Rho-dependent membrane folding causes Shigella entry into epithelial cells.
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.
Adam
T
T
Unité de Pathogénie Microbienne Moléculaire, INSERM U389, Paris, France.
Giry
M
M
Boquet
P
P
Sansonetti
P
P
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
D007527:Isoenzymes; D020558:GTP Phosphohydrolases