期刊
CELL REPORTS
卷 13, 期 7, 页码 1467-1480出版社
CELL PRESS
DOI: 10.1016/j.celrep.2015.10.001
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资金
- European Research Council (ERC) under EU FP7 ERC Starting Grant Agreement [335809]
- MRC UK
- European Commission under EU FP7 Marie Curie CIG [321703]
- Wellcome Trust [100034/Z/12/Z]
- Royal Society [100034/Z/12/Z]
- Cancer Research UK programme grant [C434/A13067]
- Wellcome Trust Senior Investigator Award [098391/Z/12/Z]
- Wellcome Trust [098391/Z/12/Z, 100034/Z/12/Z] Funding Source: Wellcome Trust
- MRC [G0801822] Funding Source: UKRI
- Cancer Research UK [13067] Funding Source: researchfish
- Medical Research Council [G0801822] Funding Source: researchfish
- Wellcome Trust [098391/Z/12/Z] Funding Source: researchfish
- European Research Council (ERC) [335809] Funding Source: European Research Council (ERC)
Dynamic nuclear SUMO modifications play essential roles in orchestrating cellular responses to proteotoxic stress, DNA damage, and DNA virus infection. Here, we describe a non-canonical host SUMOylation response to the nuclear-replicating RNA pathogen, influenza virus, and identify viral RNA polymerase activity as a major contributor to SUMO proteome remodeling. Using quantitative proteomics to compare stress-induced SUMOylation responses, we reveal that influenza virus infection triggers unique re-targeting of SUMO to 63 host proteins involved in transcription, mRNA processing, RNA quality control, and DNA damage repair. This is paralleled by widespread host deSUMOylation. Depletion screening identified ten virus-induced SUMO targets as potential antiviral factors, including C18orf25 and the SMC5/6 and PAF1 complexes. Mechanistic studies further uncovered a role for SUMOylation of the PAF1 complex component, parafibromin (CDC73), in potentiating antiviral gene expression. Our global characterization of influenza virus-triggered SUMO redistribution provides a proteomic resource to understand host nuclear SUMOylation responses to infection.
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