eIF2α (Ser51) Phosphorylated [MD434R]

eIF2α (eukaryotic translation initiation factor 2 subunit alpha), located predominantly in the cytoplasm, is a member of the eIF2 complex that regulates the initiation of protein synthesis by forming a ternary complex with GTP and initiator tRNA. The rate of formation of the ternary complex is modulated by the phosphorylation state of EIF2-alpha. While unphosphorylated eIF2α promotes normal protein synthesis, phosphorylation at Ser51 in response to cellular stress inhibits GDP/GTP exchange, leading to a reduction in protein synthesis. This regulatory mechanism allows cells to adapt to stress conditions such as nutrient deprivation, viral infection, and endoplasmic reticulum stress by conserving resources and preventing the accumulation of misfolded proteins. Dysregulation of eIF2α function is implicated in various diseases, including neurodegenerative disorders and cancer, underscoring its importance in maintaining cellular homeostasis.