Functional roles of VASP phosphorylation in the regulation of chemotaxis and osmotic stress response

Lin, Wan-Hsin; Nelson, Sharon E.; Hollingsworth, Ryan J.; Chung, Chang Y.

doi:10.1002/cm.20443

Cited by 7 publications

(3 citation statements)

References 60 publications

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“…This is not particularly surprising given that cell movement is a complex and cell type–dependent process and that VASP is involved in many actin-dependent processes ( Bear and Gertler, 2009 ). In contrast to random cell migration, little is known about the role of VASP in chemotaxis, and most studies were conducted either in slime mold ( Han et al, 2002 ; Lin et al, 2010 ) or in cell lines overexpressing chemokine receptors ( Neel et al, 2009 ).…”

Section: Discussionmentioning

confidence: 99%

VASP regulates leukocyte infiltration, polarization, and vascular repair after ischemia

Laban

Weigert

Zink

et al. 2018

Journal of Cell Biology

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Section: Discussionmentioning

confidence: 99%

VASP regulates leukocyte infiltration, polarization, and vascular repair after ischemia

Laban

Weigert

Zink

et al. 2018

Journal of Cell Biology

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“…The actin regulatory functions of VASP are highly sensitive to salt concentrations, which suggests that the phosphorylation of VASP could dramatically affect the actin regulatory activity. Of the three VASP conservative phosphorylation sites (Ser-157, Ser-239, and Thr-278), only the phosphorylation of Ser-157 led to a shift in the apparent molecular mass from 46 to 50 kDa, indicating that this phosphorylation might cause a change in the secondary structure of the molecule [26,27] . Our data showed that the far-UV CD spectra that corresponded to the VASP secondary structure were sensitive to the concentration of matrine.…”

Section: Discussionmentioning

confidence: 99%

Matrine inhibits the adhesion and migration of BCG823 gastric cancer cells by affecting the structure and function of the vasodilator-stimulated phosphoprotein (VASP)

Zhang

Shi

et al. 2013

Acta Pharmacol Sin

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Aim: Vasodilator-stimulated phosphoprotein (VASP) expression is upregulated in human cancers and correlates with more invasive advanced tumor stages. The aim of this study was to elucidate the mechanisms by which matrine, an alkaloid derived from Sophora species plants, acted on the VASP protein in human gastric cancer cells in vitro. Methods: VASP was expressed and purified. Intrinsic fluorescence spectroscopy was used to study the binding of matrine to VASP. CD spectroscopy was used to examine the changes in the VASP protein secondary structure. Human gastric carcinoma cell line BGC823 was tested. Scratch wound and cell adhesion assays were used to detect the cell migration and adhesion, respectively. Real-time PCR and Western blotting assays were used to measure mRNA and protein expression of VASP. Results: In the fluorescence assay, the dissociation constant for binding of matrine to VASP protein was 0.86 mmol/L, thus the direct binding between the two molecules was weak. However, matrine (50 μg/mL) caused obvious change in the secondary structure of VASP protein shown in CD spectrum. Treatments of BGC823 cells with matrine (50 μg/mL) significantly inhibited the cell migration and adhesion. The alkaloid changed the subcellular distribution of VASP and formation of actin stress fibers in BGC823 cells. The alkaloid caused small but statistically significant decreases in VASP protein expression and phosphorylation, but had no significant effect on VASP mRNA expression. Conclusion: Matrine modulates the structure, subcellular distribution, expression and phosphorylation of VASP in human gastric cancer cells, thus inhibiting the cancer cell adhesion and migration.

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“…39,41 DdVASP expression occurs in vegetative cells and increases with starvation peaking at 8 h. 39 Phosphorylation of VASP is important for its cortical localization and interaction with WASP and WIPa that are key regulators of F-actin organization. 42 Lin and co-workers 42 showed that VASP phosphorylation still occurs in Dictyostelium null strains of the PKA catalytic domain ( pka-cat À ) and of guanylyl cyclases (sgc/gca À ). Furthermore, no VASP phosphorylation was observed in cells treated with membranepermeable derivatives of cAMP and cGMP.…”

Section: Discussionmentioning

confidence: 99%

Intracellular photoactivation of caged cGMP induces myosin II and actin responses in motile cells

et al. 2013

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Cyclic GMP (cGMP) is a ubiquitous second messenger in eukaryotic cells. It is assumed to regulate the association of myosin II with the cytoskeleton of motile cells. When cells of the social amoeba Dictyostelium discoideum are exposed to chemoattractants or to increased osmotic stress, intracellular cGMP levels rise, preceding the accumulation of myosin II in the cell cortex. To directly investigate the impact of intracellular cGMP on cytoskeletal dynamics in a living cell, we released cGMP inside the cell by laser-induced photo-cleavage of a caged precursor. With this approach, we could directly show in a live cell experiment that an increase in intracellular cGMP indeed induces myosin II to accumulate in the cortex. Unexpectedly, we observed for the first time that also the amount of filamentous actin in the cell cortex increases upon a rise in the cGMP concentration, independently of cAMP receptor activation and signaling. We discuss our results in the light of recent work on the cGMP signaling pathway and suggest possible links between cGMP signaling and the actin system. Insight, innovation, integrationSecond messengers like cGMP play a central role in the regulatory pathways of living cells. Here, we demonstrate that an increase in intracellular cGMP can trigger not only myosin II but also actin responses in motile amoeboid cells. In previous studies, an increase in intracellular cGMP was induced indirectly via membrane receptor stimulation. In the present work, we employ, for the first time, the direct light-induced release of cGMP from a caged precursor to raise the cytosolic cGMP level in Dictyostelium cells that carry fluorescent markers for filamentous actin and myosin II. Based on this advanced combination of live cell photo-uncaging and multi-color confocal microscopy, we could identify a link between cGMP and actin dynamics in motile amoeboid cells.

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Functional roles of VASP phosphorylation in the regulation of chemotaxis and osmotic stress response

Cited by 7 publications

References 60 publications

VASP regulates leukocyte infiltration, polarization, and vascular repair after ischemia

VASP regulates leukocyte infiltration, polarization, and vascular repair after ischemia

Matrine inhibits the adhesion and migration of BCG823 gastric cancer cells by affecting the structure and function of the vasodilator-stimulated phosphoprotein (VASP)

Intracellular photoactivation of caged cGMP induces myosin II and actin responses in motile cells

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