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. 1999 Sep 17;285(5435):1920-3.
doi: 10.1126/science.285.5435.1920.

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

K Orth  1 , L E Palmer, Z Q Bao, S Stewart, A E Rudolph, J B Bliska, J E Dixon
Affiliations

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

K Orth et al. Science. .

Abstract

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 factor kappa B signaling pathways, preventing cytokine synthesis and promoting apoptosis. YopJ-related proteins that are found in a number of bacterial pathogens of animals and plants may function to block MKKs so that host signaling responses can be modulated upon infection.

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