We propose that phosphorylation of e IF2α and the consequent SG assembly is important for shutoff to occur and that the localized SG disassembly and the presence of the enhancer aid the SFV m RNAs to elude general translational arrest.
(2015) Proteomics of yeast telomerase identified Cdc48-Npl4-Ufd1 and Ufd4 as regulators of Est1 and telomere length.
(2015) The intricate roles of mammalian sirtuins in defense against viral pathogens. [Epub ahead of print] Lin KW, Mc Donald KR, Guise AJ, Chan A, Cristea IM, Zakian VA.
Infection of mouse embryo fibroblasts (MEFs) expressing a nonphosphorylatable mutant of e IF2α does not result in efficient shutoff, despite efficient viral protein production.
Furthermore, we show that the SFV translation enhancer element counteracts the translation inhibition imposed by e IF2α phosphorylation.
Alphavirus infection results in the shutoff of host protein synthesis in favor of viral translation.
Here, we show that during Semliki Forest virus (SFV) infection, the translation inhibition is largely due to the activation of the cellular stress response via phosphorylation of eukaryotic translation initiation factor 2α subunit (e IF2α).