Cell invasion of Yersinia pseudotuberculosis by invasin and YadA requires protein kinase C, phospholipase C-gamma1 and Akt kinase.

2.50
Hdl Handle:
http://hdl.handle.net/10033/97536
Title:
Cell invasion of Yersinia pseudotuberculosis by invasin and YadA requires protein kinase C, phospholipase C-gamma1 and Akt kinase.
Authors:
Uliczka, Frank; Kornprobst, Tina; Eitel, Julia; Schneider, Daniela; Dersch, Petra
Abstract:
The outer membrane proteins YadA and invasin of Yersinia pseudotuberculosis promote invasion into mammalian cells through beta(1)-integrins and trigger the production of interleukin (IL)-8. FAK, c-Src and the PI3 kinase were previously found to be important for both YadA- and invasin-promoted uptake. Here, we demonstrate that two different downstream effectors of PI3 kinase, Akt and phospholipase Cgamma1 are required for efficient cell invasion. Inhibition of Akt or phospholipase C-gamma (PLC-gamma)1 by pharmaceutical agents as well as reduced expression of the isoforms Akt1 and Akt2, and of PLC-gamma1 by RNA interference decreased entry of YadA- and Inv-expressing bacteria significantly. In addition, we report that the conventional protein kinases C (PKC)alpha and -beta, positioned downstream of PLC-gamma1, are activated upon Inv- or YadA-promoted cell entry. They colocalize with intracellular bacteria and their depletion by siRNA treatment also resulted in a strong reduction of cell entry. In contrast, neither Akt nor PLC-gamma1, and the PKCs are essential for YadA- and Inv-mediated IL-8 synthesis and release. We conclude that YadA and invasin of Y. pseudotuberculosis both trigger similar signal transduction pathways during integrin-mediated phagocytosis into epithelial cells, which lead to the activation of Akt, PLC-gamma1, PKCalpha and -beta downstream of PI3 kinase, separate from the MAPK-dependent pathway that triggers IL-8 production.
Affiliation:
Institut für Mikrobiologie, Technische Universität Braunschweig, 38106 Braunschweig, Germany.
Citation:
Cell invasion of Yersinia pseudotuberculosis by invasin and YadA requires protein kinase C, phospholipase C-gamma1 and Akt kinase. 2009, 11 (12):1782-801 Cell. Microbiol.
Journal:
Cellular microbiology
Issue Date:
Dec-2009
URI:
http://hdl.handle.net/10033/97536
DOI:
10.1111/j.1462-5822.2009.01371.x
PubMed ID:
19681907
Type:
Article
Language:
en
ISSN:
1462-5822
Appears in Collections:
publications of the department of molecular Infectionbiology (MIBI)

Full metadata record

DC FieldValue Language
dc.contributor.authorUliczka, Franken
dc.contributor.authorKornprobst, Tinaen
dc.contributor.authorEitel, Juliaen
dc.contributor.authorSchneider, Danielaen
dc.contributor.authorDersch, Petraen
dc.date.accessioned2010-04-28T08:01:39Z-
dc.date.available2010-04-28T08:01:39Z-
dc.date.issued2009-12-
dc.identifier.citationCell invasion of Yersinia pseudotuberculosis by invasin and YadA requires protein kinase C, phospholipase C-gamma1 and Akt kinase. 2009, 11 (12):1782-801 Cell. Microbiol.en
dc.identifier.issn1462-5822-
dc.identifier.pmid19681907-
dc.identifier.doi10.1111/j.1462-5822.2009.01371.x-
dc.identifier.urihttp://hdl.handle.net/10033/97536-
dc.description.abstractThe outer membrane proteins YadA and invasin of Yersinia pseudotuberculosis promote invasion into mammalian cells through beta(1)-integrins and trigger the production of interleukin (IL)-8. FAK, c-Src and the PI3 kinase were previously found to be important for both YadA- and invasin-promoted uptake. Here, we demonstrate that two different downstream effectors of PI3 kinase, Akt and phospholipase Cgamma1 are required for efficient cell invasion. Inhibition of Akt or phospholipase C-gamma (PLC-gamma)1 by pharmaceutical agents as well as reduced expression of the isoforms Akt1 and Akt2, and of PLC-gamma1 by RNA interference decreased entry of YadA- and Inv-expressing bacteria significantly. In addition, we report that the conventional protein kinases C (PKC)alpha and -beta, positioned downstream of PLC-gamma1, are activated upon Inv- or YadA-promoted cell entry. They colocalize with intracellular bacteria and their depletion by siRNA treatment also resulted in a strong reduction of cell entry. In contrast, neither Akt nor PLC-gamma1, and the PKCs are essential for YadA- and Inv-mediated IL-8 synthesis and release. We conclude that YadA and invasin of Y. pseudotuberculosis both trigger similar signal transduction pathways during integrin-mediated phagocytosis into epithelial cells, which lead to the activation of Akt, PLC-gamma1, PKCalpha and -beta downstream of PI3 kinase, separate from the MAPK-dependent pathway that triggers IL-8 production.en
dc.language.isoenen
dc.subject.meshAdhesins, Bacterialen
dc.subject.meshCell Lineen
dc.subject.meshEnzyme Inhibitorsen
dc.subject.meshHost-Pathogen Interactionsen
dc.subject.meshHumansen
dc.subject.meshInterleukin-8en
dc.subject.meshOncogene Protein v-akten
dc.subject.meshPhagocytosisen
dc.subject.meshPhospholipase C gammaen
dc.subject.meshProtein Kinase Cen
dc.subject.meshRNA Interferenceen
dc.subject.meshRNA, Small Interferingen
dc.subject.meshSignal Transductionen
dc.subject.meshYersinia pseudotuberculosisen
dc.subject.meshYersinia pseudotuberculosis Infectionsen
dc.titleCell invasion of Yersinia pseudotuberculosis by invasin and YadA requires protein kinase C, phospholipase C-gamma1 and Akt kinase.en
dc.typeArticleen
dc.contributor.departmentInstitut für Mikrobiologie, Technische Universität Braunschweig, 38106 Braunschweig, Germany.en
dc.identifier.journalCellular microbiologyen
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