Abstract Host pattern-recognition receptors (PRRs) recognize pathogen-associated molecular patterns generated by invading viruses and initiate a series of signaling cascades that lead to the activation of interferon-regulatory factor 3 (IRF3) and nuclear factor-κB (NF-κB) and subsequent induction of type I interferons (IFNs). Posttranslational modification of proteins by ubiquitin plays an essential role in mediating or regulating the virus-triggered PRRs-mediated signaling. Deubiquitination is the reversible process of ubiquitination and its role in regulating PRRs-mediated signaling has recently been explored. In this review, we first summarize the ubiquitination events in PRRs-mediated signaling that is triggered by viral nucleic acid and then focus on host and viral deubiquitinating enzymes-mediated regulation of virus-triggered signaling that modulates the activation of IRF3 and NF-κB and subsequent induction of type I IFNs.
Regulation of cellular innate antiviral signaling by ubiquitin modification
Published 2015 in Acta Biochimica et Biophysica Sinica
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- Publication year
2015
- Venue
Acta Biochimica et Biophysica Sinica
- Publication date
2015-02-03
- Fields of study
Biology, Medicine
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- External record
- Source metadata
Semantic Scholar, PubMed
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