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- W2046230501 abstract "IpaC of Shigella is essential for initial bacterial entry into epithelial cells. We report here that IpaC interacts with beta-catenin and destabilizes the cadherin-mediated cell adhesion complex. Using a yeast two-hybrid system, we identified beta-catenin as a binding partner of IpaC within the host cell after cell entry, but not in the initial entry. Co-immunoprecipitation, confocal microscopy, and GST pull-down experiments confirmed the intracellular and cell-free interactions between these two proteins. The interaction sites were mapped to the ninth armadillo repeat of beta-catenin and to the C-terminus of IpaC. IpaC-associated beta-catenin was phosphorylated at tyrosine residues. This phosphorylation led to the destabilization of the functional cadherin-catenin complex, which could be a mechanism whereby the epithelial cell-cell tight adhesion is disrupted. These events may facilitate the further basolateral invasion of bacteria through the disrupted space and/or modulate the cell-to-cell spread of Shigella." @default.
- W2046230501 created "2016-06-24" @default.
- W2046230501 creator A5010867165 @default.
- W2046230501 creator A5029447023 @default.
- W2046230501 creator A5036891831 @default.
- W2046230501 date "2003-09-01" @default.
- W2046230501 modified "2023-10-18" @default.
- W2046230501 title "IpaC of Shigella binds to the C-terminal domain of β-catenin" @default.
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- W2046230501 doi "https://doi.org/10.1016/s0882-4010(03)00093-7" @default.
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