Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases.

@article{Raught2004PhosphorylationOE,
  title={Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases.},
  author={Brian Raught and Franck Peiretti and Anne-Claude Gingras and Mark Livingstone and David Shahbazian and Greg L. Mayeur and Roberto D. Polakiewicz and Nahum Sonenberg and John W. B. Hershey},
  journal={The EMBO journal},
  year={2004},
  volume={23 8},
  pages={1761-9}
}
The eucaryotic translation initiation factor 4B (eIF4B) stimulates the helicase activity of the DEAD box protein eIF4A to unwind inhibitory secondary structure in the 5' untranslated region of eucaryotic mRNAs. Here, using phosphopeptide mapping and a phosphospecific antiserum, we identify a serum-responsive eIF4B phosphorylation site, Ser422, located in an RNA-binding region required for eIF4A helicase-promoting activity. Ser422 phosphorylation appears to be regulated by the S6Ks: (a) Ser422… CONTINUE READING
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