Phosphorylation of the eIF4E-binding protein PHAS-I after exposure of PC12 cells to EGF and NGF.

@article{Kleijn1996PhosphorylationOT,
  title={Phosphorylation of the eIF4E-binding protein PHAS-I after exposure of PC12 cells to EGF and NGF.},
  author={Mieke Kleijn and Marcel Korthout and Harry O. Voorma and Adri A. M. Thomas},
  journal={FEBS letters},
  year={1996},
  volume={396 2-3},
  pages={
          165-71
        }
}
PHAS-I or the eIF4E-binding protein 1 regulates the cap-binding activity of eIF4E by sequestering eIF4E. Binding of elF4E to PHAS-I is regulated by phosphorylation of PHAS-I. PC12 cells were used to study the signal transduction pathway leading to phosphorylation of PHAS-I. Both EGF and NGF induced phosphorylation of PHAS-I. Wortmannin, a PI-3 kinase inhibitor, staurosporine, a PKC inhibitor, and rapamycin, a FRAP inhibitor all blocked the phosphorylation of PHAS-I. Of the three inhibitors… CONTINUE READING