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Results: 5

1.

Figure. From: Paxillin controls directional cell motility in response to physical cues.

Figure 1. (A) Wild-type human lung IMR-90 fibroblasts plated on 50 μm2 fibronectin islands in serum-free medium. F-actin was labeled with Alexa-488 phalloidin (green) and FA proteins (vinculin and paxillin) were labeled by immunostaining. (B) Wild-type mouse embryonic fibroblast on a 50 μm2 fibronectin island, stimulated with PDGF (25 ng/ml) for 30 min. F-actin was labeled with Alexa-488 phalloidin and vinculin was labeled by immunostaining.

Julia E. Sero, et al. Cell Adh Migr. 2012 November 1;6(6):502-508.
2.

Figure. From: Paxillin controls directional cell motility in response to physical cues.

Figure 3. Paxillin domains and interacting proteins. Top: Paxillin protein domains. The regions comprising paxN and paxC mutant constructs are indicated. Bottom: Paxillin-protein interactions and phosphorylation sites. Tyr31 and Tyr118, targets of Src and FAK that provide binding sites for CrkII and p120RasGAP, are indicated by red arrows. Serine phosphorylation sites, including the PAK target site Ser273, are indicated by yellow arrows. Phosphorylation at this site alters affinity for FAK, Git1 and Pkl. For a review of paxillin-protein interactions, see Deakin and Turner (2008). 8

Julia E. Sero, et al. Cell Adh Migr. 2012 November 1;6(6):502-508.
3.

Figure. From: Paxillin controls directional cell motility in response to physical cues.

Figure 5. (A) Schematic of a modified matrigel plug assay. Matrigel is cast in a 7 × 7 × 2 mm PDMS mold inside a 4 mm well and implanted on a mouse back for 7–14 d. Paxillin siRNA or DNA (10 μg) is injected locally at day 3. (B) Micrograph of hematoxylin and eosin-stained implant/skin section after 7 d. Skin is shown above the dotted line and matrigel with host cells is shown below the dotted line. Scale bar = 50 µm.

Julia E. Sero, et al. Cell Adh Migr. 2012 November 1;6(6):502-508.
4.

Figure. From: Paxillin controls directional cell motility in response to physical cues.

Figure 2. (A) Time-course of the motile response to PDGF (25 ng/ml) stimulation in wild type (pax+) mouse embryonic fibroblasts (MEFs). Cells were fixed without (0 min) and at 5, 10, 15 and 30 min after addition of PDGF and stained with Alexa-488 phalloidin to label F-actin. (B) Pax+ and pax−/− MEFs stimulated with PDGF for 30 min, fixed and stained with Alexa-488 phalloidin. (C) Vinculin labeling by immunofluorescence in serum-starved pax+ and pax−/− cells on square islands showing differences in FA distribution. (D) Pax+ MEF fixed 5 min after addition of PDGF and stained for F-actin and paxillin showing large circular dorsal ruffles (CDRs). (E) Phase-contrast time-lapse video of live pax−/− MEFs stimulated with PDGF (20X). Formation of CDRs (green arrows) persisted for more than 15 min and protrusions were internalized into macropinocytic vesicles (blue arrows) by about 20 min. In pax+ cells, CDR formation and internalization was complete by 10 min after addition of PDGF.

Julia E. Sero, et al. Cell Adh Migr. 2012 November 1;6(6):502-508.
5.

Figure. From: Paxillin controls directional cell motility in response to physical cues.

Figure 4. Model of the effects of paxillin and paxillin mutants on lamellipodia formation in square cells. The square, representing a shape-constrained cell, is divided into four quadrants, which correspond to paxillin−/−, paxillin+/+, paxN and paxC cell conditions. In control (pax+) cells (top right), paxillin may bind cytosolic or membrane-bound Rac-activating complexes and recruit them to focal adhesion (FA) sites. For example, upon PDGF receptor activation paxillin could bind Pkl-PIX-PAK complexes containing Arf6-GTP and Rac-GTP and deliver them to corner regions to promote localized lamellipodia formation. In paxillin−/− cells (top left), some active Rac complexes may drive limited, non-localized lamellipodia extension at the cell periphery, but delivery from endosomal compartments to the plasma membrane may be impaired. The C-terminal paxC fragment (bottom left) could compete with Hic-5, PTP-PEST or Rac inhibiting proteins, promoting enhanced lamellipodia formation even in the absence of growth factors. Conversely, the N-terminal paxN fragment (bottom right) could sequester Rac-activating proteins and lamellipodia machinery in the cytosol. The small, spiky protrusions in these cells could be driven by Cdc42 or RhoA instead of by Rac.

Julia E. Sero, et al. Cell Adh Migr. 2012 November 1;6(6):502-508.

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