The extracellular signal-regulated kinase pathway regulates the phosphorylation of 4E-BP1 at multiple sites.

@article{Herbert2002TheES,
  title={The extracellular signal-regulated kinase pathway regulates the phosphorylation of 4E-BP1 at multiple sites.},
  author={Terence P. Herbert and Andrew R Tee and Christopher G Proud},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 13},
  pages={11591-6}
}
The phorbol ester, 12-O-tetradecanoylphorbol 13-acetate (TPA), a potent stimulator of Erk, leads to the phosphorylation of 4E-BP1 and its dissociation from eIF4E. In contrast to agonists such as insulin, this occurs independently of PKB activation. In this report, we investigate the mechanism by which TPA regulates 4E-BP1 phosphorylation. Treatment of HEK293 cells with TPA was found to result in the phosphorylation of 4E-BP1 at Ser(64), Thr(69), and Thr(36/45). The TPA-stimulated… CONTINUE READING

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