Formin-mediated actin polymerization promotes Salmonella invasion

Cell Microbiol. 2013 Dec;15(12):2051-63. doi: 10.1111/cmi.12173. Epub 2013 Aug 13.


Salmonella invade host cells using Type 3 secreted effectors, which modulate host cellular targets to promote actin rearrangements at the cell surface that drive bacterial uptake. The Arp2/3 complex contributes to Salmonella invasion but is not essential, indicating other actin regulatory factors are involved. Here, we show a novel role for FHOD1, a formin family member, in Salmonella invasion. FHOD1 and Arp2/3 occupy distinct microdomains at the invasion site and control distinct aspects of membrane protrusion formation. FHOD1 is phosphorylated during infection and this modification is required for promoting bacterial uptake by host cells. ROCK II, but not ROCK I, is recruited to the invasion site and is required for FHOD1 phosphorylation and for Salmonella invasion. Together, our studies revealan important phospho-dependent FHOD1 actin polymerization pathway in Salmonella invasion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin-Related Protein 2-3 Complex / metabolism*
  • Actins
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Bacterial Secretion Systems
  • Cell Line
  • Fetal Proteins / metabolism*
  • Formins
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism*
  • Phosphorylation
  • RNA Interference
  • RNA, Small Interfering
  • Salmonella Infections / microbiology
  • Salmonella Infections / transmission*
  • Salmonella typhimurium / genetics
  • Salmonella typhimurium / pathogenicity*
  • rho-Associated Kinases / metabolism


  • Actin-Related Protein 2-3 Complex
  • Actins
  • Bacterial Proteins
  • Bacterial Secretion Systems
  • FHOD1 protein, human
  • Fetal Proteins
  • Formins
  • Nuclear Proteins
  • RNA, Small Interfering
  • SopE protein, Salmonella
  • rho-Associated Kinases
  • SopB protein, Salmonella

Associated data

  • GENBANK/Y27632