4E-BP1 (eIF4E-binding protein) also known as PHAS, is a 10-12 kDa acidic protein that compete with eIF4G for binding of eIF4E to the mRNA 5 cap structure (1). Binding of the 4E-BPs to eIF4E is reversible and is dependent on the phosphorylation status of 4E-BP1. Non-phosphorylated 4E-BP1 will bind strongly to eIF4E while, the phosphorylated form will no (2). Akt, TOR, MAP kinase, S6 kinase, and Cdc2 are known kinases capable of inactivating 4E-BP1 binding to eIF4E by phosphorylating either threonines 35, 45, 70 or serine 64. Although, not all phosphorylation events equally block the 4EBP1-eIF4E interaction (3). It has been reported previously that phosphorylation of 4E-BP1 on Thr 37 and Thr 46 is relatively insensitive to serum deprivation and rapamycin treatment, and that phosphorylation of these residues is required for the subsequent phosphorylation of a set of unidentified serum-responsive sites (4)
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