Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector.

@article{Orth1999InhibitionOT,
  title={Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector.},
  author={Kim Orth and Lance E. Palmer and Zhao Qin Bao and Suzanne L K Stewart and Amy E. Rudolph and James B Bliska and Jack E. Dixon},
  journal={Science},
  year={1999},
  volume={285 5435},
  pages={1920-3}
}
The bacterial pathogen Yersinia uses a type III secretion system to inject several virulence factors into target cells. One of the Yersinia virulence factors, YopJ, was shown to bind directly to the superfamily of MAPK (mitogen-activated protein kinase) kinases (MKKs) blocking both phosphorylation and subsequent activation of the MKKs. These results explain the diverse activities of YopJ in inhibiting the extracellular signal-regulated kinase, c-Jun amino-terminal kinase, p38, and nuclear… CONTINUE READING
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