Positive Regulation of Interferon Regulatory Factor 3 Activation by Herc5 via ISG15 Modification

Shi, He; Yang, Kun; Liu, Xing; Liu, Xin Yi; Wei, Bo; Yu, Shan; Zhu, Lian Hui; Wang, Chen

doi:10.1128/mcb.01466-09

Cited by 233 publications

(206 citation statements)

References 59 publications

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“…This is also true for modification by other ubiquitin like proteins, such as SUMO. It has been reported that these minor ISGylated fractions have important physiological roles, such as tumor-suppressive effect through down-regulation of ⌬Np63␣ (46), inhibition of influenza A virus replication (47), sustained IRF3 activation (48), and prevention of JNK cascade (49). These reports support the significant physiological role of ISGylated PKR on the protein translation although ISGylated PKR is minor fraction.…”

Section: Discussionmentioning

confidence: 54%

Activation of Double-stranded RNA-activated Protein Kinase (PKR) by Interferon-stimulated Gene 15 (ISG15) Modification Down-regulates Protein Translation

Okumura

Uematsu

et al. 2013

Journal of Biological Chemistry

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Background: Double-stranded RNA-activated protein kinase (PKR) is activated by virus-derived RNA and inhibits protein translation. Results: PKR is covalently modified by interferon-stimulated gene 15 (ISG15), and ISG15-PKR fusion protein is active without virus RNA. Conclusion: PKR is able to be activated by ISG15 modification. Significance: PKR might be an anti-tumor molecule by inhibiting protein translation in ISG15-positive cancer cells.

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Section: Discussionmentioning

confidence: 54%

Activation of Double-stranded RNA-activated Protein Kinase (PKR) by Interferon-stimulated Gene 15 (ISG15) Modification Down-regulates Protein Translation

Okumura

Uematsu

et al. 2013

Journal of Biological Chemistry

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“…Then, culture media was replaced by serum-free DMEM, and SeV, vesicular stomatitis virus (VSV), influenza A virus (IAV), or Newcastle disease virus (NDV)-GFP was added to the media at a multiplicity of infection of 0.2-1 according to specific experiments. After 1 h, the medium was removed, and the cells were fed with DMEM containing 10% FBS (32,33). Human H1N1 IAV strain IAV-PR8/34 was kindly provided by Dr. Ze Chen (Wuhan Institute of Virology, Chinese Academy of Sciences).…”

Section: Virus Manipulationmentioning

confidence: 99%

IFN-Induced TPR Protein IFIT3 Potentiates Antiviral Signaling by Bridging MAVS and TBK1

Liu

Chen

Wei

et al. 2011

The Journal of Immunology

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156

140

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Intracellular RNA viruses are sensed by receptors retinoic acid-inducible gene I/MDA5, which trigger formation of the mitochondrial antiviral signaling (MAVS) complex on mitochondria. Consequently, this leads to the activation of TNFR-associated factor family member-associated NF-κB activator-binding kinase 1 (TBK1) and phosphorylation of IFN regulatory factor 3 (IRF3). It remains to be elucidated how MAVS activates TBK1/IRF3. In this study, we report that IFN-induced protein with tetratricopeptide repeats 3 (IFIT3) is significantly induced upon RNA virus infection. Ectopic expression or knockdown of IFIT3 could, respectively, enhance or impair IRF3-mediated gene expression. Mechanistically, the tetratrico-peptide repeat motif (E164/E165) of IFIT3 interacts with the N terminus (K38) of TBK1, thus bridging TBK1 to MAVS on the mitochondrion. Disruption of this interaction markedly attenuates the activation of TBK1 and IRF3. Furthermore, host antiviral responses are significantly boosted or crippled in the presence or absence of IFIT3. Collectively, our study characterizes IFIT3 as an important modulator in innate immunity, revealing a new function of the IFIT family proteins (IFN-induced protein with tetratricopeptide repeats).

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“…Indeed, a body of previous studies have demonstrated that different molecules and mechanisms have been employed for regulating the activation of IRF3. For example, IRF3, through Herc5-mediated ISG15 modification, can promote its self-activation (31). On the other hand, NIMA-interacting 1 (Pin 1), RNA transcriptional activator-associated ubiquitin ligase (RAUL), RBCC protein interacting with PKC1 (RBCK1), and forkhead box protein O1 (FoxO1) have been shown to mediate ubiquitin-dependent IRF3 degradation to impair production of IFN-Is (32)(33)(34)(35).…”

mentioning

confidence: 99%

A Novel Function of F-Box Protein FBXO17 in Negative Regulation of Type I IFN Signaling by Recruiting PP2A for IFN Regulatory Factor 3 Deactivation

Peng

Wang

Huang

et al. 2017

The Journal of Immunology

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The F-box proteins were originally identified as the key component of SKP1-Cullin1-F-box E3 ligase complexes that control the stability of their specific downstream substrates essential for cell growth and survival. However, the involvement of these proteins in type I IFN (IFN-I) signaling during innate immunity has not been investigated. In this study we report that the F-box protein FBXO17 negatively regulates IFN-I signaling triggered by double-strand DNA, RNA, or viral infection. We found that FBXO17 specifically interacts with IFN regulatory factor 3 (IRF3) and decreases its dimerization and nuclear translocation. The decrease of IRF3 dimerization and nuclear translocation is due to the recruitment of protein phosphatase 2 (PP2A) mediated by FBXO17, resulting in IRF3 dephosphorylation. Interestingly, PP2A recruitment does not require the F-box domain but instead the F-box associated region of the protein; thus, the recruitment is independent of the canonical function of the SKP1-Cullin1-F-box family of E3 ligase. Together, our studies identify a previously unreported role of FBXO17 in regulating IFN-I signaling and further demonstrate a novel mechanism for IRF3 deactivation by F-box protein-mediated recruitment of PP2A.

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Positive Regulation of Interferon Regulatory Factor 3 Activation by Herc5 via ISG15 Modification

Cited by 233 publications

References 59 publications

Activation of Double-stranded RNA-activated Protein Kinase (PKR) by Interferon-stimulated Gene 15 (ISG15) Modification Down-regulates Protein Translation

Activation of Double-stranded RNA-activated Protein Kinase (PKR) by Interferon-stimulated Gene 15 (ISG15) Modification Down-regulates Protein Translation

IFN-Induced TPR Protein IFIT3 Potentiates Antiviral Signaling by Bridging MAVS and TBK1

A Novel Function of F-Box Protein FBXO17 in Negative Regulation of Type I IFN Signaling by Recruiting PP2A for IFN Regulatory Factor 3 Deactivation

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