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Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity

ABSTRACT: Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity

PROVIDER: PRJNA1205384 | ENA |

REPOSITORIES: ENA

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Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity

Project description:Interferon regulatory factor 3 (IRF3) is the key transcription factor in the type I IFN signaling pathway, whose activation is regulated by multiple posttranslational modifica_x0002_tions. 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, Smyd3-deficient mice are more resistant to RNA and DNA viral infections. Zebrafish lacking smyd3 or treated with the inhibitor BCI121 are also more resistant to viral infection. Our findings reveal a role for SMYD3 in the regulation of antiviral innate immunity and provide insight into a unique modulation of IRF3 that affects its activation.

2025-01-01 | GSE285658 | GEO

Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity [II]

2025-01-03 | GSE285750 | GEO

Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity [II]

Project description:Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity [II]

| PRJNA1205763 | ENA

Identification of IRF3 methylation site catalyzed by SMYD3

Project description:Identification of IRF3 methylation site catalyzed by SMYD3

2025-01-02 | PXD059397 |

NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming

Project description:This SuperSeries is composed of the following subset Series: GSE29146: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [ChIP] GSE29147: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [RNAi] GSE29148: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [TKO] GSE29150: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [Transduction] Refer to individual Series

2011-11-29 | E-GEOD-29305 | biostudies-arrayexpress

Histone H3 lysine 9 dimethylation of miRNA genes in HMEC and HMF

Project description:Normal cell type specific histone H3 lysine 9 dimethylation of miRNA genes. HMEC and HMF represent two distinct differentiated cell type present in mammary gland each with a distinct phenotype, a distinct epigenotype as well as distinct miRNA expression pattern. The aim of the study was to determine how epigenetic modifications including histone H3 lysine 9 dimethylation affect miRNA expression. Two cell types HMEC vs. HMF. Biological replicates: 3 pairs of HMEC-HMF of 3 distinct genotypes. Immunoprecipitation using anti-histone H3 dimethylated at lysine 9 (CS200587, Millipore).

2011-04-05 | E-GEOD-28378 | biostudies-arrayexpress

Histone H3 lysine 9 dimethylation of miRNA genes in HMEC and HMF

2011-04-05 | GSE28378 | GEO

Effect of SMYD3 on MCF7 breast cancer cells (RNA-seq)

Project description:RNA-sequencing analysis of control and SMYD3-overexpressed MCF7 cell lines. SMYD3 (also known as KMT3E), a hisone H3 lysine K4 methyltransferase, is highly expressed in several human cancers, including colorectal and breast carcinomas. Results provide insight into the transcriptional regulation of SMYD3 in breast cancer.

2022-10-31 | GSE130169 | GEO

Histone 3 Lysine 9 Dimethylation Attenuates the Vascular Smooth Muscle Cell Inflammatory Response

Project description:Histone 3 Lysine 9 Dimethylation Attenuates the Vascular Smooth Muscle Cell Inflammatory Response

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AXIN1 boosts antiviral response through IRF3 stabilization and induced phase separation

Project description:Axis inhibition protein 1 (AXIN), a scaffold protein interacting with various critical molecules, plays a vital role in determining cell fate. However, its impact on the antiviral innate immune response remains largely unknown. Here, we identify AXIN acts as an effective regulator of antiviral innate immunity against both DNA and RNA virus infections. In the resting state, AXIN maintains the stability of IRF3 by preventing p62-mediated autophagic degradation of IRF3. This is achieved by recruiting ubiquitin-specific peptidase 35 (USP35), which removes lysine (K) 48-linked ubiquitination at IRF3 K366. Upon virus infection, AXIN undergoes a phase separation triggered by phosphorylated TBK1. This leads to increased phosphorylation of IRF3 and a boost in IFN-I production. Moreover, KYA1797K, a small molecule that binds to the AXIN RGS domain, enhances the AXIN-IRF3 interaction and promotes the elimination of various highly pathogenic viruses. Clinically, patients with HBV-associated hepatocellular carcinoma (HCC) who show reduced AXIN expression in pericarcinoma tissues have low overall and disease-free survival rates, as well as higher HBV levels in their blood. Overall, our findings reveal how AXIN regulates IRF3 signaling and phase separation-mediated antiviral immune responses, underscoring the potential of the AXIN agonist KYA1797K as an effective antiviral agent.

2024-10-31 | PXD055972 | Pride

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