Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation.
In: Science, Jg. 347 (2015-03-13), Heft 6227, S. 1-14
Online
academicJournal
Zugriff:
During virus infection, the adaptor proteins MAVS and STING transduce signals from the cytosolic nucleic acid sensors RIG-I and cGAS, respectively, to induce type I interferons (IFNs) and other antiviral molecules. Here we show that MAVS and STING harbor two conserved serine and threonine clusters that are phosphorylated by the kinases IKK and/or TBK1 in response to stimulation. Phosphorylated MAVS and STING then bind to a positively charged surface of interferon regulatory factor 3 (IRF3) and thereby recruit IRF3 for its phosphorylation and activation by TBK1.We further show that TRIF, an adaptor protein in Toll-like receptor signaling, activates IRF3 through a similar phosphorylation-dependent mechanism. These results reveal that phosphorylation of innate adaptor proteins is an essential and conserved mechanism that selectively recruits IRF3 to activate the type I IFN pathway. [ABSTRACT FROM AUTHOR]
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Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation.
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Autor/in / Beteiligte Person: | Liu, Siqi ; Cai, Xin ; Wu, Jiaxi ; Cong, Qian ; Chen, Xiang ; Li, Tuo ; Du, Fenghe ; Ren, Junyao ; Wu, You-Tong ; Grishin, Nick V. ; Chen, Zhijian J. |
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Zeitschrift: | Science, Jg. 347 (2015-03-13), Heft 6227, S. 1-14 |
Veröffentlichung: | 2015 |
Medientyp: | academicJournal |
ISSN: | 0036-8075 (print) |
DOI: | 10.1126/science.aaa2630 |
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