Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 7, Pages 4291-4297Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.074971
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Funding
- Chinese 973 Program [2006CB504301, 2010CB911802]
- National Natural Science Foundation of China [30630019, 30921001]
- Chinese 111 Project [B06018]
- Chinese National Science and Technology [2008ZX10002-014]
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Ubiquitination and deubiquitination have emerged as critical post-translational regulatory mechanisms for activation or attenuation of the virus-triggered type I interferon (IFN)(2) induction pathways. In this study, we identified two deubiquitinating enzymes, OTUB1 and OTUB2, as negative regulators of virus-triggered type I IFN induction. Overexpression of OTUB1 and OTUB2 inhibited virus-induced activation of IRF3 and NF-kappa B, transcription of the IFNB1 gene as well as cellular antiviral response, whereas knockdown of OTUB1 and OTUB2 had opposite effects. Coimmunoprecipitations indicated OTUB1 and -2 interacted with TRAF3 and TRAF6, two E3 ubiquitin ligases required for virus-triggered IRF3 and NF-kappa B activation, respectively. Furthermore, we found that OTUB1 and OTUB2 mediated virus-triggered deubiquitination of TRAF3 and -6. These findings suggest that OTUB1 and OTUB2 negatively regulate virus-triggered type IIFN induction and cellular antiviral response by deubiquitinating TRAF3 and -6.
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