Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity.

@article{Zenke1999IdentificationOA,
  title={Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity.},
  author={Frank T Zenke and Charles C. King and Benjamin Bohl and Gary M. Bokoch},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 46},
  pages={32565-73}
}
p21-activated kinases (Pak)/Ste20 kinases are regulated in vitro and in vivo by the small GTP-binding proteins Rac and Cdc42 and lipids, such as sphingosine, which stimulate autophosphorylation and phosphorylation of exogenous substrates. The mechanism of Pak activation by these agents remains unclear. We investigated Pak kinase activation in more detail to gain insight into the interplay between the GTPase/sphingosine binding, an intramolecular inhibitory interaction, and autophosphorylation… CONTINUE READING
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