eIF2 beta Antibody #50537

eIF2 binds GTP and Met-tRNAi and transfers Met-tRNA to the 40S subunit to form the 43S preinitiation complex (1,2). eIF2 promotes a new round of translation initiation by exchanging GDP for GTP, a reaction catalyzed by eIF2β (1,2). Kinases that are activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), or heme deficiency (HRI) can phosphorylate the α subunit of eIF2 (3,4). This phosphorylation stabilizes the eIF2-GDP-eIF2β complex and inhibits the turnover of eIF2β. Induction of PKR by IFN-γ and TNF-α induces potent phosphorylation of eIF2α at Ser51 (5,6).

The eIF2β subunit plays a major role in various interactions of the eIF2 trimer with other proteins. eIF2β has been shown to directly interact with other eIF factors, including eIF5, eIF2B, and eIF3 (7-9). eIF2β has also been shown to directly bind mRNA through a C-terminal zinc-finger motif (10,11). Phosphorylation of eIF2β by CK2 promotes the guanine nucleotide exchange activity of eIF2β (12,13).