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Measles Virus Takes a Two-Pronged Attack on PP1
Tsukasa Seya Cell Host & Microbe Volume 16, Issue 1, Pages 1-2 (July 2014) DOI: /j.chom Copyright © 2014 Elsevier Inc. Terms and Conditions
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Figure 1 Measles Virus Subverts PP1-Mediated Dephosphorylation and Activation of RLRs In response to viral RNA, PP1 dephosphorylates MDA5 (right) and RIG-I (left) to induce their activation, ultimately resulting in type I IFN production. However, measles virus (MV) subverts this response using two approaches. The MV-V protein acts as a competitive substrate for PP1 to block activation of MDA5. Additionally, the virus binds to the surface molecule DC-SIGN on dendritic cells and induces the activation of the Raf-1 kinase. Raf-1 phosphorylates the phosphatase inhibitor I-1, resulting in its association with GADD34-PP1 phosphatase holoenzymes and inhibition of their phosphatase activity. Cell Host & Microbe , 1-2DOI: ( /j.chom ) Copyright © 2014 Elsevier Inc. Terms and Conditions
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