The absence of nuclear eIF2
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چکیده
Eukaryotic translation initiation factor 2 (eIF2) is necessary for binding of the methionyl-tRNA to the small ribosomal subunit and therefore is essential to the commencement of protein translation. It is of particular interest since it is a site of regulation of protein synthesis. Phosphorylation of its α subunit by a family of stress-dependent kinases leads to rapid inhibition of protein synthesis.
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Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes
Phosphorylation of eIF2α controls translation initiation by restricting the levels of active eIF2-GTP/Met-tRNAi ternary complexes (TC). This modulates the expression of all eukaryotic mRNAs and contributes to the cellular integrated stress response. Key to controlling the activity of eIF2 are translation factors eIF2B and eIF5, thought to primarily function with eIF2-GDP and TC respectively. Us...
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