VASP-dependent regulation of actin cytoskeleton rigidity, cell adhesion, and detachment

Galler, Annette; Arguinzonis, Maísa I. García; Baumgärtner, Werner; Kuhn, Monika; Smolenski, Albert; Simm, Andreas; Reinhard, Matthias

doi:10.1007/s00418-005-0091-z

Cited by 37 publications

(39 citation statements)

References 76 publications

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“…Ena/VASP proteins localize to focal adhesions, and Drosophila Ena colocalizes with integrins at ends of planar-polarized actin bundles in follicle cells (Bateman et al, 2001). Ena/VASP inactivation does not disrupt focal adhesions (Bear et al, 2000), but may modulate their size and stress fiber robustness under mechanical stress (Galler et al, 2005;Yoshigi et al, 2005). Drosophila Ena may strengthen the cytoskeleton during germband retraction, promote amnioserosal lamellipodia or regulate extracellular matrix (ECM) adhesion more directly, as VASP does in platelets (reviewed by Krause et al, 2003) and as Ena/VASP proteins may do in Xenopus somitogenesis (Kragtorp and Miller, 2006).…”

Section: Research Articlementioning

confidence: 99%

Enabled plays key roles in embryonic epithelial morphogenesis inDrosophila

et al. 2007

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Studies in cultured cells and in vitro have identified many actin regulators and begun to define their mechanisms of action. Among these are Enabled (Ena)/VASP proteins, anti-Capping proteins that influence fibroblast migration, growth cone motility, and keratinocyte cell adhesion in vitro. However, partially redundant family members in mammals and maternal Ena contribution in Drosophila previously prevented assessment of the roles of Ena/VASP proteins in embryonic morphogenesis in flies or mammals. We used several approaches to remove maternal and zygotic Ena function, allowing us to address this question. We found that inactivating Ena does not disrupt cell adhesion or epithelial organization, suggesting its role in these processes is cell type-specific. However, Ena plays an important role in many morphogenetic events, including germband retraction, segmental groove retraction and head involution, whereas it is dispensable for other morphogenetic movements. We focused on dorsal closure, analyzing mechanisms by which Ena acts. Ena modulates filopodial number and length, thus influencing the speed of epithelial zippering and the ability of cells to match with correct neighbors. We also explored filopodial regulation in cultured Drosophila cells and embryos. These data provide new insights into developmental and mechanistic roles of this important actin regulator.

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Section: Research Articlementioning

confidence: 99%

Enabled plays key roles in embryonic epithelial morphogenesis inDrosophila

et al. 2007

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“…Further studies of Abl action will be needed to clarify the mechanisms by which it downregulates Ena. Interestingly, manipulating mammalian Ena/VASP can affect cell contractility (Galler et al, 2006;Hoffman et al, 2006). Thus, Enadownregulation may permit proper VF cell contractility.…”

Section: Research Articlementioning

confidence: 99%

Abelson kinase (Abl) and RhoGEF2 regulate actin organization during cell constriction inDrosophila

2007

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Morphogenesis involves the interplay of different cytoskeletal regulators. Investigating how they interact during a given morphogenetic event will help us understand animal development. Studies of ventral furrow formation, a morphogenetic event during Drosophila gastrulation, have identified a signaling pathway involving the G-protein Concertina (Cta) and the Rho activator RhoGEF2. Although these regulators act to promote stable myosin accumulation and apical cell constriction, loss-of-function phenotypes for each of these pathway members is not equivalent, suggesting the existence of additional ventral furrow regulators. Here, we report the identification of Abelson kinase (Abl) as a novel ventral furrow regulator. We find that Abl acts apically to suppress the accumulation of both Enabled (Ena) and actin in mesodermal cells during ventral furrow formation. Further, RhoGEF2 also regulates ordered actin localization during ventral furrow formation, whereas its activator, Cta, does not. Taken together, our data suggest that there are two crucial preconditions for apical constriction in the ventral furrow: myosin stabilization/activation, regulated by Cta and RhoGEF2; and the organization of apical actin, regulated by Abl and RhoGEF2. These observations identify an important morphogenetic role for Abl and suggest a conserved mechanism for this kinase during apical cell constriction.

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“…The adhesive ability of tumor cells to the extracellular matrix (ECM) may be an important event in the progression to metastasis (28). VASP possesses an important role in the regulation of cell adhesion (29). Previous studies have established that HIF-1α binds to the VASP promoter and this inhibits VASP transcription, which suppresses cell adhesion (24).…”

Section: Il-17 Augments Tnf-α-induced Hif-1 α Gene Expression In Mda-mentioning

confidence: 99%

Interleukin-17 augments tumor necrosis factor α-mediated increase of hypoxia-inducible factor-1α and inhibits vasodilator-stimulated phosphoprotein expression to reduce the adhesion of breast cancer cells

Kuang

et al. 2017

Oncology Letters

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Abstract. and tumor necrosis factor (TNF)-α are able to cooperatively alter the expression levels of a number of genes. In the present study, the mRNA expression levels of hypoxia-inducible factor (HIF)-1α were analyzed in MDA-MB-231 breast cancer cells following treatment with IL-17, TNF-α or the combination of IL-17 and TNF-α. The protein expression levels of HIF-1α and vasodilator-stimulated phosphoprotein (VASP) were evaluated using western blot analysis. The adhesive ability of the cells was determined using an MTT assay following treatment with HIF-1α-small interfering RNA and short hairpin RNA-VASP that were used to suppress the expression levels of HIF-1α and VASP protein, respectively. These results demonstrated that IL-17 augmented TNF-α-induced gene expression of HIF-1α. The combination of IL-17 and TNF-α promoted an increase in HIF-1α expression and a decrease in VASP expression and a reduction in the adhesive ability of cells. These results demonstrated that IL-17 effectively enhanced the TNF-α-induced increase in HIF-1α and inhibited VASP expression, thus reducing the adhesion of MDA-MB-231 cells.

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VASP-dependent regulation of actin cytoskeleton rigidity, cell adhesion, and detachment

Cited by 37 publications

References 76 publications

Enabled plays key roles in embryonic epithelial morphogenesis inDrosophila

Enabled plays key roles in embryonic epithelial morphogenesis inDrosophila

Abelson kinase (Abl) and RhoGEF2 regulate actin organization during cell constriction inDrosophila

Interleukin-17 augments tumor necrosis factor α-mediated increase of hypoxia-inducible factor-1α and inhibits vasodilator-stimulated phosphoprotein expression to reduce the adhesion of breast cancer cells

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