Modulation of the eukaryotic initiation factor 2 alpha-subunit kinase PERK by tyrosine phosphorylation.

@article{Su2008ModulationOT,
  title={Modulation of the eukaryotic initiation factor 2 alpha-subunit kinase PERK by tyrosine phosphorylation.},
  author={Qiaozhu Su and Shuo Wang and Hong Qing Gao and Shirin Kazemi and Heather P Harding and David Ron and Antonis E. Koromilas},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 1},
  pages={
          469-75
        }
}
The endoplasmic reticulum (ER)-resident protein kinase PERK attenuates protein synthesis in response to ER stress through the phosphorylation of translation initiation factor eIF2alpha at serine 51. ER stress induces PERK autophosphorylation at several serine/threonine residues, a process that is required for kinase activation and phosphorylation of eIF2alpha. Herein, we demonstrate that PERK also possesses tyrosine kinase activity. Specifically, we show that PERK is capable of… CONTINUE READING
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