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Binding of the Shigella protein IpaA to vinculin induces F‐actin depolymerization
Author(s) -
BourdetSicard Raphaëlle,
Rüdiger Manfred,
Jockusch Brigitte M.,
Gou Pierre,
Sansonetti Philippe J.,
Tran Van Nhieu Guy
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.21.5853
Subject(s) - vinculin , biology , actin , shigella flexneri , microbiology and biotechnology , biophysics , focal adhesion , biochemistry , signal transduction , escherichia coli , gene
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.