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Interaction between the Yersinia protein tyrosine phosphatase YopH and eukaryotic Cas/Fyb is an important virulence mechanism
Umeå University, Faculty of Medicine, Molecular Biology.
Umeå University, Faculty of Medicine, Molecular Biology.
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).
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2003 (English)In: Cellular Microbiology, ISSN 1462-5814, E-ISSN 1462-5822, Vol. 5, no 1, 53-64 p.Article in journal (Refereed) Published
Abstract [en]

The tyrosine phosphatase YopH is an essential virulence factor produced by pathogenic Yersinia species. YopH is translocated into host cells via a type III secretion system and its dephosphorylating activity causes disruption of focal complex structures and blockage of the phagocytic process. Among the host cell targets of YopH are the focal adhesion proteins Crk-associated substrate (p130Cas) and focal adhesion kinase (FAK) in epithelial cells, and p130Cas and Fyn-binding protein (Fyb) in macrophages. Previous studies have shown that the N-terminal domain of YopH acts as a substrate-binding domain. In this study, the mechanism and biological importance of the targeting of YopH to focal complexes relative to its interaction with p130Cas/Fyb was elucidated. Mutants of YopH that were defective in p130Cas/Fyb binding but otherwise indistinguishable from wild type were constructed. Mutants unable to bind p130Cas did not localize to focal complex structures in infected cells, indicating that the association with p130Cas is critical for appropriate subcellular localization of YopH. These yopH mutants were also clearly attenuated in virulence, showing that binding to p130Cas and/or Fyb is biologically relevant in Yersinia infections.

Place, publisher, year, edition, pages
2003. Vol. 5, no 1, 53-64 p.
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Cell and Molecular Biology
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URN: urn:nbn:se:umu:diva-33321DOI: 10.1046/j.1462-5822.2003.00236.xPubMedID: 12542470OAI: oai:DiVA.org:umu-33321DiVA: diva2:311552
Available from: 2010-04-21 Created: 2010-04-21 Last updated: 2017-12-12Bibliographically approved

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Deleuil, FabienneMogemark, LenaFrancis, Matthew SWolf-Watz, HansFällman, Maria
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Molecular BiologyDepartment of Molecular Biology (Faculty of Science and Technology)Umeå Centre for Microbial Research (UCMR)Department of Molecular Biology (Faculty of Medicine)
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