Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1.

@article{Sekiyama2015MolecularMO,
  title={Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1.},
  author={Naotaka Sekiyama and Haribabu Arthanari and Evangelos Papadopoulos and Ricard A. Rodriguez-Mias and Gerhard Wagner and M{\'e}lissa L{\'e}ger-Abraham},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2015},
  volume={112 30},
  pages={E4036-45}
}
The eIF4E-binding protein (4E-BP) is a phosphorylation-dependent regulator of protein synthesis. The nonphosphorylated or minimally phosphorylated form binds translation initiation factor 4E (eIF4E), preventing binding of eIF4G and the recruitment of the small ribosomal subunit. Signaling events stimulate serial phosphorylation of 4E-BP, primarily by mammalian target of rapamycin complex 1 (mTORC1) at residues T37/T46, followed by T70 and S65. Hyperphosphorylated 4E-BP dissociates from eIF4E… CONTINUE READING
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