Involvement of c-Src Tyrosine Kinase Upstream of Class I Phosphatidylinositol (PI) 3-Kinases in Salmonella Enteritidis Rck Protein-mediated Invasion

Journal of Biological Chemistry - Tập 287 - Trang 31148 - 2012
Elisabeth Bottreau1,2, Manon Rosselin1, Lily Mijouin1, Agnès Wiedemann2,1, Philippe Velge1,2
1UMR 1282 Infectiologie et Santé Publique, Institut National de la Recherche Agronomique (INRA), F-37380 Nouzilly
2UMR 1282 Infectiologie et Santé Publique, Université François Rabelais de Tours, F-37000 Tours, France

Tóm tắt

The Salmonella outer membrane protein Rck mediates a Zipper entry mechanism controlled by tyrosine phosphorylation and class I phosphatidylinositol 3-kinase (PI 3-kinase). However, the underlying mechanism leading to this signaling cascade remains unclear. The present study showed that using Rck-coated beads or Rck-overexpressing Escherichia coli, Rck-mediated actin polymerization and invasion were blocked by PP2, a Src family tyrosine kinase inhibitor. In addition, phosphorylation of Src family kinases significantly increased after stimulation with Rck. The specific contribution of c-Src, one member of the Src family kinases, was demonstrated using c-Src-deficient fibroblasts or c-Src siRNA transfected epithelial cells. We also observed that Rck-mediated internalization led to the formation of a complex between c-Src and at least one tyrosine-phosphorylated protein. Furthermore, our results revealed that the c-Src signal molecule was upstream of PI 3-kinase during the Rck-mediated signaling pathway as Rck-mediated PI 3-kinase activation was blocked by PP2, and PI 3-kinase inhibitor had no effect on the Src phosphorylation. These results demonstrate the involvement of c-Src upstream of the PI 3-kinase in the Zipper entry process mediated by Rck.

Từ khóa

#Microbiology #Signaling #siRNA #Src #Tyrosine Protein Kinase (Tyrosine Kinase)

Tài liệu tham khảo

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