ライフサイエンスコーパス: VASP

1 VASP bundles Rac1, Rac2, cyclic AMP-dependent, and cycli

2 VASP knockdown results in a reduction in surface AMPAR d

3 VASP localizes to regions of dynamic actin reorganizatio

4 VASP promotes actin-based movement alone, in the absence

5 VASP-E exploits the central observation that three dimen

6 VASP-E was used to examine a nonredundant subset of the

7 VASP-VASP complex formation and the interaction of VASP

8 vation as assessed by analyses of serine 157 VASP phosphorylation as well as Epac-mediated Rap1 activ

9 vivo, which leads to enhanced formation of a VASP-RIAM complex at focal adhesions and subsequent incr

10 normally observed with S-nitrosylated actin, VASP binding to actin, elevated Rac activity, and elevat

11 e VASP tetramer, demonstrating that adjacent VASP molecules synergize in the elongation of a single f

12 to the observed genetic effects by affecting VASP mRNA expression.

13 tions between Lamellipodin (Lpd), actin, and VASP, both in vivo and in vitro.

14 actin regulatory proteins alpha-actinin and VASP to compromised stress fiber zones.

15 Dimerization, membrane association, and VASP binding are all required for lamellipodin to incorp

16 tion, ticagrelor increased platelet cAMP and VASP-P in the absence of ADP in an adenosine receptor-in

17 es of the actin-binding proteins cofilin and VASP, which are upstream regulators of conformational in

18 cadherin, p120-catenin, ZO-1, cortactin, and VASP.

19 es to changes in the accumulation of ENA and VASP fluorescence in their tips over time.

20 odyan to quantify the recruitment of ENA and VASP preceding filopodia formation in neuronal growth co

21 We demonstrate that EVL and VASP are selectively required for activated T-cell traff

22 Instead, deletion of EVL and VASP impaired T-cell diapedesis.

23 study identifies a specific role for EVL and VASP in T-cell diapedesis and trafficking.

24 Deletion of EVL and VASP resulted in the impairment in alpha4 integrin (CD49

25 Overall, EVL and VASP selectively mediate activated T-cell trafficking by

26 ts of a set of distinct formin fragments and VASP on site-specific, lamellipodial versus cytosolic ac

27 K (extracellular signal-related kinase), and VASP (vasodilator-stimulated phosphoprotein).

28 In adherent cells only, mDia1 and VASP also contribute to filopodial assembly, and filopod

29 PD response by LTA, VN-P2Y12, and VASP during all treatments appeared similar between age

30 phosphate 5 to 20 muM), VerifyNow P2Y12, and VASP phosphorylation assays were performed.

31 n mediates both filament elongation rate and VASP anti-capping activity.

32 er internalization/inactivation, and Src and VASP phosphorylation, but not apical plasma membrane AT(

33 -VASP complexes as well as VASP-vinculin and VASP-profilin complexes at membrane sites.

34 Similar results were observed by VN and VASP.

35 Appropriate VASP ubiquitination and deubiquitination are required fo

36 formation of VASP-VASP complexes as well as VASP-vinculin and VASP-profilin complexes at membrane si

37 lity assay, we show that WAVE directly binds VASP, resulting in an increase in Arp2/3 complex-based a

38 In higher ionic strength buffers, VASP requires profilin for effective polymerase and anti

39 In low ionic strength buffers, VASP tetramers are weakly processive (K(off) = 0.69 s(-1

40 active vinculin mutant, vinculin Y1065F, but VASP phosphorylation and membrane localization were unaf

41 st that actin polymerization and bundling by VASP are critical for spine formation, expansion, and mo

42 s increases the polymerization efficiency by VASP but decreases its efficiency as an anti-capper; bin

43 in bundle formation and motility mediated by VASP.

44 tion of the actin filament polymerase called VASP is part of the guidance system.

45 ropose that at physiological salt conditions VASP nucleation activity is too weak to promote motility

46 Once formed, tip complexes containing VASP and lamellipodin grow by fusing with each other, bu

47 t actin-rich cellular protrusions containing VASP, a filopodial marker.

48 Conversely, VASP deficiency induced proinflammatory M1 macrophage ac

49 ng with VASP and antagonizes TRIM9-dependent VASP ubiquitination.

50 Dephosphorylated VASP in beta3-null cells is preferentially associated wi

51 To fill this gap, this paper describes VASP-E (Volumetric Analysis of Surface Properties with E

52 ated into discrete foci at the leading edge, VASP promotes filopodia assembly and forms part of a poo

53 revious analyses of fast and slow elongating VASP proteins by in vitro total internal reflection fluo

54 sis was independent of alpha-actinin and ENA-VASP, both of which bind to the N-terminal domain of zyx

55 tor-stimulated phosphoprotein (VASP) and Ena-VASP-like (EVL) are cytoskeletal effector proteins impli

56 Ena/VASP proteins act as actin polymerases that drive the pr

57 Ena/VASP proteins and the WAVE regulatory complex (WRC) regu

58 Ena/VASP proteins mediate the effects of guidance cues on th

59 Ena/VASP proteins regulate the actin cytoskeleton during cel

60 Ena/VASP tetramers are processive actin elongation factors t

61 Ena/VASP's ability to bind F-actin and profilin-complexed G-

62 Ena/VASP-deficiency also impaired integrin-mediated adhesion

63 Ena/VASP-family actin polymerases, for example, modulate cel

64 UNC-34 (Ena/VASP), the Rac GTPases MIG-2 and CED-10 and the actin bi

65 Mena is an Ena/VASP family actin regulator with roles in cell migration

66 genesis, and cooperates with c-Abl in an Ena/VASP-dependent manner.

67 interactions between SHIP2 and Mena, an Ena/VASP-family actin regulatory protein.

68 d was highly dependent on profilin-1 and Ena/VASP but not formins.

69 alpha-Actinin and Ena/VASP proteins bind to the stress fiber reinforcement dom

70 through interactions with Scar/WAVE and Ena/VASP proteins to promote the formation of cellular protr

71 alpha-catenin acts through vinculin and Ena/VASP proteins to reinforce the cell against mechanical s

72 ngated at filopodial tips by formins and Ena/VASP proteins.

73 egulates the interaction between Lpd and Ena/VASP proteins.

74 rto unknown intermediary between Abl and Ena/VASP proteins.

75 odin [a PI(3,4)P(2)-binding protein] and Ena/VASP to the leading edge.

76 its association with both Scar/WAVE and Ena/VASP, whereas Src-dependent phosphorylation enhances bin

77 cluding the Arp2/3 complex, formins, and Ena/VASP, which have largely been analyzed separately.

78 players in lamellipodial protrusion are Ena/VASP proteins, which enhance actin filament elongation.

79 recruitment of actin regulators, such as ENA/VASP proteins, to sites of protrusion underlies diverse

80 gation promoting factors (NEPFs) such as Ena/VASP, formins, and WASP-family proteins recruit profilin

81 Our results identify bacterial Ena/VASP mimics and reveal that pathogens imitate the full s

82 work of multivalent interactions between Ena/VASP proteins, EVH1 ligands, and actin filaments.

83 gement is dependent on its actin binding Ena/VASP homology 2 (EVH2) domain and its EVH1 domain, which

84 ion of profilin1 (Pfn1), Arp3, cofilin1, Ena/VASP, and CapZ, is an indicator of poor prognosis in ccR

85 hat the founding member of the conserved Ena/VASP (Enabled/Vasodilator Activated Protein) family is r

86 In this context, Ena/VASP-depending signaling pathways, in particular interac

87 We propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their

88 loped a kinetic model to further dissect Ena/VASP's processive mechanism on bundled filaments.

89 ing with F-actin and the actin effectors Ena/VASP proteins and the SCAR/WAVE complex.

90 Filopodia initiated by either Ena/VASP or mDia2 contained similar molecular inventory but

91 cell migration via both actin-elongating Ena/VASP proteins and the Scar/WAVE complex, which stimulate

92 at increased Lamellipodin levels enhance Ena/VASP and Scar/WAVE activities at the plasma membrane to

93 by Cdc42 or downstream effectors (Eps8, Ena/VASP).

94 nteractions between the C-terminal EVH1 (Ena/VASP [vasodilator-stimulated phosphoprotein] homology do

95 exocytosis and involves a novel role for Ena/VASP in exocytosis.

96 eudomallei and B. mallei BimA mimic host Ena/VASP actin polymerases in their ability to nucleate, elo

97 Taken together, our results identify Ena/VASP as a significant modifier of tumor growth through r

98 One important Ena/VASP regulator is the mig-10/Lamellipodin/RIAM family of

99 Indeed, a change in Ena/VASP protein distribution is sufficient to recapitulate

100 ively regulate Lpd-Ena/VASP interaction, Ena/VASP recruitment to Lpd at the leading edge, and Lpd-Ena

101 ular domain, which can bind and localize Ena/VASP family actin regulators.

102 e role for the EVH1 domain in localizing Ena/VASP family members.

103 ment to Lpd at the leading edge, and Lpd-Ena/VASP function in axonal morphogenesis and in PDGF-induce

104 that Abl kinases positively regulate Lpd-Ena/VASP interaction, Ena/VASP recruitment to Lpd at the lea

105 we show that the Ena/VASP family member, Ena/VASP-like (EVL), polymerizes actin at FAs, which promote

106 Notably, Ena/VASP's processive run length increases with the number o

107 Our data thus uncover novel Ena/VASP functions of these actin polymerases that are fully

108 data demonstrate that the activities of Ena/VASP and the WRC are intimately linked to ensure optimal

109 , selective, peptidomimetic inhibitor of Ena/VASP EVH1 domain interactions.

110 Loss of Ena/VASP function also abolished the formation of microspike

111 In vivo, perturbation of Ena/VASP function in tumor myofibroblast precursor cells sig

112 an evolutionarily conserved property of Ena/VASP homologues, including human VASP and Caenorhabditis

113 3 complex and the elongating activity of Ena/VASP proteins for the formation of actin networks.

114 CRISPR/Cas9-mediated loss of Ena/VASP proteins reduced lamellipodial actin assembly and p

115 consistent with the idea that binding of Ena/VASP to WAVE potentiates Arp2/3 complex activity and lam

116 Loss-of-function of Ena/VASP, alpha5beta1-integrins or talin in the somitic cell

117 Moreover, in the absence of Ena/VASP, filopodia generated by mDia2 did not support initi

118 erfering with the polymerase activity of Ena/VASP, its surface recruitment or its bundling activity a

119 ments, we established a kinetic model of Ena/VASP-mediated actin filament elongation.

120 the network by, for example, formins or Ena/VASP family members and its influence on the effectivene

121 riants that lack either alpha-actinin or Ena/VASP-binding capacity display compromised response to me

122 sembled by Arp2/3 complex and formins or Ena/VASP.

123 d/Vasodilator-stimulated phosphoprotein (Ena/VASP) protein family members link actin dynamics and cel

124 d/vasodilator-stimulated phosphoprotein (Ena/VASP)-deficient MV(D7) fibroblasts, which are also devoi

125 ed either by adding the actin polymerase Ena/VASP or by boosting Arp2/3 complex activity at the surfa

126 ocalization and function of postsynaptic Ena/VASP family protein is dependent on conserved C-terminal

127 vasodilator-stimulated phospho-proteins (Ena/VASP) to promote actin assembly.

128 as focal adhesions, all of which recruit Ena/VASP family members hitherto thought to antagonize effic

129 pd) regulates cell motility and recruits Ena/VASP proteins (Ena, Mena, VASP, EVL) to the leading edge

130 ment or its bundling activity all reduce Ena/VASP's ability to maintain polarized network growth in t

131 ber of the actin cytoskeleton regulators Ena/VASP, is overexpressed in high-risk preneoplastic lesion

132 Robo, to members of the actin-regulatory Ena/VASP family.

133 ct with neurofibromin via its N-terminal Ena/VASP Homology 1 (EVH1) domain and to mediate membrane tr

134 We conclude that Ena/VASP and mDia2 support the formation of filopodia with s

135 We demonstrate that Ena/VASP and the WRC control actin polymerization in a coope

136 gnificantly distinct properties and that Ena/VASP regulates mDia2-initiated filopodial morphology, dy

137 ve manner through the interaction of the Ena/VASP EVH1 domain with an extended proline rich motif in

138 pithelial cells, where it works with the Ena/VASP family member EVL to assemble the actin cytoskeleto

139 Here, we show that the Ena/VASP family member, Ena/VASP-like (EVL), polymerizes act

140 n a collection of proteins including the Ena/VASP family member, vasodilator-stimulated phosphoprotei

141 The single C. elegans homolog of the Ena/VASP family of proteins, UNC-34, is required for the mig

142 ially drives actin polymerization by the Ena/VASP protein, EVL.

143 the AR of zDHHC17 was identified for the Ena/VASP-like protein.

144 enhances binding to Scar/WAVE but not to Ena/VASP.

145 One pathway uses Ena/VASP-regulated actin dynamics coordinated with VAMP2-med

146 Enabled/Vasodilator (Ena/VASP) proteins promote actin filament assembly at multip

147 regulating actin filament elongation via Ena/VASP proteins.

148 in are important for its effect, whereas Ena/VASP tetramerization is not necessary.

149 interaction with Scar/WAVE but not with Ena/VASP is required for random 2D cell migration.

150 s thought to promote actin assembly with Ena/VASP.

151 raction increases cell migration and enables VASP to cooperatively enhance WRC stimulation of Arp2/3

152 Knockdown of endogenous VASP by siRNA led to a significant decrease in the densi

153 sts, which express high levels of endogenous VASP.

154 is became equivalent between control and EVL/VASP dKO T cells upon alpha4 integrin blockade.

155 lly, we found a defect in trafficking of EVL/VASP double-knockout (dKO) T cells to the inflamed skin

156 we show an impairment in trafficking of EVL/VASP-deficient activated T cells to the inflamed central

157 Unexpectedly, EVL/VASP dKO T cells did not exhibit alterations in shear-re

158 hesion sites is a necessary prerequisite for VASP-mediated molecular processes necessary for actin po

159 hat actin ATP hydrolysis is not required for VASP-mediated filament assembly.

160 d phosphoprotein (VASP); however, a role for VASP in FA development has been elusive.

161 ngation proteins, Diaphanous-related formin, VASP, and fascin are recruited subsequently.

162 and the transplantation of bone marrow from VASP-deficient donor mice into normal recipients caused

163 C6), "protein binding" (PICALM, STX4, GPNMB, VASP, extended-synaptotagmin 2 [ESYT2], and leucine-rich

164 flammation are tonically inhibited by NO --> VASP signal transduction, and that reduced NO --> VASP s

165 Our data implicate endothelial NO --> VASP signaling as a physiological determinant of macroph

166 signal transduction, and that reduced NO --> VASP signaling is involved in the effect of HFD feeding

167 omain 1) binding domains of Lpd and the host VASP (vasodilator-stimulated phosphoprotein) recruited t

168 e binding modes and provides a model for how VASP promotes actin filament assembly.

169 It is not fully understood how VASP directly functions in actin-based motility and how

170 tion of the actin-regulatory proteins HSP20, VASP, cofilin, and paxillin.

171 erty of Ena/VASP homologues, including human VASP and Caenorhabditis elegans UNC-34.

172 Here we identify VASP as a novel substrate for protein kinase D1 (PKD1).

173 he actin-binding protein profilin1 (Pfn1) in VASP-mediated regulation of cell motility.

174 this PKD1-mediated phosphorylation switch in VASP is increased filopodia formation and length at the

175 cAMP and significantly reduced SOCE-induced VASP and CREB phosphorylation.

176 TSP-1 also inhibited VASP phosphorylation stimulated by the nonhydrolyzable c

177 The elongation mechanism involves VASP oligomerization and its binding to profilin, a G-ac

178 SP reduces VASP filopodial tip localization, VASP dynamics at tips, and filopodial stability.

179 even with 300 mg daily of clopidogrel, mean VASP PRI was 68.3% (95% CI, 44.9%-91.6%) and mean PRU, 2

180 r in response to RhoA activation and mediate VASP re-localization from focal contacts to the leading

181 y and recruits Ena/VASP proteins (Ena, Mena, VASP, EVL) to the leading edge of cells.

182 onger localizes to the leading edge and Mena/VASP is non-functional.

183 on and collaboration between Arp2/3 and Mena/VASP networks exist at different PFN1 concentrations.

184 the leading edge, where both Arp2/3 and Mena/VASP-based filament assembly was inhibited.

185 PKA activation, and phosphorylation of Mena/VASP proteins as well as growth cone morphology and neur

186 Vinculin, in turn, directly recruits Mena/VASP proteins to support junctional actin assembly.

187 ASP from vinculin or ectopically target Mena/VASP to junctions, we show that tension-sensitive actin

188 cytoskeletal regulatory proteins of the Mena/VASP (vasodilator-stimulated phosphoprotein) family.

189 By combining strategies that uncouple Mena/VASP from vinculin or ectopically target Mena/VASP to ju

190 Moreover, VASP increases the amount of PSD-scaffolding proteins an

191 Moreover, VASP localizes both to adhesion complexes and to the lea

192 We explored the role of multiple VASP variants.

193 phosphorylation by expression of the mutant VASP S157A in ASM tissues suppressed VASP phosphorylatio

194 Our findings also identify the NO/VASP pathway as a novel potential target for the treatme

195 nt platelet reactivity than did noncarriers (VASP platelet reactivity index [PRI]: mean, 70.0%; 95% C

196 ingly, expression of formin variants but not VASP reduced lamellipodial protrusion in B16-F1 cells, a

197 emonstrate that SHIP2 recruits Mena, but not VASP, to invadopodia and that disruption of SHIP2-Mena i

198 The ability of VASP to modulate spine and synapse formation, maturation

199 Activation of VASP by the phosphodiesterase-5 inhibitor, sildenafil, i

200 Coexpression of VASP with constitutively active mDia2(M/A) rescued these

201 protrusion waves in which local depletion of VASP from the leading edge by adhesions-along with later

202 ated with this ligand showed displacement of VASP from focal adhesions, as well as from the front of

203 We show that disruption of VASP results in significant hepatic steatosis as a resul

204 interfering ligases is a critical element of VASP dynamics, filopodial stability, and axon guidance.

205 associated with increased mRNA expression of VASP (vasodilator-stimulated phosphoprotein).

206 ACh but not FSK triggered the formation of VASP-VASP complexes as well as VASP-vinculin and VASP-pr

207 eptor function as ADP-mediated inhibition of VASP phosphorylation was unchanged.

208 Inhibition of VASP Ser(157) phosphorylation by expression of the mutan

209 The interaction of VASP with activated vinculin at membrane adhesion sites

210 ASP complex formation and the interaction of VASP with vinculin and profilin were inhibited by expres

211 Overexpression of VASP in hepatocytes increased AMPK phosphorylation and f

212 ymerization rates and that overexpression of VASP, an actin anti-capping protein that promotes actin

213 Rac1, a binding partner of VASP, acts in tandem with VASP to regulate FAs.

214 ons through AMPK-mediated phosphorylation of VASP, and thereby halts stress fiber elongation and ensu

215 MP concentrations and the phosphorylation of VASP, indicating that TSP-1 modulated the cAMP/PKA signa

216 stimulates actin assembly in the presence of VASP and Mena in vitro, but CRMP-1-dependent actin assem

217 vel model in which coordinated regulation of VASP ubiquitination by a pair of interfering ligases is

218 thodologies, we demonstrate a requirement of VASP for optimal development of FAs and cell spreading i

219 lly, we show evidence for the requirement of VASP to form tetramers and provide an amended model of p

220 ay smooth muscle (ASM); however, the role of VASP in regulating actin dynamics in ASM is not known.

221 These studies identify a role of VASP to enhance hepatic fatty acid oxidation by activati

222 gradient of TRIM9-mediated ubiquitination of VASP creates a filopodial stability gradient during axon

223 strate that TRIM9-mediated ubiquitination of VASP reduces VASP filopodial tip localization, VASP dyna

224 ve siRNA knockdown approach and a variety of VASP mutants coupled with complementary cell imaging met

225 ular localization and enhances its effect on VASP polymerase activity.

226 Epac or PKA, determined by Rap1 activity or VASP phosphorylation, respectively.

227 pho-vasodilator-stimulated phosphoprotein (p-VASP) by isoproterenol (ISO), prostaglandin E(2) (PGE(2)

228 n1 potentially negatively regulates the Pfn1-VASP interaction.

229 on of vasodilator-stimulated phosphoprotein (VASP) and CREB.

230 Vasodilator-stimulated phosphoprotein (VASP) and Ena-VASP-like (EVL) are cytoskeletal effector

231 Vasodilator-stimulated phosphoprotein (VASP) can catalyze actin polymerization by elongating ac

232 (Ena)/vasodilator-stimulated phosphoprotein (VASP) homology 1 (EVH1) domains.

233 on of vasodilator-stimulated phosphoprotein (VASP) in washed human or mouse platelets.

234 Vasodilator-stimulated phosphoprotein (VASP) is active in many filopodium-based and cytoskeleto

235 ilator-associated stimulated phosphoprotein (VASP) level measured predose and after each 12-day treat

236 otein vasodilator-stimulated phosphoprotein (VASP) regulates the density, size, and morphology of den

237 ether vasodilator-stimulated phosphoprotein (VASP) signaling improves lipid metabolism in the liver a

238 (Ena)/vasodilator-stimulated phosphoprotein (VASP), a family of conserved actin-elongating proteins,

239 on of vasodilator-stimulated phosphoprotein (VASP), a key downstream mediator of intracellular NO sig

240 on of vasodilator-stimulated phosphoprotein (VASP), a key downstream target of endothelially derived

241 ilator-associated stimulated phosphoprotein (VASP).

242 , the vasodilator-stimulated phosphoprotein (VASP).

243 otein vasodilator-stimulated phosphoprotein (VASP).

244 mber, vasodilator-stimulated phosphoprotein (VASP); however, a role for VASP in FA development has be

245 ults (vasodilator-stimulated phosphoprotein [VASP] phosphorylation and VerifyNow P2Y(12) assays) and

246 Phosphorylated VASP abrogates the augmented polymerization normally obs

247 assay and a Western blot for phosphorylated VASP, we determined that cAMP levels increase upon plate

248 Levels of phosphorylated VASP were diminished, and PTHrP levels were dysregulated

249 Moreover, RSK1 phosphorylated VASP on T278, a site regulating its binding to actin.

250 of the short F-actin pool and phosphorylates VASP on serine 153.

251 We show that PKD1 directly phosphorylates VASP at two serine residues, Ser-157 and Ser-322.

252 r-stimulated phosphoprotein phosphorylation (VASP-P).

253 he liver through mechanisms related to a PKG/VASP/NF-kappaB/NLRP3 inflammasome circuit.

254 k found that the filopodial actin polymerase VASP and consequently filopodial stability are negativel

255 and ubiquitinates the barbed-end polymerase VASP to modulate filopodial stability during netrin-depe

256 s and provide an amended model of processive VASP-mediated actin assembly in clustered arrays.

257 ent, VASP is deubiquitinated, which promotes VASP tip localization and filopodial stability.

258 PKA-modulated phosphorylation of the protein VASP.

259 otein vasodilator-activated phospho-protein (VASP), although the formation and morphology of focal ad

260 e found that vasodilator-stimulated protein (VASP) exhibits high affinity for S-nitrosylated short fi

261 Rather, VASP recruits F-actin seeds from the solution and promot

262 arriers (mean ratios of platelet reactivity, VASP PRI, 0.92; 90% CI, 0.85-0.99, and PRU, 0.94; 90% CI

263 lamellipodin (Lpd) that subsequently recruit VASP and initiate filopodia formation.

264 Zyxin-deficient cells failed to recruit VASP to cell-cell junctions at the wound edge and had a

265 Our results suggest that, by recruiting VASP, zyxin regulates actin assembly at the sites of for

266 RIM9-mediated ubiquitination of VASP reduces VASP filopodial tip localization, VASP dynamics at tips,

267 alidation revealed that the actin regulators VASP and Mena interact with RSK1.

268 With this integrated representation, VASP-E is able to dissect the electrostatic environments

269 apses, whereas expression of siRNA-resistant VASP rescued this defect.

270 ctrostatic influence on binding specificity, VASP-E identified electrostatically influential amino ac

271 ACh and FSK stimulated VASP Ser(157) phosphorylation by different kinases.

272 vel biomarkers of drug response and suggests VASP as a potential determinant of thiazide diuretics BP

273 mutant VASP S157A in ASM tissues suppressed VASP phosphorylation and membrane localization in respon

274 At steady state, it entails that tetrameric VASP uses one of its arms to processively track growing

275 s its localization at the membrane, but that VASP Ser(157) phosphorylation and membrane localization

276 We conclude that VASP phosphorylation at Ser(157) mediates its localizati

277 We found that VASP's interaction with Pfn1 is promoted by cell-substra

278 Our results show that VASP is a critical regulator of actin dynamics and tensi

279 ent with our model simulations, we show that VASP localization at the leading edge oscillates, with V

280 We also show that VASP-E can accurately classify closely related ligand bi

281 These results suggest that VASP-E should prove a useful tool for the characterizati

282 onomers to the filament tip, suggesting that VASP operates as a single tetramer in solution or when c

283 nase G (PKG)-mediated phosphorylation of the VASP (vasodilator-stimulated phosphoprotein) Ser239 resi

284 Moreover, baseline expression of the VASP mRNA was significantly higher in 25 good responders

285 P-proline-rich domain and the binding of the VASP-F-actin binding domain to the side of growing filam

286 We found that the VASP-F-actin binding domain is required for the recruitm

287 bly proceeded with the same rate as with the VASP tetramer, demonstrating that adjacent VASP molecule

288 raction of profilin-actin complexes with the VASP-proline-rich domain and the binding of the VASP-F-a

289 Consistent with this, VASP significantly enhances the retention of GluR1 in sp

290 in and its EVH1 domain, which contributes to VASP localization to actin-rich structures.

291 Upon netrin treatment, VASP is deubiquitinated, which promotes VASP tip localiz

292 al neurons, along with a non-ubiquitinatable VASP mutant, demonstrate that TRIM9-mediated ubiquitinat

293 d via Density Functional Theory method using VASP software.

294 lection fluorescence microscopy to visualize VASP tetramers interacting with static and growing actin

295 metabolism in the liver and, if so, whether VASP's effects are mediated by AMPK.

296 RIM67 outcompetes TRIM9 for interacting with VASP and antagonizes TRIM9-dependent VASP ubiquitination

297 ization at the leading edge oscillates, with VASP leading-edge enrichment greatest just prior to prot

298 nificantly reduced platelet reactivity, with VASP PRI decreasing to 48.9% (95% CI, 44.6%-53.2%) and P

299 binding partner of VASP, acts in tandem with VASP to regulate FAs.

300 tin bundles that grow from the surface of WT-VASP-coated beads induced movement of the beads.