eIF2α functions by forming a ternary complex with GTP and the initiator tRNA. This complex binds to the small ribosomal subunit and facilitates the identification of the start codon on mRNA. Upon recognition, GTP is hydrolyzed to GDP, and the eIF2 complex is released, allowing the large ribosomal subunit to join and initiate protein synthesis. Phosphorylation of eIF2α at serine 51 inhibits this process, serving as a regulatory mechanism during cellular stress.
