Identification of two essential phosphorylated threonine residues in the catalytic domain of Mekk1. Indirect activation by Pak3 and protein kinase C.

@article{Siow1997IdentificationOT,
  title={Identification of two essential phosphorylated threonine residues in the catalytic domain of Mekk1. Indirect activation by Pak3 and protein kinase C.},
  author={Yaw Chris Siow and G B Kalmar and Jasbinder S. Sanghera and Guihua Tai and Steven S Oh and Steven Pelech},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 12},
  pages={7586-94}
}
The 78-kDa protein kinase Mekk1 plays an important role in the stress response pathway that involves the activation of downstream kinases Sek1 and stress-activated protein kinase/c-Jun NH2-terminal kinase. Conserved serine and threonine residues located between the kinase subdomains VII and VIII of many protein kinases are phosphorylated for maximal kinase activation. Two threonine residues within this region in Mekk1 at positions 560 and 572, but not the serine at 557, were shown to be… CONTINUE READING

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