Phosphorylation of eukaryotic initiation factor 4E (eIF4E) at Ser209 is not required for protein synthesis in vitro and in vivo.

@article{McKendrick2001PhosphorylationOE,
  title={Phosphorylation of eukaryotic initiation factor 4E (eIF4E) at Ser209 is not required for protein synthesis in vitro and in vivo.},
  author={L. McKendrick and Simon J. Morley and Virginia M. Pain and Rosemary Jagus and Beenu Joshi},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 20},
  pages={5375-85}
}
Eukaryotic translation initiation factor 4E (eIF4E) is essential for efficient translation of the vast majority of capped cellular mRNAs; it binds the 5'-methylated guanosine cap of mRNA and serves as a nucleation point for the assembly of the 48S preinitiation complex. eIF4E is phosphorylated in vivo at residue 209 of the human sequence. The phosphorylated form is often regarded as the active state of the protein, with ribosome-associated eIF4E enriched for the phosphorylated form and… CONTINUE READING