TRAF6 and MEKK1 play a pivotal role in the RIG-I-like helicase antiviral pathway.

Yoshida, Ryoko; Takaesu, Giichi; Yoshida, Hideyuki; Okamoto, F.; Yoshioka, Tomoko; Choi, Yongwon; Akira, Shizuo; Kawai, Taro; Yoshimura, Akihiko; Kobayashi, Takashi

doi:10.1074/jbc.a806576200

Cited by 22 publications

(28 citation statements)

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“…The C-terminal TIM of MAVS has been shown to bind TRAF6 [13], and although previous studies demonstrated that TRAF6 did not function in IFN signaling [13,61], we sought to confirm that the activity of MAVS ∆aa 101-450 was mediated by TRAF3 and not TRAF6. In TRAF6 +/+ and TRAF6 −/− MEFs, the MAVS ∆aa 101-450 construct induced IFNα4 activity, both in the presence or absence of TRAF6, whereas MAVS ∆aa 101-480 did not activate the IFNα4 promoter in either TRAF6 +/+ or TRAF6 −/− MEFs ( Figure 2D), thus ruling out the involvement of TRAF6 in MAVS ∆aa 101-450-driven activity.…”

Section: Traf3 Binds To a Functional Site Within The C-terminus Of Mavsmentioning

confidence: 99%

A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response

et al. 2011

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Section: Traf3 Binds To a Functional Site Within The C-terminus Of Mavsmentioning

confidence: 99%

A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response

et al. 2011

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“…Similar to the TLR3 signaling pathway, TRAF6 and TAK1 play critical roles in the activation of NF-kB and MAPK signaling pathways (10)(11)(12). TRAF6 can also interact with MAPK kinase 1, which in turn contributes to the activation of IkB kinase and MAPKK, leading to activation of the NF-kB and MAPK signaling pathways (13).…”

mentioning

confidence: 99%

Inducible Major Vault Protein Plays a Pivotal Role in Double-Stranded RNA– or Virus-Induced Proinflammatory Response

Peng

Shi

Xia

et al. 2016

The Journal of Immunology

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Pathogen invasion triggers robust antiviral cytokine production via different transcription factor signaling pathways. We have previously demonstrated that major vault protein (MVP) induces type I IFN production during viral infection; however, little is known about the role of MVP in proinflammatory responses. In this study, we found in vitro that expression of MVP, IL-6, and IL-8 was inducible upon dsRNA stimulation or viral infection. Moreover, MVP was essential for the induction of IL-6 and IL-8, as impaired expression of IL-6 and IL-8 in MVP-deficient human PBMCs, human lung epithelial cells (A549), and THP-1 monocytes, as well as in murine splenocytes, peritoneal macrophages, and PBMCs from MVP-knockout (MVP−/−) mice, was observed. Upon investigation of the underlying mechanisms, we demonstrated that MVP acted in synergy with AP-1 (c-Fos) and CCAAT/enhancer binding protein (C/EBP)β–liver-enriched transcriptional activating protein to activate the IL6 and IL8 promoters. Introduction of mutations into the AP-1 and C/EBPβ binding sites on the IL6 and IL8 promoters resulted in the loss of synergistic activation with MVP. Furthermore, we found that MVP interacted with both c-Fos and C/EBPβ. The interactions promoted nuclear translocation and recruitment of these transcription factors to IL6 and IL8 promoter regions. In the MVP−/− mouse model, significantly decreased expression of early antiviral cytokines resulted in higher viral titer in the lung, higher mortality, and heavier lung damage after infection with lethal influenza A virus. Taken together, our findings help to delineate a novel role of MVP in host proinflammatory response.

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“…The IFN type I signalling is mediated through activation of both Janus kinase (JAK) and signal transducers and activator of transcription (STAT) known as JAK-STAT pathway: after receptor activation STAT1/1 homodimers migrate to nucleus and initiate a complex formation with IFN regulatory factor-9 (IRF-9) and interferon stimulated-regulatory elements (ISREs) to induce the expression of many IFN-α/β inducible genes [20]. IFNs production, from host cell, is stimulated via several virus infection, some stress condition and endotoxin exposure resulted in enhancement of the cell response by activation of Jun N-terminal kinasee (JNK) and termed stress-activated protein kinasee (SAPK) [21]. Such events theoretically up-regulates the activity of transcription factor of AP-1 family.…”

Section: Introductionmentioning

confidence: 99%

The Intracellular Signalling that Associated with Influenza A Virus Infection

Khalil¹

2017

Pediatric Infect Dis

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Influenza-A virus infection induces a variety of intracellular signalling pathways that are either antiviral or required to ensure efficient replication. A prominent cellular antiviral event is the activation of cascade that produces type I interferon's (IFNs): IFN-α and IFN-β. Consequently, an appreciated number of antiviral proteins that encoded by so-called IFN stimulated genes are activated, such as Mx1, PKR and ISG-15 genes. Conversely, virus-supportive signalling processes activated upon infection are I kappa B kinase/nuclear factor kappa-light-chain-enhancer of activated B cells (IKK/ NF-κB), phosphatidylinositol-3-kinasee/Akt (PI3K/Akt), and the RNA activating factor-1(Raf-1). Specific inhibition of the latter signalling cascade leads to striking impairment of the replication of all influenza A viruses, as a result of nuclear retention of RNPs in late stages of the replication cycle. In this review, the intracellular signaling that associated with IAV infection will be highlighted to realize the appropriate therapeutically strategy against IAV infection.

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TRAF6 and MEKK1 play a pivotal role in the RIG-I-like helicase antiviral pathway.

Abstract: On page 30551, Table 1, first column, the experimentally determined values of EC 50 of ER activation for MC, Polysantol, Javanol, and androstenol have been presented with the wrong concentration (mM). The correct concentration is M.

Cited by 22 publications

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A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response

A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response

Inducible Major Vault Protein Plays a Pivotal Role in Double-Stranded RNA– or Virus-Induced Proinflammatory Response

The Intracellular Signalling that Associated with Influenza A Virus Infection

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