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={Anudharan Balendran and Ricardo M. Biondi and Peter C. F. Cheung and Antonio Casamayor and M{\'a}ria De{\'a}k and Dario R. 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… 

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The Phosphoinositide-dependent Kinase, PDK-1, Phosphorylates Conventional Protein Kinase C Isozymes by a Mechanism That Is Independent of Phosphoinositide 3-Kinase*
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Characterization of Phosphatidylinositol 3-Kinase-dependent Phosphorylation of the Hydrophobic Motif Site Thr389 in p70 S6 Kinase 1*
TLDR
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TLDR
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Identification of Tyrosine Phosphorylation Sites on 3-Phosphoinositide-dependent Protein Kinase-1 and Their Role in Regulating Kinase Activity*
TLDR
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Regulation of 3-Phosphoinositide-dependent Protein Kinase-1 (PDK1) by Src Involves Tyrosine Phosphorylation of PDK1 and Src Homology 2 Domain Binding*
TLDR
Data suggest that phosphorylation of PDK1 on Tyr9, distinct from Tyr373/376, is important for PDK3-Phosphoinositide-dependent protein kinase-1/Src complex formation, leading toPDK1 activation.
Mouse 3-Phosphoinositide-dependent Protein Kinase-1 Undergoes Dimerization and trans-Phosphorylation in the Activation Loop*
TLDR
The results show that mPDK1 autophosphorylation occurs at multiple sites through both cis and trans mechanisms and suggest that dimerization and trans-ph phosphorylation may serve as mechanisms to regulate PDK1 activity in cells.
Differential roles of PDK 1-and PDK 2-phosphorylation sites in the yeast AGC kinases Ypk 1 , Pkc 1 and Sch 9
TLDR
Genetic and biochemical methods have been used to investigate the physiological consequences of phosphorylation at the PDK1 and PDK2 sites of Ypk1, Pkc1 and Sch9, and it was found that phosphorylated at thePDK1 site in the activation loop is indispensable for the essential functions of all three kinases in vivo.
Differential roles of PDK1- and PDK2-phosphorylation sites in the yeast AGC kinases Ypk1, Pkc1 and Sch9.
TLDR
Genetic and biochemical methods have been used to investigate the physiological consequences of phosphorylation at the PDK1 and PDK2 sites of Ypk1, Pkc1 and Sch9 and it was found that phosphorylated at thePDK1 site in the activation loop is indispensable for the essential functions of all three kinases in vivo.
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TLDR
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