A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation.

@article{Dppler2007ANT,
  title={A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation.},
  author={Heike R. D{\"o}ppler and Peter Storz},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 44},
  pages={31873-81}
}
Protein kinase D1 (PKD1) is a mediator of oxidative stress signaling where it regulates cellular detoxification and survival. Critical for the regulation of PKD1 activity in response to oxidative stress are Src- and Abl-mediated tyrosine phosphorylations that eventually lead to protein kinase Cdelta (PKCdelta)-mediated activation of PKD1. Here we identify Tyr95 in PKD1 as a previously undescribed phosphorylation site that is regulated by oxidative stress. Our data suggest that PKD1… CONTINUE READING

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