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 phosphorylation was evaluated using phosphorylation

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

6 VASP-E exploits the central observation that three dimen

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

8 VASP-VASP complex formation and the interaction of VASP

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

10 ter with potential binding partners: SLP-76, VASP, and SKAP-HOM.

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

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

13 d the E2-induced increase in PKG-I activity, VASP/p-VASP expression.

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

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

16 filaments grew faster in profilin-actin and VASP than with profilin-actin alone.

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

18 fiber damage, whereas both alpha-actinin and VASP independently contribute to limiting stress fiber e

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

20 ndothelial permeability, Rac1 activation and VASP phosphorylation are prevented by overexpression of

21 ssion/phosphorylation, PKG-I activation, and VASP/p-VASP expression, which paralleled a decrease in l

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

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

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

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

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

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

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

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

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

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

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

33 s with these pathways: uPA, uPAR, LASP1, and VASP.

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

35 ics and lack of two family members, Mena and VASP, in mice results in failure of neural tube closure.

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

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

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

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

40 Similar results were observed by VN and VASP.

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

42 , CO selectively promotes phosphorylation at VASP Ser-157, whereas NO promotes phosphorylation primar

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

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

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

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

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

48 Actin filaments were captured directly by VASP-coated surfaces via interactions with growing barbe

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

50 in bundle formation and motility mediated by VASP.

51 Filament growth was unchanged by VASP, but filaments grew faster in profilin-actin and VA

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

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

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

55 Conversely, VASP deficiency induced proinflammatory M1 macrophage ac

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

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

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

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

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

61 Ena/VASP (vasodialator-stimulated protein) proteins regulate

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

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

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

65 Ena/VASP proteins regulate the actin cytoskeleton during cel

66 Ena/VASP proteins, a conserved family of actin-regulatory pr

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

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

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

70 Mena, an Ena/VASP protein, is upregulated in the invasive subpopulati

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

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

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

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

75 how Diaphanous (Dia)-related formins and Ena/VASP proteins cooperate in this process.

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

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

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

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

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

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

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

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

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

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

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

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

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

89 at the lamellipodial tip (where it binds Ena/VASP), and this mediates the hypermotility.

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

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

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

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

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

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

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

97 signaling by Sprouty related with EVH1 (Ena/VASP homology 1) domain (Spred), a family of signaling i

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

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

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

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

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

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

104 Here we review recent findings into Ena/VASP function in neurite initiation, axon outgrowth and

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

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

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

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

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

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

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

112 3 complex and the elongating activity of Ena/VASP proteins for the formation of actin networks.

113 inking and putative scaffolding roles of Ena/VASP proteins.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

128 ivated Ras-GTPases with actin regulatory Ena/VASP proteins to induce local changes in cytoskeletal dy

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

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

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

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

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

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

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

136 Members of the Ena/VASP family of proteins are localized to sites of cellul

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

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

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

140 Thus, Ena/VASP proteins promote actin assembly by interacting dire

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

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

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

144 regulating actin filament elongation via Ena/VASP proteins.

145 In vitro, Ena/VASP activities on actin are complex and varied.

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

147 To determine the mechanisms by which Ena/VASP proteins regulate actin dynamics at barbed ends, we

148 The precise mechanism by which Ena/VASP proteins regulate this process, however, is not und

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 s of two important actin regulators: Enabled/VASP proteins and Capping protein.

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

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

154 sts, which express high levels of endogenous VASP.

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

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

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

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

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

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

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

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

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

164 ol EPCs and in HMECs exposed to low glucose, VASP was redistributed to filopodia-like structures foll

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

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

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

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

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

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

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

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

173 eficient in ADAP, but not those deficient in VASP or SKAP-HOM, failed to form these structures.

174 iabetic platelets, neither agent resulted in VASP phosphorylation.

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

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

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

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

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

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

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

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

189 We explored the role of multiple VASP variants.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

207 Overexpression of VASP in hepatocytes increased AMPK phosphorylation and f

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

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

210 Phosphorylation of VASP at Ser239 (p-VASP) can be used to assess PKG signal

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

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

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

214 l actin filaments growing in the presence of VASP and profilin using total internal reflection fluore

215 toskeletal remodeling through recruitment of VASP.

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

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

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

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

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

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

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

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

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

225 Phosphorylation of VASP at Ser239 (p-VASP) can be used to assess PKG signaling activity.

226 hosphorylation, PKG-I activation, and VASP/p-VASP expression, which paralleled a decrease in lung inj

227 2-induced increase in PKG-I activity, VASP/p-VASP expression.

228 on of vasodilator-stimulated phosphoprotein (VASP) and a subsequent down-regulation of Rac1 activity.

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

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

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

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

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

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

235 (PKG)/vasodilator-stimulated phosphoprotein (VASP) pathway.

236 (Ena)/vasodilator-stimulated phosphoprotein (VASP) proteins regulate cell motility by controlling the

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

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

239 on of vasodilator-stimulated phosphoprotein (VASP), a critical actin motor protein required for cell

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

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

242 ilator-associated stimulated phosphoprotein (VASP).

243 , the vasodilator-stimulated phosphoprotein (VASP).

244 otein vasodilator-stimulated phosphoprotein (VASP).

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

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

247 ylate vasodilator-stimulated phosphoprotein, VASP, after cGMP analog treatment.

248 Phosphorylated VASP abrogates the augmented polymerization normally obs

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

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

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

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

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

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

255 vely suggest that activation of the eNOS-PKG/VASP pathway by E2 protects against trauma-hemorrhage-in

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

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

258 m the Varicella Active Surveillance Project (VASP) were used to compare rates of hospitalization and

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

260 PKA-modulated phosphorylation of the protein VASP.

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

262 (LASP1), and vasodilator-stimulated protein (VASP) as a possible mechanism accounting for the loss of

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

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

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

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

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

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

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

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

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

272 changes through site- and cell type-specific VASP phosphorylation, and in diabetes, blunted responses

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

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

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

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

277 The observation that zyxin targets VASP, a partner of zyxin in regulation of actin assembly

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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.