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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins / physiology*
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Calcium-Calmodulin-Dependent Protein Kinases / antagonists & inhibitors*
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Cell Line
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Enzyme Activation
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Enzyme Inhibitors / pharmacology*
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HeLa Cells
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Humans
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MAP Kinase Kinase Kinase 1*
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NF-kappa B / metabolism
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Phosphorylation
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Protein Binding
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Transfection
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Virulence
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Yersinia pseudotuberculosis / genetics
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Yersinia pseudotuberculosis / metabolism
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Yersinia pseudotuberculosis / pathogenicity
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Yersinia pseudotuberculosis / physiology*
Substances
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Bacterial Proteins
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Enzyme Inhibitors
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NF-kappa B
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Recombinant Fusion Proteins
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YopP protein, Yersinia
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Protein Serine-Threonine Kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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MAP Kinase Kinase Kinase 1
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MAP3K1 protein, human