Mouse 3-phosphoinositide-dependent protein kinase-1 undergoes dimerization and trans-phosphorylation in the activation loop.

@article{Wick2003Mouse3P,
  title={Mouse 3-phosphoinositide-dependent protein kinase-1 undergoes dimerization and trans-phosphorylation in the activation loop.},
  author={Michael J Wick and Fresnida J. Ramos and Hui Chen and Michael J. Quon and Lily Q. Dong and Feng Liu},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 44},
  pages={42913-9}
}
Activation of mouse 3-phosphoinositide-dependent protein kinase-1 (mPDK1) requires phosphorylation at a conserved serine residue, Ser244, in the activation loop. However, the mechanism by which mPDK1 is phosphorylated at this site remains unclear. We have found that kinase-defective mPDK1 (mPDK1KD), but not a kinase-defective mPDK1 in which Ser244 was replaced with alanine (mPDK1KD/S244A), is significantly phosphorylated in intact cells and is a direct substrate of wild-type mPDK1 fused to the… CONTINUE READING

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