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Capping of actin filaments by vinculin activated by the Shigella IpaA carboxyl‐terminal domain
Author(s) -
Ramarao Nalini,
Le Clainche Christophe,
Izard Tina,
Bourdet-Sicard Raphaëlle,
Ageron Elisabeth,
Sansonetti Philippe J.,
Carlier Marie-France,
Tran Van Nhieu Guy
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.01.057
Subject(s) - vinculin , actin , shigella flexneri , microbiology and biotechnology , chemistry , cytoskeleton , shigella , biophysics , biology , cell , biochemistry , escherichia coli , gene
Shigella , the causative agent of bacillary dysentery, invades epithelial cells. Upon bacterial–cell contact, the type III bacterial effector IpaA binds to the cytoskeletal protein vinculin to promote actin reorganization required for efficient bacterial uptake. We show that the last 74 C‐terminal residues of IpaA (A559) bind to human vinculin (HV) and promotes its association with actin filaments. Polymerisation experiments demonstrated that A559 was sufficient to induce HV‐dependent partial capping of the barbed ends of actin filaments. These results suggest that IpaA regulates actin polymerisation/depolymerisation at sites of Shigella invasion by modulating the barbed end capping activity of vinculin.