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The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion.

Thwaites T, Nogueira AT, Campeotto I, Silva AP, Grieshaber SS, Carabeo RA - J. Biol. Chem. (2014)

Bottom Line: The conserved leucine residues within the L(D/E)XLLXXL motif were essential to the recruitment of FAK, Cdc42, p34(Arc), and actin to the plasma membrane.In the absence of FAK, TarP-LD-mediated F-actin assembly was reduced, highlighting the functional relevance of this interaction.Together, the data indicate that a prokaryotic version of the paxillin LD2 domain targets the FAK signaling pathway, with TarP representing the first example of an LD-containing Type III virulence effector.

View Article: PubMed Central - PubMed

Affiliation: From the Centre for Molecular Microbiology and Infection, Imperial College, London SW7 2AZ, United Kingdom, Bacteriology Section, Programme in Microbiology, Institute of Medical Sciences, School of Medical Sciences, University of Aberdeen, Aberdeen AB25 2ZD, United Kingdom, and.

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The TarP-LD domain mediates Arp2/3 complex and actin remodeling.A, Cos7 cells expressing TirM-TarP-LD or the negative control TirM were infected with Δtir EPEC to induce clustering. Transfected cells were identified by their ability to recruit actin (red) and pY397-FAK (green). The white arrowheads indicate colocalization of Δtir EPEC, pY397-FAK, and actin. B, as above except p34Arc (green) colocalization with bacteria and actin was monitored. Scale bars, 10 μm. Insets show a magnification of a selected area of the cell.
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Figure 6: The TarP-LD domain mediates Arp2/3 complex and actin remodeling.A, Cos7 cells expressing TirM-TarP-LD or the negative control TirM were infected with Δtir EPEC to induce clustering. Transfected cells were identified by their ability to recruit actin (red) and pY397-FAK (green). The white arrowheads indicate colocalization of Δtir EPEC, pY397-FAK, and actin. B, as above except p34Arc (green) colocalization with bacteria and actin was monitored. Scale bars, 10 μm. Insets show a magnification of a selected area of the cell.

Mentions: Using the EPEC system described above, we investigated if TarP-LD could recruit actin and the Arp2/3 complex. Cells expressing TarP-LD or the negative control TirM were infected with Δtir EPEC, and the samples were stained with fluorescent phalloidin to visualize recruited actin. From confocal images, actin assembly in cells expressing TirM-LD was observed, which was in contrast to cells expressing TirM alone (Fig. 6A). Furthermore, we observed >75% coincidence of pY397-FAK or p34Arc with actin (Fig. 6, A and B), supporting a signaling related recruitment of actin.


The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion.

Thwaites T, Nogueira AT, Campeotto I, Silva AP, Grieshaber SS, Carabeo RA - J. Biol. Chem. (2014)

The TarP-LD domain mediates Arp2/3 complex and actin remodeling.A, Cos7 cells expressing TirM-TarP-LD or the negative control TirM were infected with Δtir EPEC to induce clustering. Transfected cells were identified by their ability to recruit actin (red) and pY397-FAK (green). The white arrowheads indicate colocalization of Δtir EPEC, pY397-FAK, and actin. B, as above except p34Arc (green) colocalization with bacteria and actin was monitored. Scale bars, 10 μm. Insets show a magnification of a selected area of the cell.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4215226&req=5

Figure 6: The TarP-LD domain mediates Arp2/3 complex and actin remodeling.A, Cos7 cells expressing TirM-TarP-LD or the negative control TirM were infected with Δtir EPEC to induce clustering. Transfected cells were identified by their ability to recruit actin (red) and pY397-FAK (green). The white arrowheads indicate colocalization of Δtir EPEC, pY397-FAK, and actin. B, as above except p34Arc (green) colocalization with bacteria and actin was monitored. Scale bars, 10 μm. Insets show a magnification of a selected area of the cell.
Mentions: Using the EPEC system described above, we investigated if TarP-LD could recruit actin and the Arp2/3 complex. Cells expressing TarP-LD or the negative control TirM were infected with Δtir EPEC, and the samples were stained with fluorescent phalloidin to visualize recruited actin. From confocal images, actin assembly in cells expressing TirM-LD was observed, which was in contrast to cells expressing TirM alone (Fig. 6A). Furthermore, we observed >75% coincidence of pY397-FAK or p34Arc with actin (Fig. 6, A and B), supporting a signaling related recruitment of actin.

Bottom Line: The conserved leucine residues within the L(D/E)XLLXXL motif were essential to the recruitment of FAK, Cdc42, p34(Arc), and actin to the plasma membrane.In the absence of FAK, TarP-LD-mediated F-actin assembly was reduced, highlighting the functional relevance of this interaction.Together, the data indicate that a prokaryotic version of the paxillin LD2 domain targets the FAK signaling pathway, with TarP representing the first example of an LD-containing Type III virulence effector.

View Article: PubMed Central - PubMed

Affiliation: From the Centre for Molecular Microbiology and Infection, Imperial College, London SW7 2AZ, United Kingdom, Bacteriology Section, Programme in Microbiology, Institute of Medical Sciences, School of Medical Sciences, University of Aberdeen, Aberdeen AB25 2ZD, United Kingdom, and.

Show MeSH
Related in: MedlinePlus