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. 2019 Jul 22;47(16):8838–8859. doi: 10.1093/nar/gkz628

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© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 8. — A proposed model of mRNA degradation by Regnase-1 and Roquin. Regnase-1 recognizes stem–loop on 3′ UTR of inflammatory mRNAs prior to binding with UPF1 and translation. In the Regnase-1 pathway, SMG1 phosphorylates UPF1 at T28, which is supported by the association of Regnase-1-(90-130) linker region with UPF1 RecA helicase domain. The T28-phosphorylated N-terminal region of UPF1 is associated with Regnase-1 RNase domain (K257R258) to form stable interaction between Regnase-1 and UPF1. The association with Regnase-1 promotes UPF1 ATPase/helicase activity and the unwinding of stem–loop by UPF1 helicase activity induces RNA cleavage by Regnase-1. The SMG1-UPF1–Regnase-1 axis destabilizes inflammatory mRNAs bound by CBP80 during pioneer round of translation, whereas Roquin regulates mRNAs bound by eIF4E after steady-state round of translation. NCR, N-terminal conserved region; RecA, RecA-like domain.