Rho-dependent Membrane Folding Causes Shigella Entry Into Epithelial Cells

EMBO J. 1996 Jul 1;15(13):3315-21.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Membrane / metabolism
  • Cell Membrane / microbiology
  • Cytoskeleton / metabolism
  • Epithelial Cells
  • Epithelium / microbiology
  • Epithelium / ultrastructure
  • GTP Phosphohydrolases / metabolism*
  • HeLa Cells
  • Humans
  • Isoenzymes / metabolism*
  • Microscopy, Electron, Scanning
  • Molecular Sequence Data
  • Shigella / physiology*
  • Shigella / ultrastructure


  • Isoenzymes
  • GTP Phosphohydrolases