Shigella actin-based motility in the absence of vinculin

Goldberg, Marcia B.

doi:10.1002/(sici)1097-0169(1997)37:1<44::aid-cm5>3.0.co;2-h

Cited by 35 publications

(17 citation statements)

References 41 publications

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“…Although we have discussed an important role for vinculin in Shigella actinbased motility, there have been two controversial reports on the requirement for vinculin. Goldberg (1997) examined the functional role of vinculin in Shigella actin-based motility in a vinculin-deficient F9 cell line variant 5.51, and observed that Shigella are able to form actin tails and are motile as in the F9 cells, suggesting that vinculin is not the essential factor. In contrast, Laine et al (1997) found that vinculin proteolysis occurred in Shigellainfected cells and that the cleaved head portion of vinculin is a rate-limiting factor in Shigella motility.…”

Section: Discussionmentioning

confidence: 99%

Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri

et al. 1998

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Section: Discussionmentioning

confidence: 99%

Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri

et al. 1998

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“…Bacterial entry was analysed by gentamicin protection assays, performed as described previously (Way et al, 1998). In all other experiments, Shigella infection of mammalian cells was performed as described previously (Goldberg, 1997). In brief, exponential phase bacteria were centrifuged at 700 g for 10 min onto semi-confluent monolayers of cells that had been seeded onto cover glasses in six-well plates, using a multiplicity of infection (MOI) of 100:1.…”

Section: Bacterial Infection Of Cellsmentioning

confidence: 99%

“…Vinculin is not required to reconstitute IcsA-mediated motility using purified cytoskeletal proteins , indicating that it is not essential, but not ruling out the possibility that it contributes to maximal efficiency of actin assembly. Actin-based motility of Shigella in F9 5.51 cells, which are deficient in vinculin, is no different from that in the vinculin-expressing parent cell line (Goldberg, 1997). However, small amounts of truncated vinculin can be detected in F9 5.51 cells, leading other investigators to suggest that the small amount of truncated protein is © 2004 Blackwell Publishing Ltd, Cellular Microbiology , 6 , 355-366 sufficient for efficient actin assembly by Shigella (Southwick et al ., 2000).…”

Section: Introductionmentioning

confidence: 99%

Shigella interactions with the actin cytoskeleton in the absence of Ena/VASP family proteins

Ally

Sauer

Loureiro

et al. 2004

Cellular Microbiology

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Shigella move 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 intracellular Shigella. VASP binds both profilin, an actin monomer-binding protein, and vinculin, a component of intercellular contacts that also binds the Shigella actin assembly protein IcsA. It has been postulated that VASP might serve as a linker between vinculin and profilin on intracellular Shigella, thereby delivering profilin to the Shigella actin assembly machinery. We show that Shigella actin-based motility is unaltered in cells that are deficient for the Ena/VASP family of proteins. In these cells, Shigella form 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 to Shigella is not correlated with vinculin recruitment, indicating that the role of vinculin in Shigella motility is not recruitment of Arp2/3. Thus, although VASP is recruited to the surface of intracellular Shigella, it is not essential for Shigella actin-based motility.

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“…It has been reported that infection of cells by Shigella leads to a recruitment of vinculin by IcsA followed by a cleavage of vinculin, which is then able to recruit VASP (Laine et al, 1997). However, the role of vinculin remains controversial as Shigella motility proceeds normally in vinculin-negative cells (Goldberg, 1997).…”

Section: Icsa Ligandsmentioning

confidence: 99%

Actin-based motility of pathogens: the Arp2/3 complex is a central player. Microreview

Cossart

2000

Cell Microbiol

130

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Bacterial actin‐based motility has provided cell biologists with tools that led to the recent discovery that, in many forms of actin‐based motilities, a key player is a protein complex named the Arp2/3 complex. The Arp2/3 complex is evolutionally conserved and made up of seven polypeptides involved in both actin filament nucleation and organization. Interestingly, this complex is inactive by itself and recent work has highlighted the fact that its activation is achieved differently in the different types of actin‐based motilities, including the well‐known examples of Listeria and Shigella motilities. Proteins of the WASP family and small G‐proteins are involved in most cases. It is interesting that bacteria bypass or mimic some of the events occurring in eukaryotic systems. The Shigella protein IcsA recruits N‐WASP and activates it in a Cdc42‐like fashion. This activation leads to Arp2/3 complex recruitment, activation of the complex and ultimately actin polymerization and movement. The Listeria ActA protein activates Arp2/3 directly and, thus, seems to mimic proteins of the WASP family. A breakthrough in the field is the recent reconstitution of the actin‐based motilities of Listeria and N‐WASP‐coated E. coli (IcsA) using a restricted number of purified cellular proteins including F‐actin, the Arp2/3 complex, actin depolymerizing factor (ADF or cofilin) and capping protein. The movement was more effective upon addition of profilin, α‐actinin and VASP (for Listeria). Bacterial actin‐based motility is now one of the best‐documented examples of the exploitation of mammalian cell machineries by bacterial pathogens.

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Shigella actin-based motility in the absence of vinculin

Cited by 35 publications

References 41 publications

Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri

Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri

Shigella interactions with the actin cytoskeleton in the absence of Ena/VASP family proteins

Actin-based motility of pathogens: the Arp2/3 complex is a central player. Microreview

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