Safer B, Jagus R
Biochimie. 1981 Aug-Sep;63(8-9):709-17. doi: 10.1016/s0300-9084(81)80219-2.
The regulation of eIF-2 activity during protein synthesis initiation has been postulated to involve phosphorylation/dephosphorylation mechanisms and/or the participation of ancillary protein factors. Both mechanisms would affect directly the binding of initiator methionyl-tRNAi by eIF-2. Recent data concerning the phosphorylation state of eIF-2 in hemin-deficient lysates and other covalent modifications which alter the efficiency of eIF-2 utilization, however, suggest that modulation of eIF-2 activity is more complex, and involves alteration of its catalytic recycling.