modifiers in Cancer.Cancer science · 2025Review
- T3SS effector EseJ in Edwardsiella piscicida inhibits PANoptosis in macrophages.Communications biology · 2025Article
- Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Authors and funding
9 authors.
Funding
Abstract
Interferon regulatory factor 3 (IRF3) is the key transcription factor in the type I IFN signaling pathway, whose activation is regulated by multiple posttranslational modifications. Here, we identify SMYD3, a lysine methyltransferase, as a negative regulator of IRF3. SMYD3 interacts with IRF3 and catalyzes the dimethylation of IRF3 at lysine 39. This modification reduces IRF3 phosphorylation, dimerization, and subsequent nuclear translocation, leading to the inhibition of downstream type I interferon production. In addition,
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