Open AccessShigella interactions with the actin cytoskeleton in the absence of Ena/VASP family proteins
Author(s) -
Ally Shabeen,
Sauer Noel J.,
Loureiro Joseph J.,
Snapper Scott B.,
Gertler Frank B.,
Goldberg Marcia B.
Publication year - 2004
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1046/j.1462-5822.2003.00359.x
Subject(s) - vinculin , profilin , biology , microbiology and biotechnology , shigella flexneri , actin , shigella , actin cytoskeleton , actin remodeling , cytoskeleton , biochemistry , focal adhesion , signal transduction , bacteria , cell , genetics , escherichia coli , salmonella , gene
Summary Shigellamove through the cytosol of infected cells by assembly of a propulsive actin tail at one end of the bacterium. Vasodilator‐stimulated phosphoprotein (VASP), a member of the Ena/VASP family of proteins, is important in cellular actin dynamics and is present on intracellularShigella. VASP binds both profilin, an actin monomer‐binding protein, and vinculin, a component of intercellular contacts that also binds theShigellaactin assembly protein IcsA. It has been postulated that VASP might serve as a linker between vinculin and profilin on intracellularShigella, thereby delivering profilin to theShigellaactin assembly machinery. We show thatShigellaactin‐based motility is unaltered in cells that are deficient for the Ena/VASP family of proteins. In these cells,Shigellaform normal‐appearing actin tails and move at rates that are comparable to the rates of bacterial movement in Ena/VASP‐deficient cells complemented with the Ena/VASP family member Mena. Finally, whereas vinculin can bind the Arp2/3 complex, we show that Arp2/3 recruitment toShigellais not correlated with vinculin recruitment, indicating that the role of vinculin inShigellamotility is not recruitment of Arp2/3. Thus, although VASP is recruited to the surface of intracellularShigella, it is not essential forShigella actin‐based motility.