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Inhibition of the Mitogen-Activated Protein Kinase Kinase Superfamily by a Yersinia Effector

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Science  17 Sep 1999:
Vol. 285, Issue 5435, pp. 1920-1923
DOI: 10.1126/science.285.5435.1920

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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.

  • * Present address: Howard Hughes Medical Institute and Department of Immunology, University of Washington, Seattle, WA 98195, USA.

  • Present address: Monsanto/Searle, 800 North Lindbergh Boulevard, St. Louis, MO 631667, USA.

  • To whom correspondence should be addressed. E-mail: jedixon{at}umich.edu

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