self protection from anti-viral responses – ro52 promotes degradation of the transcription factor irf7 downstream of the viral toll-like receptors从抗病毒反应自我保护u2014u2014ro52促进降解下游转录因子irf7的病毒toll样受体.pdfVIP

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2017-09-11 发布于上海
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self protection from anti-viral responses – ro52 promotes degradation of the transcription factor irf7 downstream of the viral toll-like receptors从抗病毒反应自我保护u2014u2014ro52促进降解下游转录因子irf7的病毒toll样受体.pdf

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self protection from anti-viral responses – ro52 promotes degradation of the transcription factor irf7 downstream of the viral toll-like receptors从抗病毒反应自我保护u2014u2014ro52促进降解下游转录因子irf7的病毒toll样受体

Self Protection from Anti-Viral Responses – Ro52 Promotes Degradation of the Transcription Factor IRF7 Downstream of the Viral Toll-Like Receptors 1 1 1 ´ 1 2 Rowan Higgs , Elisa Lazzari , Claire Wynne , Joan Nı Gabhann , Alexander Espinosa , Marie 2 1 Wahren-Herlenius , Caroline A. Jefferies * 1 Molecular and Cellular Therapeutics and RSCI Research Institute, Royal College of Surgeons in Ireland, Dublin, Ireland, 2 Department of Medicine, Karolinska Institutet, Stockholm, Sweden Abstract Ro52 is a member of the TRIM family of single-protein E3 ligases and is also a target for autoantibody production in systemic ¨ lupus erythematosus and Sjogren’s syndrome. We previously demonstrated a novel function of Ro52 in the ubiquitination and proteasomal degradation of IRF3 following TLR3/4 stimulation. We now present evidence that Ro52 has a similar role in regulating the stability and activity of IRF7. Endogenous immunoprecipitation of Ro52-bound proteins revealed that IRF7 associates with Ro52, an effect which increases following TLR7 and TLR9 stimulation, suggesting that Ro52 interacts with IRF7 post-pathogen recognition. Furthermore, we show that Ro52 ubiquitinates IRF7 in a dose-dependent manner, resulting in a decrease in total IRF7 expression and a subsequent decrease in IFN-a production. IRF7 stability was increased in bone marrow-derived macrophages from Ro52-deficient mice stimulated with imiquimod or CpG-B, consistent with a role for Ro52 in the negative regulation of IRF7 signalling. Taken together, these results suggest that Ro52-mediated ubiquitination promotes the degradation of IRF7 following TL