A 3-Phosphoinositide-dependent Protein Kinase-1 (PDK1) Docking Site Is Required for the Phosphorylation of Protein Kinase Cζ (PKCζ) and PKC-related Kinase 2 by PDK1*

@article{Balendran2000A3P,
  title={A 3-Phosphoinositide-dependent Protein Kinase-1 (PDK1) Docking Site Is Required for the Phosphorylation of Protein Kinase C$\zeta$ (PKC$\zeta$) and PKC-related Kinase 2 by PDK1*},
  author={A. Balendran and R. Biondi and P. Cheung and A. Casamayor and M. De{\'a}k and D. Alessi},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={20806 - 20813}
}
Members of the AGC subfamily of protein kinases including protein kinase B, p70 S6 kinase, and protein kinase C (PKC) isoforms are activated and/or stabilized by phosphorylation of two residues, one that resides in the T-loop of the kinase domain and the other that is located C-terminal to the kinase domain in a region known as the hydrophobic motif. Atypical PKC isoforms, such as PKCζ, and the PKC-related kinases, like PRK2, are also activated by phosphorylation of their T-loop site but… Expand
The C-terminus of PRK2/PKNgamma is required for optimal activation by RhoA in a GTP-dependent manner.
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Regulation of protein kinase C ζ by PI 3-kinase and PDK-1
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