Affinage

VASP

Vasodilator-stimulated phosphoprotein · UniProt P50552

Length
380 aa
Mass
39.8 kDa
Annotated
2026-06-11
100 papers in source corpus 52 papers cited in narrative 52 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

VASP is a tetrameric actin polymerase that drives barbed-end filament elongation at sites of dynamic actin assembly—leading-edge lamellipodia, filopodial tips, focal adhesions, and cell-cell junctions—coupling membrane signaling to cytoskeletal remodeling (PMID:7828592, PMID:12086607, PMID:32391788). The native protein is an elongated homotetramer organized into an N-terminal EVH1 domain that docks onto proline-rich FP4/polyproline motifs in scaffolds, a central proline-rich region binding profilin, and a C-terminal EVH2 domain that mediates both actin engagement and tetramerization and is required for focal-adhesion targeting and motility function (PMID:7737110, PMID:7828592, PMID:9693373, PMID:12134088). Mechanistically, VASP associates with growing barbed ends and shields them from capping protein, yielding longer, less-branched filaments; clustering on membranes converts this into processive, capping-resistant elongation in which one tetramer arm tracks the barbed end while the other arms recruit and deliver G-actin through their WH2/GAB motifs, an activity that does not require actin ATP hydrolysis and depends on tetramer formation (PMID:12086607, PMID:15939738, PMID:18923426, PMID:21217643, PMID:28667124). EVH1-mediated recruitment by zyxin, vinculin, lamellipodin, RIAM, palladin, migfilin, IRSp53, and the WAVE-regulatory-complex subunit Abi positions and clusters VASP at distinct actin structures, with CDC42-activated and PIP2-clustered IRSp53 and actin-filament-bound lamellipodin both enhancing its polymerase activity (PMID:9560340, PMID:9693373, PMID:15469845, PMID:15469846, PMID:16505170, PMID:16531412, PMID:24076653, PMID:25203209, PMID:26295568, PMID:36240267). VASP function is gated by differential phosphorylation: Ser157 (PKA, PKC, Rho kinase, PKD1) primarily controls localization, Ser239 (PKG) and Thr278 (AMPK) reduce actin-assembly activity, and Tyr39 (Abl) reduces zyxin binding and focal-adhesion targeting (PMID:8182057, PMID:16197368, PMID:19825941, PMID:22014333, PMID:23846685). As a downstream effector of cyclic-nucleotide signaling, VASP mediates cAMP/cGMP-dependent inhibition of platelet aggregation, maintains endothelial barrier integrity through αII-spectrin complexes and Rac1 activation, and modulates Rac1/PAK and Rap1b pathways (PMID:9878048, PMID:12055190, PMID:18195108, PMID:19118163, PMID:27620165). VASP also forms liquid-like condensates within which polymerizing actin is organized into parallel filament bundles (PMID:38405682).

Mechanistic history

Synthesis pass · year-by-year structured walk · 23 steps
  1. 1994 High

    Established VASP as a multi-site phosphorylation substrate of both PKA and PKG, defining the regulatory residues (Ser157, Ser239, Thr278) that would later be mapped to distinct functions.

    Evidence In vitro kinase assays with site mapping by HPLC peptide sequencing and 32P labeling in intact platelets

    PMID:8182057

    Open questions at the time
    • Did not establish the functional consequence of each phosphorylation site
    • Kinase identities for each site under physiological stimuli not resolved
  2. 1995 High

    Defined VASP's tripartite domain architecture, homotetrameric structure, and direct binding to profilin, linking VASP to the actin monomer supply and identifying the EVH2 domain as essential for focal-adhesion targeting.

    Evidence Molecular cloning, hydrodynamic analysis of purified protein, profilin affinity chromatography, and truncation-mutant immunofluorescence in BHK21 cells

    PMID:7737110 PMID:7828592

    Open questions at the time
    • Did not directly demonstrate actin polymerase activity
    • Mechanism of how EVH2 mediates focal-adhesion targeting not resolved
  3. 1998 High

    Showed VASP is recruited to focal adhesions and bacterial surfaces via EVH1 binding to proline-rich motifs in scaffolds (zyxin, vinculin, ActA) and established functional conservation with Drosophila Ena.

    Evidence Co-immunoprecipitation, PIP2 binding assays, in vitro binding, and Drosophila genetic rescue with EVH1/EVH2 mutants

    PMID:9560340 PMID:9693373

    Open questions at the time
    • Did not define the actin-regulatory output of these recruitment events
    • Hierarchy among competing EVH1 ligands not addressed
  4. 1999 High

    Demonstrated VASP is required for actin-based motility and that Ser157 phosphorylation modulates F-actin affinity, while genetic knockout pinned VASP specifically to cyclic-nucleotide-dependent inhibition of platelet aggregation.

    Evidence In vitro Listeria motility with VASP immunodepletion/add-back, affinity measurements, and platelet assays in VASP-null mice

    PMID:10087267 PMID:9878048

    Open questions at the time
    • The molecular mechanism linking VASP to integrin function in platelets was inferred, not shown
    • How Ser157 phosphorylation alters actin engagement mechanistically unresolved
  5. 2000 High

    Resolved that Ena/VASP activity at the leading edge (not focal adhesions) negatively regulates fibroblast translocation, indicating a localization-dependent control of motility.

    Evidence Gain/loss-of-function, FP4-mitochondrial sequestration, membrane targeting, and quantitative migration assays

    PMID:10892743

    Open questions at the time
    • The biochemical basis for slowed motility was not yet defined
    • Did not reconcile negative regulation of motility with positive actin assembly
  6. 2002 High

    Defined the core actin mechanism: Ena/VASP associates with barbed ends and antagonizes capping protein, producing longer, less-branched lamellipodial filaments, with the EVH2 domain and its phosphorylation sites being the functionally essential elements.

    Evidence Electron microscopy of lamellipodial architecture, in vitro polymerization/capping assays, and null-cell complementation with Mena mutants

    PMID:12086607 PMID:12134088

    Open questions at the time
    • The processivity and clustering requirements were not yet established
    • Profilin-binding region appeared dispensable for random motility, leaving its role unclear
  7. 2004 Medium

    Identified a network of EVH1-binding scaffolds (lamellipodin, RIAM, palladin, FAT1) that recruit VASP to specific actin structures and couple it to phosphoinositide and Rap1 signaling.

    Evidence Co-IP, yeast two-hybrid, PH-domain lipid binding, peptide arrays, siRNA knockdown, and live-cell imaging

    PMID:14983521 PMID:15343270 PMID:15469845 PMID:15469846

    Open questions at the time
    • Whether scaffolds act redundantly or for distinct structures not resolved
    • Direct effect of each scaffold on VASP polymerase activity not measured at this stage
  8. 2005 High

    Mechanistically resolved anti-capping as an EVH2-intrinsic activity requiring both F-actin and G-actin binding motifs, enhanced by profilin-actin and downregulated by EVH2 phosphorylation.

    Evidence In vitro polymerization assays with multiple capping proteins, EVH2 domain mutagenesis, and PKA phosphorylation

    PMID:15939738

    Open questions at the time
    • The role of membrane clustering versus soluble activity not yet distinguished
    • Single-filament dynamics not directly visualized
  9. 2006 Medium

    Identified zyxin and migfilin as recruiters of VASP to focal/matrix adhesions and dissected the kinase pathways converging on Ser157.

    Evidence Zyxin-null fibroblasts, migfilin LPPPPPP motif mutagenesis, and site-specific phospho-antibody analysis with kinase inhibitors in platelets

    PMID:16197368 PMID:16505170 PMID:16531412

    Open questions at the time
    • Functional consequence of adhesion recruitment on actin output not fully resolved
    • Relative contribution of PKC vs Rho kinase to Ser157 under physiological agonists unclear
  10. 2007 High

    Distinguished an anti-capping-independent filopodial function, showed Ser239 phosphorylation triggers lamellipodial retraction, and established Ena/VASP requirement for endothelial F-actin, barrier function, and vascular development in vivo.

    Evidence FRAP and EVH2 mutant analysis, GFP-VASP S239A live imaging with PKG pharmacology, and triple-knockout mouse vascular phenotyping

    PMID:17475772 PMID:17684063 PMID:17998398

    Open questions at the time
    • Mechanism of stable filopodial-tip retention versus dynamic lamellipodial exchange not fully explained
    • How Ser239 phosphorylation mechanistically retracts lamellipodia unresolved
  11. 2008 High

    Demonstrated that membrane clustering converts VASP into a processive, capping-resistant elongator delivering monomers via WH2 domains, and identified the αII-spectrin interaction as the basis for VASP-dependent endothelial barrier maintenance.

    Evidence In vitro TIRF, functionalized-bead motility, EM structure, single-filament barbed-end capture, and αII-spectrin co-IP with phosphomutant rescue in VASP-null endothelial cells

    PMID:18195108 PMID:18283104 PMID:18923426

    Open questions at the time
    • How clustering geometry maps to processivity quantitatively not yet defined
    • Physiological trigger for αII-spectrin junctional assembly partly inferred
  12. 2009 High

    Assigned distinct functional consequences to each phosphosite (Ser157 localization; Ser239/Thr278 assembly inhibition, with AMPK as the Thr278 kinase) and connected VASP to chemokine receptor signaling and cAMP-mediated Rac1 activation.

    Evidence Phosphomimetic null-cell reconstitution, in vitro polymerization, CXCR2 binding/knockdown chemotaxis, and Rac1 pull-downs in VASP-null endothelial cells

    PMID:19118163 PMID:19435808 PMID:19825941

    Open questions at the time
    • Integration of the multiple phosphosites under combined stimuli not modeled
    • Direct vs indirect link between VASP and Rac1 activation not fully resolved
  13. 2010 Medium

    Connected Abl-kinase phosphorylation of lamellipodin to enhanced Ena/VASP recruitment and showed integrin-dependent VASP phosphorylation controls a VASP–RIAM–talin module governing adhesion and migration.

    Evidence In vitro Abl kinase assays, co-IP, and β3-integrin knockout fibroblasts with talin-integrin binding analysis

    PMID:20404115 PMID:20417104

    Open questions at the time
    • Whether VASP polymerase activity or scaffolding dominates in adhesion control not separated
    • In vivo relevance of the RIAM-talin switch not tested
  14. 2011 High

    Quantified that elongation rate is set by WH2-mediated G-actin recruitment and that VASP is saturated with actin in vivo, providing a kinetic model for processive monomer delivery.

    Evidence TIRF with chimeric VASP, thermodynamic/kinetic actin-binding analysis, and mathematical modeling

    PMID:21217643

    Open questions at the time
    • Did not address how clustering modifies the saturation regime on membranes
    • Coordination among the four WH2 sites within a tetramer not resolved here
  15. 2012 Medium

    Added tyrosine phosphorylation (Abl/Abi-1 at Tyr39) as a regulatory layer that lowers VASP affinity for zyxin and reduces focal-adhesion accumulation.

    Evidence In vitro Abl kinase assay with Abi-1, Y39D phosphomimetic, co-IP, and adhesion imaging

    PMID:22014333

    Open questions at the time
    • Physiological stimuli driving Tyr39 phosphorylation not established
    • Single-lab phosphomimetic analysis without endogenous confirmation
  16. 2013 High

    Established CDC42-driven IRSp53 clustering as the switch that drives high-density VASP clustering for processive elongation, defined PKD1 as a Ser157 kinase, and linked VASP–Crkl to Rap1b regulation in platelets.

    Evidence In vitro polymerization, VASP-IRSp53 binding/liposome recruitment with CDC42, PKD1 kinase assays, and Crkl co-IP with VASP-null platelet Rap1b assays

    PMID:23846685 PMID:24076653 PMID:27620165

    Open questions at the time
    • How many of the distinct clustering scaffolds operate simultaneously in a given cell unclear
    • C3G involvement in the Crkl/VASP/Rap1b pathway was proposed but not directly shown
  17. 2014 Medium

    Showed cooperation between Ena/VASP and the WAVE/Arp2/3 machinery via EVH1–Abi binding and a palladin-dependent route for VASP recruitment to dorsal stress fibers.

    Evidence In vitro Arp2/3 assembly assays, Abi co-IP, Drosophila genetic rescue, and palladin knockdown with live imaging/FRAP

    PMID:24496446 PMID:25203209

    Open questions at the time
    • How VASP elongation and Arp2/3 branching are spatially coordinated not resolved
    • Relative importance of each recruiter for different actin structures unclear
  18. 2015 Medium

    Showed lamellipodin tethers VASP to actin filaments to boost polymerase activity, defined tension-sensitive zyxin-dependent VASP recruitment to focal adherens junctions, and clarified that Ser157-driven membrane localization requires activated vinculin to enable actin assembly.

    Evidence In vitro actin-binding/TIRF polymerization with Lpd, SIM with zyxin-binding mutants, and S157A/vinculin-Y1065F analysis in airway smooth muscle

    PMID:25759389 PMID:26295568 PMID:26611125

    Open questions at the time
    • Whether tethering and clustering mechanisms are additive or redundant not resolved
    • Generality of the vinculin-prerequisite model beyond smooth muscle untested
  19. 2017 High

    Resolved the tetramer mechanism at single-filament resolution: one arm tracks the barbed end while three GABs recruit monomers, with elongation independent of actin ATP hydrolysis and dependent on tetramerization and surface-based synergy.

    Evidence TIRF with systematic variation of oligomeric state, GAB number, and actin ATP-hydrolysis mutants plus kinetic modeling

    PMID:28667124

    Open questions at the time
    • In vivo confirmation of the one-arm-tracks/three-arms-deliver model not provided
    • Structural basis of inter-molecule synergy on surfaces not determined
  20. 2019 Medium

    Identified an unexpected nuclear role in which VASP participates in a DVL3/β-catenin/TCF4 complex to drive Wnt target transcription, including its own gene, in a feedback loop.

    Evidence Wnt reporter assays, nuclear-complex co-IP, nuclear fractionation, and ChIP in breast cancer cells

    PMID:31831834

    Open questions at the time
    • Single-lab finding without independent validation of the nuclear complex
    • How an actin-regulatory protein contributes to transcription mechanistically unclear
  21. 2020 High

    Provided comprehensive loss-of-function evidence that Ena/VASP shapes lamellipodial network geometry, microspikes, adhesion, and traction force, and extended VASP signaling to PKG/NF-κB anti-inflammatory control.

    Evidence CRISPR knockout with quantitative EM, traction-force microscopy, and VASP-null mice with sGC pharmacology and NF-κB/inflammasome readouts

    PMID:32391788 PMID:33106416

    Open questions at the time
    • Direct mechanism linking Ser239 phosphorylation to NF-κB suppression not defined
    • How VASP loss alters Arp2/3 and capping-protein distribution mechanistically unresolved
  22. 2022 High

    Reconstituted that PIP2-driven IRSp53 self-clustering on membranes is sufficient to recruit VASP and initiate local actin assembly, building filopodia-like protrusions from defined components.

    Evidence In vitro membrane reconstitution, liposome assays, live-cell nanotube pulling, and molecular simulation

    PMID:36240267

    Open questions at the time
    • Quantitative regulation of cluster density in cells not addressed
    • Single-lab reconstitution; cellular sufficiency in physiological context untested
  23. 2023 High

    Revealed that VASP forms liquid-like condensates within which polymerizing actin is organized into parallel bundles, with droplet fluidity being essential for filament rearrangement.

    Evidence In vitro LLPS assays, fluorescence microscopy, and continuum-scale computational modeling comparing solid vs liquid droplets

    PMID:38405682

    Open questions at the time
    • Whether VASP condensates form at physiological actin structures in cells not demonstrated
    • Relationship between condensate-driven bundling and membrane-clustered processive elongation unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the dozen+ EVH1-binding scaffolds, the multi-site phosphorylation code, membrane clustering, and condensate formation are integrated to select between lamellipodial, filopodial, junctional, and bundling outputs in a single cell remains unresolved.
  • No unified model linking scaffold choice to actin-network outcome
  • Physiological role of VASP liquid-liquid phase separation in cells unestablished
  • Crosstalk between cytoplasmic actin function and nuclear Wnt role unexplored

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 5 GO:0008092 cytoskeletal protein binding 4 GO:0060090 molecular adaptor activity 4
Localization
GO:0005856 cytoskeleton 4 GO:0005886 plasma membrane 3 GO:0005634 nucleus 1
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-109582 Hemostasis 2 R-HSA-1266738 Developmental Biology 1
Partners
ABI1CRKLIRSP53/BAIAP2PFN1RAPH1SPTAN1VCLZYX
Complex memberships
VASP homotetramerWAVE regulatory complex (via Abi)

Evidence

Reading pass · 52 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1994 VASP is phosphorylated by both cAMP-dependent protein kinase (PKA) and cGMP-dependent protein kinase (PKG) at three sites: Ser157 (serine 1), Ser239 (serine 2), and Thr278 (threonine), both in vitro and in intact human platelets. PKG phosphorylates Ser157 more rapidly than PKA, while both kinases rapidly phosphorylate Ser239. Ser239 phosphorylation is responsible for the mobility shift of VASP on SDS-PAGE. In vitro kinase assay with purified VASP, reversed-phase HPLC peptide mapping, sequence analysis of phosphopeptides, 32P labeling in intact platelets The Journal of biological chemistry High 8182057
1995 VASP directly binds profilins (from human platelets, calf thymus, and birch pollen) via its central proline-rich domain containing GPPPPP motifs; VASP and profilin co-purify from cell lysates by profilin affinity chromatography and are eluted by poly-L-proline or a VASP proline-rich peptide. Profilin affinity chromatography, direct binding assay with purified proteins, co-localization by immunofluorescence The EMBO journal High 7737110
1995 VASP is organized into three domains: an N-terminal EVH1 domain, a central proline-rich domain (containing GPPPPP repeats and kinase phosphorylation sites), and a C-terminal EVH2 domain. The native protein forms a homotetramer with elongated structure. The C-terminal EVH2 domain is required for localization to focal adhesions; truncation of this domain abolishes focal adhesion targeting. Molecular cloning, hydrodynamic analysis of purified VASP, transfection of truncation mutants in BHK21 cells with immunofluorescence The EMBO journal High 7828592
1995 VASP phosphorylation is regulated by serine/threonine phosphatases: PP1 and PP2A preferentially dephosphorylate VASP in vitro; okadaic acid (PP1/PP2A inhibitor) causes accumulation of phospho-VASP in intact platelets, indicating PP1/PP2A control the phosphorylation state of VASP in cells. In vitro dephosphorylation assay with purified phosphatases, okadaic acid treatment of intact human platelets followed by immunoblotting FEBS letters Medium 7656973
1998 VASP interacts with vinculin in a complex that can be co-immunoprecipitated from cell lysates; both proteins colocalize in nascent focal adhesions. PIP2 binds the vinculin tail, disrupts vinculin head-tail autoinhibition, and greatly enhances VASP–vinculin complex formation. Both the EVH1 and EVH2 domains of VASP participate in vinculin binding. Co-immunoprecipitation from cell lysates, PIP2 binding assay, domain-deletion analysis, immunofluorescence colocalization Current biology Medium 9560340
1998 Human VASP rescues embryonic lethality caused by loss of Drosophila Enabled (Ena), demonstrating functional homology. A missense mutation in the EVH1 domain abolishes in vitro binding to zyxin; a nonsense mutation truncating the EVH2 domain prevents multimerization and reduces zyxin and Abl-SH3 domain binding. Drosophila genetic rescue assay, in vitro binding assay, biochemical co-precipitation Molecular biology of the cell High 9693373
1999 VASP is required for actin-based Listeria motility. The EVH1 domain binds the proline-rich ActA region of Listeria with high affinity; the EVH2 domain binds F-actin, linking the bacterium to the actin tail. PKA phosphorylation of Ser157 increases VASP affinity for F-actin ~40-fold (phospho-VASP Kd ~0.5×10^8 M^-1 vs. 40-fold lower for dephospho-VASP). Immunodepletion of VASP from platelet extracts abolishes motility; add-back of recombinant VASP restores it. In vitro Listeria motility assay, immunodepletion and add-back of recombinant VASP, domain-binding assays, PKA phosphorylation with affinity measurements The Journal of cell biology High 10087267
1999 VASP-null mice show significantly reduced cAMP- and cGMP-mediated inhibition of platelet aggregation, while smooth muscle cAMP/cGMP-dependent relaxation is normal. VASP-independent pathways mediate inhibition of calcium mobilization and granule secretion in platelets; VASP specifically mediates the cyclic nucleotide-dependent inhibition of aggregation, likely through regulation of integrin function. VASP gene knockout in mice, platelet aggregation assays, calcium measurements, granule secretion assays The EMBO journal High 9878048
2000 Ena/VASP proteins negatively regulate fibroblast motility: overexpression decreases movement, and loss-of-function (deletion or neutralization) increases cell movement in a dose-dependent manner. Selective depletion from focal adhesions (but not the leading edge) has no effect; constitutive membrane targeting of Ena/VASP inhibits motility. Overexpression, dominant-negative inhibition, loss-of-function with pharmacological sequestration, targeted membrane localization, quantitative cell migration assays Cell High 10892743
2000 PKA phosphorylation of EVL (an Ena/VASP family member) at its Ser-equivalent residue decreases actin nucleation activity and abolishes binding to Abl and nSrc SH3 domains but not to profilin. Two profilin dimers bind cooperatively to the polyproline sequence, and profilin competes with SH3 domains for partially overlapping binding sites on EVL. In vitro kinase assay, actin nucleation assay, SH3/WW domain binding assays, profilin binding assays The Journal of biological chemistry Medium 10945997
2000 Fyb/SLAP binds the EVH1 domain of Ena/VASP proteins. Upon TCR engagement, Fyb/SLAP, Evl, WASP, and the Arp2/3 complex concentrate at the T cell–APC interface. Inhibition of Fyb/SLAP–Ena/VASP or WASP–Arp2/3 interactions impairs TCR-dependent actin rearrangement. Co-localization by immunofluorescence, co-immunoprecipitation, dominant-negative inhibition, T cell activation assays The Journal of cell biology Medium 10747096
2001 A molecular complex containing Ena/VASP proteins, Fyb/SLAP, SLP-76, Nck, and WASP forms during Fcγ receptor-mediated phagocytosis. Ena/VASP proteins are recruited to phagocytic cups coincident with actin reorganization, and their recruitment is required for pseudopod extension and efficient particle internalization. Co-immunoprecipitation, immunofluorescence localization in macrophages, dominant-negative inhibition of phagocytosis Journal of cell science Medium 11739662
2002 Ena/VASP proteins at the lamellipodial leading edge promote actin filament elongation by associating with barbed ends and shielding them from capping protein, resulting in longer, less branched filaments. Ena/VASP-deficient lamellipodia have shorter, more branched filaments. In vitro, Ena/VASP promotes filament elongation by interacting with barbed ends and antagonizing capping protein. Electron microscopy of lamellipodia actin architecture, in vitro actin polymerization/capping assay, cell migration assays with Ena/VASP gain and loss of function Cell High 12086607
2002 Using Ena/VASP-deficient cell complementation, cyclic nucleotide-dependent kinase phosphorylation sites and the F-actin binding motif within the EVH2 domain are essential for Ena/VASP function in cell motility. The profilin-binding proline-rich region is dispensable for regulating random cell motility. The C-terminal EVH2 domain alone is sufficient to complement Ena/VASP loss. Reconstitution of Ena/VASP-null fibroblasts with Mena point mutants and domain truncations, quantitative cell motility assays Molecular biology of the cell High 12134088
2002 VASP-deficient fibroblasts exhibit enhanced Rac1 activation and elevated PAK activity after PDGF or serum stimulation, along with increased cell spreading. These data reveal a VASP-dependent modulation of the Rac/PAK signaling pathway. VASP knockout fibroblasts, PAK kinase assays, Rac activation pull-down assays, cell spreading measurements The Journal of biological chemistry Medium 12055190
2004 Palladin directly binds VASP via its N-terminal proline-rich domain; synthetic peptide array identifies two discrete VASP-binding sites (polyproline motifs) in palladin. VASP binding is mediated through the EVH1 domain. Both proteins colocalize along stress fibers and partially in focal adhesions. Co-immunoprecipitation with endogenous proteins, blot overlay with recombinant palladin, synthetic peptide array, immunofluorescence colocalization Cell motility and the cytoskeleton Medium 14983521
2004 Lamellipodin (Lpd) directly interacts with Ena/VASP proteins and co-localizes with them at lamellipodia/filopodia tips. Lpd contains a PH domain that specifically binds PI(3,4)P2. Lpd overexpression increases lamellipodial protrusion velocity in an Ena/VASP-dependent manner; Lpd knockdown reduces lamellipodia formation and F-actin content. Yeast two-hybrid/binding assays, co-immunoprecipitation, PH domain lipid binding assay, siRNA knockdown, live-cell imaging Developmental cell High 15469845
2004 RIAM (a Rap1-GTP-interacting adaptor) interacts with both Ena/VASP proteins and Profilin via proline-rich motifs, linking Rap1 signaling to actin dynamics. RIAM overexpression promotes lamellipodia formation requiring actin polymerization; knockdown reduces F-actin content and displaces Rap1-GTP from the plasma membrane. Co-immunoprecipitation, pulldown assays, siRNA knockdown, overexpression with actin polymerization and adhesion readouts Developmental cell Medium 15469846
2004 FAT1 protocadherin directly interacts with Ena/VASP proteins. FAT1 localizes at the leading edge; when targeted to mitochondria, FAT1 cytoplasmic domain recruits components of the actin polymerization machinery sufficient to induce ectopic actin polymerization. FAT1 knockdown decreases VASP recruitment to the leading edge and impairs lamellipodial dynamics. Co-immunoprecipitation/pulldown, ectopic mitochondrial targeting assay, siRNA knockdown, live-cell imaging The EMBO journal Medium 15343270
2005 VASP promotes actin polymerization at barbed ends in the presence of capping proteins (CP, CapG, gelsolin-actin). Profilin enhances VASP anti-capping activity by requiring interactions with both G-actin and VASP. The EVH2 domain is sufficient for barbed-end protection from capping; both F-actin and G-actin binding motifs in EVH2 are required. PKA phosphorylation within EVH2 reduces anti-capping and F-actin bundling activities. In vitro actin polymerization assay with recombinant proteins, domain truncation/mutagenesis, PKA phosphorylation of VASP, capping protein competition assay The Journal of biological chemistry High 15939738
2006 Zyxin-null fibroblasts show severely reduced accumulation of Ena/VASP proteins at focal adhesions, identifying zyxin as a key recruiter of Ena/VASP to focal adhesions. Loss of zyxin results in deficits in actin stress fiber remodeling. Zyxin gene knockout by homologous recombination, immunofluorescence analysis of focal adhesion composition The Journal of cell biology Medium 16505170
2006 Migfilin directly interacts with VASP via the VASP EVH1 domain and a single LPPPPPP motif in migfilin's proline-rich domain. Migfilin facilitates VASP localization to cell-matrix adhesions, and this interaction is required for migfilin-mediated regulation of cell migration. Co-immunoprecipitation, pulldown with EVH1 domain, site-directed mutagenesis of the LPPPPPP motif, siRNA-mediated VASP knockdown, cell migration assays The Journal of biological chemistry Medium 16531412
2006 PKC phosphorylates VASP at Ser157 (but not Ser239) in human platelets in response to phorbol ester. Thrombin-induced Ser157 phosphorylation occurs through both PKC-dependent and PKC-independent pathways; the PKC-independent pathway involves Rho kinase. Site-specific phospho-antibody immunoblotting in human platelets, kinase inhibitor pharmacology (BIM I, H-89, Rho kinase inhibitor), phorbol ester stimulation The Biochemical journal Medium 16197368
2007 Ena/VASP proteins have an anti-capping-independent function in filopodia formation. The entire EVH2 domain is the minimal domain required for filopodia induction. VASP exchanges rapidly at lamellipodial tips (by FRAP) but shows virtually no exchange at filopodial tips. Mutation of the G-actin-binding motif (GAB) partially compromises VASP stabilization at filopodial tips. siRNA depletion of capping protein, VASP mutant expression, FRAP in live cells, cell spreading assay Molecular biology of the cell Medium 17475772
2007 Syndecan-2 induces filopodia formation via a neurofibromin → PKA → Ena/VASP pathway. Neurofibromin activates cAMP/PKA signaling downstream of syndecan-2; PKA phosphorylates Ena/VASP proteins, promoting actin polymerization and filopodia formation. Blocking Ena/VASP activity abolishes syndecan-2-induced filopodia. Kinase inhibitor screen, RNAi, dominant-negative mutants, deletion mutant analysis, inhibition of Ena/VASP activity The Journal of cell biology Medium 17548511
2007 NO-stimulated cGMP-dependent protein kinase II phosphorylates VASP Ser239, which causes rapid retraction of lamellipodia and cell rounding. A VASP Ser239Ala mutant lacking this PKG phosphorylation site is insensitive to NO-induced lamellipodial retraction. Live-cell imaging with GFP-VASP constructs, site-directed mutagenesis (Ser239Ala), pharmacological inhibition of guanylate cyclase and PKG isoforms Journal of cell science Medium 17684063
2007 Ena/VASP activity is required for normal F-actin content, actomyosin contractility, proper response to shear stress, and endothelial barrier function in vivo. Ena/VASP-deficient embryos exhibit vascular patterning defects, edema, hemorrhaging, and late embryonic lethality. Triple Ena/VASP knockout mice, analysis of vascular phenotype, F-actin quantification in endothelial cells, shear stress response assays The Journal of cell biology High 17998398
2008 Clustered VASP on functionalized beads drives processive actin filament elongation insensitive even to high concentrations of capping protein (CP), whereas soluble VASP is inhibited by low CP concentrations. In vitro TIRF microscopy demonstrates VASP delivers actin monomers via its WH2 domains to the growing barbed end. EM structural data support a model where membrane-associated VASP oligomers use WH2 domains to tether and processively elongate actin filaments. In vitro TIRF microscopy, functionalized bead motility assay, EM structure of the protein, VASP mutant analysis in vivo The EMBO journal High 18923426
2008 αII-spectrin binds VASP via its SH3 domain interacting with the VASP triple GP(5)-motif. PKA-mediated phosphorylation of VASP at Ser157 inhibits this αII-spectrin–VASP interaction. In confluent endothelial cells, dephosphorylated VASP colocalizes with αII-spectrin at cell-cell junctions. Expression of the αII-spectrin SH3 domain at cell-cell contacts translocates VASP, initiates cortical actin formation, and decreases endothelial permeability; αII-spectrin-binding-deficient VASP mutants fail to rescue elevated permeability in VASP-null cells. Differential proteomics/mass spectrometry, co-immunoprecipitation, phosphomutant rescue in VASP-null cells, endothelial permeability assays, confocal microscopy The Journal of cell biology High 18195108
2008 Ena/VASP proteins capture actin filament barbed ends directly. Using TIRF microscopy, VASP-coated surfaces capture filament barbed ends; end-attached filaments transiently pause then resume growth via filament-side attachment. In the presence of profilin-actin, VASP accelerates filament growth rate and blocks capping. Total internal reflection fluorescence (TIRF) microscopy of individual actin filaments, VASP-coated surface experiments The Journal of biological chemistry High 18283104
2009 VASP is phosphorylated differentially at three main sites with distinct functional consequences: Ser157 phosphorylation influences VASP localization with minor impact on F-actin assembly; Ser239 and Thr278 phosphorylation impairs VASP-driven actin filament formation in vitro and in living cells. AMPK phosphorylates VASP at Thr278. Reconstitution of VASP-null cells with phosphomimetic mutants, in vitro actin polymerization assays, site-specific kinase phosphorylation, phosphorylation-status-specific antibodies Journal of cell science High 19825941
2009 VASP directly interacts with CXCR2; this interaction is enhanced by CXCL8 stimulation and triggers VASP phosphorylation via PKA- and PKCδ-mediated pathways. The CXCR2–VASP interaction requires free F-actin barbed ends to recruit VASP to the leading edge. VASP knockdown severely impairs CXCR2-mediated chemotaxis and cell polarization. Proteomics identification, direct binding assay, co-immunoprecipitation, siRNA knockdown, chemotaxis assays Journal of cell science Medium 19435808
2009 VASP deficiency in endothelial cells reduces cAMP-mediated Rac1 activation (~50% reduction). Both AKAP-mediated PKA anchoring and VASP are required for full cAMP-mediated Rac1 activation and endothelial barrier stabilization. VASP-null endothelial cells (MyEnd VASP-/-), Rac1 activation assays (pull-down), transendothelial resistance measurements, FITC-dextran flux permeability assay, PKA inhibitor (PKI), AKAP-disrupting peptide (HT31) American journal of physiology. Cell physiology Medium 19118163
2010 Lamellipodin (Lpd) is a substrate of Abl kinases; Abl phosphorylation of Lpd positively regulates the Lpd–Ena/VASP interaction and the recruitment of Mena and EVL to the leading edge. This interaction is required for Lpd-dependent dorsal ruffling and axonal morphogenesis. In vitro Abl kinase assay, Abl SH2 pulldown, Lpd–Mena co-immunoprecipitation, c-Abl knockout/dominant-negative, neurite morphology assays Current biology Medium 20417104
2010 Loss of β3 integrin causes reduced PKA-dependent phosphorylation of VASP; dephosphorylated VASP preferentially associates with RIAM, forming an enhanced VASP–RIAM complex at focal adhesions that increases talin binding to β1 integrin, promoting β1-dependent adhesion and migration defects. β3 integrin knockout fibroblasts, co-immunoprecipitation (VASP–RIAM in vitro and in vivo), PKA phosphorylation analysis, talin–integrin binding assays, 2D and 3D motility assays The Journal of cell biology Medium 20404115
2011 Ena/VASP-mediated actin filament elongation rate depends on G-actin recruitment by the WASP homology 2 (WH2) motif. TIRF and kinetic analyses show a saturation dependence on actin monomer concentration, meaning Ena/VASP is fully saturated with actin in vivo. Processive VASP-mediated elongation on surfaces does not involve spontaneous monomer addition. In vitro TIRF microscopy with chimeric VASP proteins, thermodynamic and kinetic actin binding analyses, mathematical modeling The EMBO journal High 21217643
2012 VASP is a substrate for Abelson (Abl) tyrosine kinase, phosphorylated at Tyr39 via Abi-1 bridging. Abl/Abi-1-mediated tyrosine phosphorylation of VASP reduces its accumulation at focal adhesions; the phosphomimetic Y39D mutation reduces VASP affinity for the proline-rich region of zyxin. In vitro Abl kinase assay with Abi-1, co-expression in cells, phosphomimetic Y39D mutant, co-immunoprecipitation, focal adhesion imaging, K562 cell adhesion assay The Biochemical journal Medium 22014333
2013 CDC42 switches IRSp53 from an inhibitor of barbed-end actin growth to a promoter by inducing high-density clustering of VASP, which is required for processive actin filament elongation. VASP binds directly to IRSp53; this interaction is regulated by activated CDC42 and promotes VASP clustering and recruitment to liposomes. In vitro actin polymerization assays, VASP:IRSp53 binding assays, liposome recruitment, CDC42 activation experiments, genetic removal of IRSp53 in cells The EMBO journal High 24076653
2013 PKD1 directly phosphorylates VASP at Ser157 and Ser322 in response to RhoA activation. These phosphorylations mediate VASP relocalization from focal contacts to the leading edge, increasing filopodia formation and length, but persistent signaling causes membrane ruffling and decreased motility. In vitro PKD1 kinase assay with VASP, site-directed mutagenesis, RhoA activation assays, live-cell VASP localization, filopodia morphometry The Journal of biological chemistry Medium 23846685
2013 Crkl forms a direct complex with VASP in platelets: Crkl co-immunoprecipitates VASP from platelet lysates; recombinant VASP binds directly to the N-terminal SH3 domain of Crkl; Crkl and VASP colocalize at actin-rich protrusions during platelet spreading. PKA-mediated phosphorylation of VASP at Ser157 abrogates Crkl binding. VASP-null platelets show reduced agonist-induced Rap1b activation, and a Crkl/VASP/C3G pathway is proposed to regulate Rap1b and platelet aggregation. Co-immunoprecipitation from platelet lysates, recombinant GST-Crkl domain pulldown, phosphomutant analysis, Rap1b activation assay, VASP-null platelets Cell communication and signaling Medium 27620165
2014 Palladin is required for recruitment of VASP to dorsal stress fibers; palladin and VASP associate as a complex with similar rapid dynamics at dorsal stress fibers (assessed by live imaging). Loss of palladin specifically disrupts non-contractile dorsal stress fiber assembly through failure to recruit VASP. Palladin knockdown/knockout, immunofluorescence, live-cell imaging of GFP-tagged proteins, FRAP, 3D collagen migration assay Journal of cell science Medium 24496446
2014 Ena/VASP and the WAVE regulatory complex (WRC) cooperate in actin polymerization through direct interaction of the Ena/VASP EVH1 domain with a proline-rich motif in Abi (a WRC component). This interaction enhances WRC stimulation of Arp2/3-mediated actin assembly in vitro in the presence of Rac, and is required in vivo for lamellipodia formation and cell spreading. Co-immunoprecipitation, in vitro Arp2/3 actin assembly assay with purified proteins, Drosophila genetic rescue (abi mutants), cell spreading/lamellipodia assays Developmental cell High 25203209
2015 Lamellipodin (Lpd) binds directly to actin filaments; this actin-filament interaction regulates Lpd subcellular localization and enhances VASP polymerase activity. Lpd delivers Ena/VASP proteins to growing barbed ends and increases their polymerase activity by tethering them to filaments. In vitro actin filament binding assay with purified Lpd, TIRF microscopy, VASP polymerization assays with and without Lpd, Lpd localization analysis in cells eLife High 26295568
2015 VASP, zyxin, and TES are recruited to Focal Adherens Junctions (FAJ) in a tension-sensitive manner independent of the α-catenin/vinculin module. VASP localization to FAJs requires binding to zyxin; localization mutants of VASP that cannot bind zyxin fail to incorporate into FAJs. Structured Illumination Microscopy (SIM), tension manipulation, VASP/zyxin binding-deficient mutant expression, immunofluorescence Scientific reports Medium 26611125
2015 VASP Ser157 phosphorylation mediates membrane localization in airway smooth muscle (ASM) cells. Acetylcholine-induced contraction triggers formation of VASP–VASP oligomers and VASP–vinculin and VASP–profilin complexes at membrane sites; this requires activated vinculin (via Tyr1065 phosphorylation). VASP Ser157 phosphorylation and membrane localization alone are insufficient to activate its actin polymerization activity; interaction with activated vinculin is a necessary prerequisite. Phosphomutant VASP expression (S157A) in ASM tissues, co-immunoprecipitation of VASP complexes, vinculin Y1065F inactive mutant, contraction assays, actin polymerization measurements The Journal of biological chemistry Medium 25759389
2017 Tetrameric VASP uses one arm to processively track growing filament barbed ends while three G-actin-binding sites (GABs) on other arms recruit and deliver monomers. In solution, elongation rates correlate with the number of free GABs; on surfaces, adjacent VASP molecules synergize for filament elongation irrespective of oligomeric state. ATP hydrolysis by actin is not required for VASP-mediated filament assembly. VASP tetramer formation is required for function. In vitro TIRF microscopy, oligomerization state variation, GAB number variation by chimeric protein design, actin ATP hydrolysis mutant analysis, kinetic modeling Proceedings of the National Academy of Sciences High 28667124
2019 VASP is a target gene of the Wnt/β-catenin signaling pathway. In breast cancer cells, VASP localizes to the nucleus where it forms a complex with DVL3, β-catenin, and TCF4 to activate Wnt target gene transcription (including VASP itself, c-myc, and cyclin D1), creating a positive feedback loop. Luciferase reporter assay for Wnt target genes, co-immunoprecipitation of nuclear complex (VASP/DVL3/β-catenin/TCF4), nuclear fractionation, ChIP Oncogene Medium 31831834
2020 PKG-mediated phosphorylation of VASP at Ser239 reduces NF-κB activity and decreases Il1b and Nlrp3 gene transcription in Kupffer cells; this constitutes a sGC/PKG/VASP/NF-κB/NLRP3 inflammasome circuit mediating anti-inflammatory effects. VASP-null mice on high-fat diet, pharmacological sGC stimulator (praliciguat), phospho-Ser239 VASP immunoblotting, NF-κB reporter assays, inflammasome component analysis Proceedings of the National Academy of Sciences Medium 33106416
2020 CRISPR/Cas9-mediated loss of Ena/VASP proteins reduces lamellipodial actin assembly, perturbs network geometry (shorter filaments, fewer filaments), causes abnormal Arp2/3 complex and capping protein accumulation, abolishes microspikes within lamellipodia, impairs integrin-mediated adhesion, and reduces traction forces. CRISPR/Cas9 knockout in multiple cell lines, quantitative EM of actin networks, Arp2/3/capping protein localization, traction force microscopy, adhesion assays eLife High 32391788
2020 VASP co-localizes with and is co-immunoprecipitated by CRKL in HCC cells. VASP dynamically colocalizes at the SH3N domain of CRKL and mediates CRKL function, activating AKT and ERK signaling to promote EMT and MMP expression. Co-immunoprecipitation, immunofluorescence colocalization, gain- and loss-of-function studies Theranostics Low 30279729
2022 IRSp53 self-assembles into clusters on PIP2-containing membranes, and these clusters recruit VASP to assemble actin filaments locally, generating actin-filled membrane protrusions resembling filopodia. In vitro reconstitution demonstrates IRSp53 clusters are sufficient to recruit VASP and initiate actin assembly on membranes. In vitro reconstitution on membranes, liposome assays, live-cell nanotube pulling, in silico molecular simulations Science advances High 36240267
2023 VASP forms liquid-like condensates under physiological conditions. Actin polymerizes within these VASP droplets; elongating filaments partition to droplet edges forming an actin ring. As actin polymerizes, the ring's rigidity eventually overcomes droplet surface tension, deforming into parallel-filament bundles. Fluid droplet properties are critical for bundling; more solid droplets prevent filament rearrangement and bundle formation. In vitro liquid-liquid phase separation assay, fluorescence microscopy, continuum-scale computational modeling, comparison of solid vs. liquid droplet conditions Nature physics High 38405682

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell 684 12086607
2003 Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration. Annual review of cell and developmental biology 543 14570581
1995 The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. The EMBO journal 405 7737110
2000 Negative regulation of fibroblast motility by Ena/VASP proteins. Cell 395 10892743
1994 cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. The Journal of biological chemistry 367 8182057
2004 RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion. Developmental cell 334 15469846
1999 Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. The Journal of cell biology 283 10087267
1999 The vasodilator-stimulated phosphoprotein (VASP) is involved in cGMP- and cAMP-mediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function. The EMBO journal 274 9878048
2005 Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins. The Journal of biological chemistry 262 15939738
2004 Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics. Developmental cell 262 15469845
2000 Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton. The Journal of cell biology 247 10747096
2009 Ena/VASP: towards resolving a pointed controversy at the barbed end. Journal of cell science 209 19494122
2008 Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation. The EMBO journal 192 18923426
2007 Ena/VASP proteins have an anti-capping independent function in filopodia formation. Molecular biology of the cell 178 17475772
1995 Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP. The EMBO journal 174 7828592
2001 Actin-based motility: stop and go with Ena/VASP proteins. Trends in biochemical sciences 168 11295557
2001 Evidence for a molecular complex consisting of Fyb/SLAP, SLP-76, Nck, VASP and WASP that links the actin cytoskeleton to Fcgamma receptor signalling during phagocytosis. Journal of cell science 164 11739662
2000 cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains. The Journal of biological chemistry 159 10945997
2004 Protocadherin FAT1 binds Ena/VASP proteins and is necessary for actin dynamics and cell polarization. The EMBO journal 153 15343270
2009 Differential VASP phosphorylation controls remodeling of the actin cytoskeleton. Journal of cell science 151 19825941
2018 Hypoxia-induced up-regulation of VASP promotes invasiveness and metastasis of hepatocellular carcinoma. Theranostics 140 30279729
2006 Genetic ablation of zyxin causes Mena/VASP mislocalization, increased motility, and deficits in actin remodeling. The Journal of cell biology 138 16505170
1998 The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. Current biology : CB 136 9560340
2003 Function and regulation of Ena/VASP proteins. Trends in cell biology 133 12837609
2011 Molecular mechanism of Ena/VASP-mediated actin-filament elongation. The EMBO journal 129 21217643
2007 Syndecan-2 induces filopodia and dendritic spine formation via the neurofibromin-PKA-Ena/VASP pathway. The Journal of cell biology 116 17548511
2011 Endothelial NO/cGMP/VASP signaling attenuates Kupffer cell activation and hepatic insulin resistance induced by high-fat feeding. Diabetes 114 21911751
2002 Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration. Molecular biology of the cell 112 12134088
2013 CDC42 switches IRSp53 from inhibition of actin growth to elongation by clustering of VASP. The EMBO journal 99 24076653
2008 Cytoskeleton assembly at endothelial cell-cell contacts is regulated by alphaII-spectrin-VASP complexes. The Journal of cell biology 98 18195108
1998 Mutations in Drosophila enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1) and EVH2 domains. Molecular biology of the cell 98 9693373
1993 Role of cyclic nucleotide-dependent protein kinases and their common substrate VASP in the regulation of human platelets. Advances in experimental medicine and biology 97 8209791
2007 Ena/VASP is required for endothelial barrier function in vivo. The Journal of cell biology 96 17998398
2001 Zyxin is not colocalized with vasodilator-stimulated phosphoprotein (VASP) at lamellipodial tips and exhibits different dynamics to vinculin, paxillin, and VASP in focal adhesions. Molecular biology of the cell 94 11598195
2004 Caenorhabditis elegans WASP and Ena/VASP proteins play compensatory roles in morphogenesis and neuronal cell migration. Genetics 92 15280232
2001 A WASp-VASP complex regulates actin polymerization at the plasma membrane. The EMBO journal 92 11598004
2008 Ena/VASP: proteins at the tip of the nervous system. Current opinion in neurobiology 89 18508258
2014 Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton. Developmental cell 88 25203209
2019 Dynamics and distribution of paxillin, vinculin, zyxin and VASP depend on focal adhesion location and orientation. Scientific reports 77 31320676
2020 Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion. eLife 75 32391788
2016 Lamellipodin promotes invasive 3D cancer cell migration via regulated interactions with Ena/VASP and SCAR/WAVE. Oncogene 75 26996666
2004 Palladin is a novel binding partner for Ena/VASP family members. Cell motility and the cytoskeleton 75 14983521
2008 Ena/VASP proteins capture actin filament barbed ends. The Journal of biological chemistry 74 18283104
2004 ENA/VASP proteins: multifunctional regulators of actin cytoskeleton dynamics. Frontiers in bioscience : a journal and virtual library 72 14977545
2009 Loss of profilin-1 expression enhances breast cancer cell motility by Ena/VASP proteins. Journal of cellular physiology 71 19115233
2006 Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser157 by protein kinase C-dependent and -independent mechanisms in thrombin-stimulated human platelets. The Biochemical journal 71 16197368
2015 Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments. eLife 70 26295568
2005 WASP-related proteins, Abi1 and Ena/VASP are required for Listeria invasion induced by the Met receptor. Journal of cell science 70 15769844
2010 c-Abl, Lamellipodin, and Ena/VASP proteins cooperate in dorsal ruffling of fibroblasts and axonal morphogenesis. Current biology : CB 69 20417104
2010 Alpha v beta3 integrin spatially regulates VASP and RIAM to control adhesion dynamics and migration. The Journal of cell biology 67 20404115
2008 VASP is involved in cAMP-mediated Rac 1 activation in microvascular endothelial cells. American journal of physiology. Cell physiology 65 19118163
2002 The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs. Current biology : CB 60 12372256
2015 VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the α-catenin-vinculin module. Scientific reports 57 26611125
2014 Ena/VASP regulates mDia2-initiated filopodial length, dynamics, and function. Molecular biology of the cell 57 24989797
2022 Ena/VASP proteins in cell edge protrusion, migration and adhesion. Journal of cell science 56 35285496
2020 Stimulation of soluble guanylate cyclase exerts antiinflammatory actions in the liver through a VASP/NF-κB/NLRP3 inflammasome circuit. Proceedings of the National Academy of Sciences of the United States of America 55 33106416
2017 Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays. Proceedings of the National Academy of Sciences of the United States of America 55 28667124
2003 Phosphorylation of the vasodilator-stimulated phosphoprotein (VASP) by the anti-platelet drug, cilostazol, in platelets. Platelets 55 14602552
2006 Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration. The Journal of biological chemistry 54 16531412
2020 Interleukin 1β-mediated HOXC10 Overexpression Promotes Hepatocellular Carcinoma Metastasis by Upregulating PDPK1 and VASP. Theranostics 53 32206125
2020 Arp2/3 and Mena/VASP Require Profilin 1 for Actin Network Assembly at the Leading Edge. Current biology : CB 52 32470361
2009 VASP is a CXCR2-interacting protein that regulates CXCR2-mediated polarization and chemotaxis. Journal of cell science 52 19435808
2023 Liquid-like VASP condensates drive actin polymerization and dynamic bundling. Nature physics 51 38405682
2011 The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation. PLoS computational biology 49 21814501
2005 Differential expression of VASP in normal lung tissue and lung adenocarcinomas. Thorax 49 15994266
2007 Modulation of lamellipodial structure and dynamics by NO-dependent phosphorylation of VASP Ser239. Journal of cell science 48 17684063
2003 Endothelium-dependent and -independent relaxation and VASP serines 157/239 phosphorylation by cyclic nucleotide-elevating vasodilators in rat aorta. Biochemical pharmacology 48 12527332
1995 Dephosphorylation of the focal adhesion protein VASP in vitro and in intact human platelets. FEBS letters 48 7656973
2013 Regulation of VASP by phosphorylation: consequences for cell migration. Cell adhesion & migration 47 24401601
2009 Green tea (-)-epigallocatechin-3-gallate down-regulates VASP expression and inhibits breast cancer cell migration and invasion by attenuating Rac1 activity. European journal of pharmacology 47 19171136
2005 PREL1 provides a link from Ras signalling to the actin cytoskeleton via Ena/VASP proteins. FEBS letters 45 15642358
2001 Distribution, cellular localization, and postnatal development of VASP and Mena expression in mouse tissues. Histochemistry and cell biology 44 11810195
2014 Baicalein inhibits agonist- and tumor cell-induced platelet aggregation while suppressing pulmonary tumor metastasis via cAMP-mediated VASP phosphorylation along with impaired MAPKs and PI3K-Akt activation. Biochemical pharmacology 43 25268843
2006 VASP governs actin dynamics by modulating filament anchoring. Biophysical journal 42 17098798
1998 The focal adhesion phosphoprotein, VASP. The international journal of biochemistry & cell biology 42 9611773
2020 ITGA3 interacts with VASP to regulate stemness and epithelial-mesenchymal transition of breast cancer cells. Gene 41 31987909
2006 Regulation of somitogenesis by Ena/VASP proteins and FAK during Xenopus development. Development (Cambridge, England) 41 16421193
2005 NO-dependent osteoclast motility: reliance on cGMP-dependent protein kinase I and VASP. Journal of cell science 41 16291726
2019 The Wnt/β-catenin/VASP positive feedback loop drives cell proliferation and migration in breast cancer. Oncogene 39 31831834
2002 Increased spreading, Rac/p21-activated kinase (PAK) activity, and compromised cell motility in cells deficient in vasodilator-stimulated phosphoprotein (VASP). The Journal of biological chemistry 39 12055190
2022 Activated I-BAR IRSp53 clustering controls the formation of VASP-actin-based membrane protrusions. Science advances 38 36240267
2017 Ena/VASP proteins regulate activated T-cell trafficking by promoting diapedesis during transendothelial migration. Proceedings of the National Academy of Sciences of the United States of America 38 28320969
2020 Initiation and disassembly of filopodia tip complexes containing VASP and lamellipodin. Molecular biology of the cell 36 32579429
2008 Role of Ena/VASP proteins in homeostasis and disease. Handbook of experimental pharmacology 36 18491048
2003 Disruption of cardiac Ena-VASP protein localization in intercalated disks causes dilated cardiomyopathy. American journal of physiology. Heart and circulatory physiology 36 12933343
2016 Vasodilator-Stimulated Phosphoprotein (VASP)-dependent and -independent pathways regulate thrombin-induced activation of Rap1b in platelets. Cell communication and signaling : CCS 35 27620165
2013 Protein kinase D1-mediated phosphorylations regulate vasodilator-stimulated phosphoprotein (VASP) localization and cell migration. The Journal of biological chemistry 35 23846685
2016 Fat3 and Ena/VASP proteins influence the emergence of asymmetric cell morphology in the developing retina. Development (Cambridge, England) 34 27122175
2012 Abl-1-bridged tyrosine phosphorylation of VASP by Abelson kinase impairs association of VASP to focal adhesions and regulates leukaemic cell adhesion. The Biochemical journal 34 22014333
2009 Role of VASP phosphorylation for the regulation of microglia chemotaxis via the regulation of focal adhesion formation/maturation. Molecular and cellular neurosciences 34 19733667
2013 Mena/VASP and αII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy. Cell communication and signaling : CCS 33 23937664
2014 Palladin promotes assembly of non-contractile dorsal stress fibers through VASP recruitment. Journal of cell science 32 24496446
2015 Vasodilator-stimulated phosphoprotein (VASP) regulates actin polymerization and contraction in airway smooth muscle by a vinculin-dependent mechanism. The Journal of biological chemistry 30 25759389
1996 High expression of the focal adhesion- and microfilament-associated protein VASP in vascular smooth muscle and endothelial cells of the intact human vessel wall. Basic research in cardiology 30 8922250
2020 Betulinic acid inhibits cell proliferation and migration in gastric cancer by targeting the NF-κB/VASP pathway. European journal of pharmacology 29 32860808
2005 VASP-dependent regulation of actin cytoskeleton rigidity, cell adhesion, and detachment. Histochemistry and cell biology 29 16267652
2013 Matrine inhibits the adhesion and migration of BCG823 gastric cancer cells by affecting the structure and function of the vasodilator-stimulated phosphoprotein (VASP). Acta pharmacologica Sinica 28 23685951
2012 A VASP-Rac-soluble guanylyl cyclase pathway controls cGMP production in adipocytes. Science signaling 28 22932701
2014 VASP activation via the Gα13/RhoA/PKA pathway mediates cucurbitacin-B-induced actin aggregation and cofilin-actin rod formation. PloS one 27 24691407
2007 Association of VASP with TRPC4 in PKG-mediated inhibition of the store-operated calcium response in mesangial cells. American journal of physiology. Renal physiology 27 17913834

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