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• W2012153529 startingPage "5853" @default.
• W2012153529 abstract "Shigella flexneri, the causative agent of bacillary dysentery, enters into epithelial cells by a macropinocytic process. IpaA, a Shigella protein secreted upon cell contact, binds to the focal adhesion protein vinculin and is required for efficient bacterial uptake. IpaA was shown here to bind with high affinity to the N-terminal residues 1-265 of vinculin. Using co-sedimentation and solid-phase assays, we demonstrated that binding of IpaA to vinculin strongly increases the association of vinculin with F-actin. We also characterized a depolymerizing activity on actin filaments associated with the vinculin-IpaA complex both in vitro and in microinjected cells. We propose that the conformational change of vinculin induced by IpaA binding allows interaction of the vinculin-IpaA complex with F-actin and subsequent depolymerization of actin filaments." @default.
• W2012153529 created "2016-06-24" @default.
• W2012153529 creator A5031844194 @default.
• W2012153529 date "1999-11-01" @default.
• W2012153529 modified "2023-10-18" @default.
• W2012153529 title "Binding of the Shigella protein IpaA to vinculin induces F-actin depolymerization" @default.
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• W2012153529 doi "https://doi.org/10.1093/emboj/18.21.5853" @default.
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