Eukaryotic translation initiation factor 2α (eIF2α) promotes the binding of initiator tRNA to the 40S ribosomal subunits, and controls translational rates via phosphorylation/dephosphorylation mechanisms. The double-stranded RNA (dsRNA)-activated protein kinase (PKR) provides an important control in the regulation of protein synthesis initiation through the phosphorylation of eIF2α. Phosphorylated eIF2α inhibits cell growth and induces apoptosis. Phosphorylation of eIF2α occurs under a variety of conditions, including viral infection, apoptosis, nutrient deprivation, heme-deprivation, and certain stresses. eIF2 exists as a heterotrimeric protein composed of 3 nonidentical subunits: α (36kDa), β (38kDa), and γ (52kDa).
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