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

Kim Orth, Lance E. Palmer, Zhao Qin Bao, Scott Stewart, Amy E. Rudolph, James B. Bliska, Jack E. Dixon

Research output: Contribution to journalArticle

310 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1920-1923
Number of pages4
JournalScience
Volume285
Issue number5435
DOIs
StatePublished - Sep 17 1999

ASJC Scopus subject areas

  • General

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    Orth, K., Palmer, L. E., Bao, Z. Q., Stewart, S., Rudolph, A. E., Bliska, J. B., & Dixon, J. E. (1999). Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science, 285(5435), 1920-1923. https://doi.org/10.1126/science.285.5435.1920