title: Rho-dependent membrane folding causes Shigella entry into epithelial cells.
abstract: The small GTPase rho is functionally involved in the formation of cytoskeletal structures like stress fibers or focal adhesion plaques. Shigella entry into HeLa cells induces a blossom-like membrane structure at the bacterial entry site. We show here that this membrane-folding process is rho-dependent. The three rho isoforms were recruited into bacterial entry sites with differential localization relative to the membrane structure. A rho-specific inhibitor abolished Shigella-induced membrane folding and impaired bacterial entry accordingly. S1-myosin labeling indicated that rho was involved in Shigella-induced actin polymerization but not actin nucleation in the bacterial invasion site. This provides a major link in the signalization cascade allowing entry of a bacterial pathogen into a eukaryotic cell.
authors.affiliation: Unité de Pathogénie Microbienne Moléculaire, INSERM U389, Paris, France.
authors.forename: T
authors.initials: T
authors.lastname: Adam
authors.forename: M
authors.initials: M
authors.lastname: Giry
authors.forename: P
authors.initials: P
authors.lastname: Boquet
authors.forename: P
authors.initials: P
authors.lastname: Sansonetti
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism / Q000382:microbiology; D003599:Cytoskeleton / Q000378:metabolism; D004847:Epithelial Cells; D004848:Epithelium / Q000382:microbiology / Q000648:ultrastructure; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning; D008969:Molecular Sequence Data; D012760:Shigella / Q000502:physiology* / Q000648:ultrastructure
chemical_list: D007527:Isoenzymes; D020558:GTP Phosphohydrolases