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Originally published In Press as doi:10.1074/jbc.M301226200 on March 6, 2003

J. Biol. Chem., Vol. 278, Issue 20, 18514-18523, May 16, 2003
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The Yersinia Virulence Factor YopM Forms a Novel Protein Complex with Two Cellular Kinases*

Christine McDonaldDagger , Panayiotis O. VacratsisDagger , James B. Bliska§, and Jack E. DixonDagger

From the Dagger  Department of Biological Chemistry, University of Michigan Medical School, Life Sciences Institute, Ann Arbor, Michigan 48109 and the § Department of Molecular Genetics and Microbiology, Center for Infectious Diseases, State University of New York, Stony Brook, New York 11794

Pathogenic Yersinia contain a virulence plasmid that encodes genes for intracellular effectors, which neutralize the host immune response. One effector, YopM, is necessary for Yersinia virulence, but its function in host cells is unknown. To identify potential cellular pathways affected by YopM, proteins that co-immunoprecipitate with YopM in mammalian cells were isolated and identified by mass spectrometry. Results demonstrate that two kinases, protein kinase C-like 2 (PRK2) and ribosomal S6 protein kinase 1 (RSK1), interact directly with YopM. These two kinases associate only when YopM is present, and expression of YopM in cells stimulates the activity of both kinases. RSK1 is activated directly by interaction with YopM, and RSK1 kinase activity is required for YopM-stimulated PRK2 activity. YopM activation of RSK1 occurs independently of the actions of YopJ on the MAPK pathway. YopM is also required for Yersinia-induced changes in RSK1 mobility in infected macrophage cells. These results identify the first intracellular targets of YopM and suggest YopM acts to stimulate the activity of PRK2 and RSK1.

* This work was supported by National Institutes of Health Grants RO1 AI43389 (to J. B. B.), R37 DK18024, and R01 DK18849 (to J. E. D.), and funds from the Ellison Medical Foundation (to J. E. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 858-822-3529; Fax: 858-534-6573; E-mail: jedixon@umich.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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