Identification of the Minimal Phosphoacceptor Site Required for in Vivo Activation of Interferon Regulatory Factor 3 in Response to Virus and Double-stranded RNA*

@article{Servant2003IdentificationOT,
  title={Identification of the Minimal Phosphoacceptor Site Required for in Vivo Activation of Interferon Regulatory Factor 3 in Response to Virus and Double-stranded RNA*},
  author={Marc J. Servant and Nathalie Grandvaux and Benjamin R. tenOever and Delphine Duguay and Rongtuan Lin and John Hiscott},
  journal={The Journal of Biological Chemistry},
  year={2003},
  volume={278},
  pages={9441 - 9447}
}
The ubiquitously expressed latent interferon regulatory factor (IRF) 3 transcription factor is activated in response to virus infection by phosphorylation events that target a cluster of Ser/Thr residues,382GGASSLENTVDLHISNSHPLSLTSDQY408at the C-terminal end of the protein. To delineate the minimal phosphoacceptor sites required for IRF-3 activation, several point mutations were generated and tested for transactivation potential and cAMP-response element-binding protein-binding protein/p300… 
Contribution of Ser386 and Ser396 to activation of interferon regulatory factor 3.
TLDR
It appears that Ser385 and Ser386 serve antagonistic functions in regulating IRF-3 phosphoactivation, and support a phosphorylation-oligomerization model for IRf-3 activation.
Identification of a Novel in Vivo Virus-targeted Phosphorylation Site in Interferon Regulatory Factor-3 (IRF3)*
TLDR
The results show that IRF3 is subject to multiple interdependent phosphorylations, and Thr390 is identified as a novel in vivo phosphorylated site that modulates the phosphorylation status of TBK1-targeted Ser396.
Identification of Ser-386 of Interferon Regulatory Factor 3 as Critical Target for Inducible Phosphorylation That Determines Activation*
TLDR
The results strongly suggest that Ser-386 is the target of the IRF-3 kinase and critical determinant for the activation of IRf-3.
Mechanisms of activation of interferon regulator factor 3: the role of C-terminal domain phosphorylation in IRF-3 dimerization and DNA binding
TLDR
Analysis of the binding characteristics leads to the conclusion that binding of dimeric IRF-3 to the DNA with two tandem-binding sites, which are twisted by ∼100° relative to each other, requires considerable work to untwist and/or bend the DNA.
Differential Modification of Interferon Regulatory Factor 3 following Virus Particle Entry
TLDR
Current techniques used to detect interferon regulatory factor 3 activation are insufficient to infer its role in mediating downstream biological response induction and should be utilized with caution.
A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response
TLDR
It is demonstrated that MAVS harbors a functional C-terminal TRAF3-binding site that participates in positive and negative regulation of the IFN antiviral response.
Role of Cyclophilin B in Activation of Interferon Regulatory Factor-3*
TLDR
Findings indicate that cyclophilin B plays a critical role in IRF-3 activation.
Nuclear Localization of the Nipah Virus W Protein Allows for Inhibition of both Virus- and Toll-Like Receptor 3-Triggered Signaling Pathways
TLDR
It is reported that V and W proteins also block virus activation of the beta interferon (IFN-β) promoter and the IFN regulatory factor 3 (IRF3)-responsive IFN-stimulated gene 54 promoter.
Epstein-Barr Virus BGLF 4 Kinase Suppresses the Interferon Regulatory Factor 3 Signaling Pathway †
The BGLF4 protein kinase of Epstein-Barr virus (EBV) is a member of the conserved family of herpesvirus protein kinases which, to some extent, have a function similar to that of the cellular
Regulatory Serine Residues Mediate Phosphorylation-dependent and Phosphorylation-independent Activation of Interferon Regulatory Factor 7*
TLDR
A comprehensive structure-activity examination of potential IRF7 phosphorylation sites through analysis of mutant proteins in which specific serine residues were altered to alanine or aspartate found a conformational element required for function.
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TLDR
It is demonstrated that IRF-3 is a phosphoprotein that is uniquely activated via virus-dependent C-terminal phosphorylation, and that Paramyxoviridae including measles virus and rhabdoviraceae, vesicular stomatitis virus, are potent inducers of a unique virus-activated kinase activity.
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TLDR
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