ライフサイエンスコーパス: barbed end

1 association of CP with and affinity for the barbed end.

2 on to and high affinity interaction with the barbed end.

3 AtFH14 moves processively on the elongating barbed end.

4 filaments or by dissociating Cdc12p from the barbed end.

5 de novo and stay associated with the growing barbed end.

6 the ability of capping protein to block the barbed end.

7 1-mediated transfer of actin subunits to the barbed end.

8 w that tropomyosin regulates dynamics at the barbed end.

9 and reduces the rate of elongation from the barbed end.

10 affinity and decreases its affinity for the barbed end.

11 vitro to render it incapable of binding the barbed end.

12 ation of actin-binding regions of FH2 to the barbed end.

13 of the formin mDia1 simultaneously bind the barbed end.

14 associating with, and dissociating from, the barbed end.

15 nto a version with moderate affinity for the barbed end.

16 (CAPZ), which blocks actin polymerization at barbed ends.

17 nishing the filament subpopulation with free barbed ends.

18 rization of actin filaments by capping their barbed ends.

19 ation of active ADF/cofilin and free F-actin barbed ends.

20 In addition, the C terminus binds filament barbed ends.

21 g activity of cofilin to generate actin-free barbed ends.

22 o control cofilin's generation of actin-free barbed ends.

23 port of G-actin monomers to the polymerizing barbed ends.

24 and delivering ATP-actin to growing filament barbed ends.

25 in-mediated processive elongation of growing barbed ends.

26 y displaces the Bnr1 FH2 domain from growing barbed ends.

27 ermediates with lowered affinity for CapZ at barbed ends.

28 oated surfaces via interactions with growing barbed ends.

29 wever, CYK-1 rapidly re-associates with free barbed ends.

30 n, helps to maintain Ena/VASP at the growing barbed ends.

31 s at concentrations that block CP binding to barbed ends.

32 cement of filament growth from newly created barbed ends.

33 mote flux of subunits through actin filament barbed ends.

34 hange and delivery of subunits onto filament barbed ends.

35 ormin homology 2 (FH2) domains with filament barbed ends.

36 rocessively associated with the fast-growing barbed ends.

37 hibit elongation and subunit dissociation at barbed ends.

38 ifically inhibits filament elongation at the barbed ends.

39 filaments capped by Cdc12p to grow at their barbed ends.

40 (Acp1p and Acp2p) that binds actin filament barbed ends.

41 estering actin monomers and capping filament barbed ends.

42 ing and remains bound to the newly generated barbed ends.

43 and restraining elongation to remaining free barbed ends.

44 ely active, diffusing freely to find and cap barbed ends.

45 han the diffusion-limited rate of unattached barbed ends.

46 gather and simultaneously elongate multiple barbed ends.

47 mn2 alternately kick off each other from the barbed ends.

48 opodia-like F-actin networks without tapered barbed ends.

49 vivo, and is proposed to cap actin filament barbed ends.

50 n lifetime when force was applied toward the barbed (+) end.

51 partly invaginated CCSs with actin filament barbed ends abutting the CCS neck, to a polarized comet

52 the absence of profilin, but profilin slows barbed-end acceleration from constructs containing the P

53 ion of the Arp2/3 complex with CK666 reduced barbed end actin assembly site density at the leading ed

54 sistant to cytochalasin D that inhibits fast barbed end actin assembly.

55 Adducin functions as a barbed-end actin capping protein to regulate actin filam

56 factors Diaphanous and Enabled both promote barbed-end actin polymerization and can stimulate filopo

57 ndling by either FRL1 or mDia2, but inhibits barbed end activities.

58 at tension is generated by myosin pulling on barbed-end-anchored actin filaments in a stochastic slid

59 her proteins, including formins, bind at the barbed end and allow filament growth.

60 agonizes CP by reducing its affinity for the barbed end and by uncapping CP-capped filaments, whereas

61 within dendritic spines, as revealed by free-barbed end and FRAP assays, consistent with a role for E

62 ly accessible site on CP bound to a filament barbed end and inducing a change in the conformation of

63 ent nucleation then remain on the elongating barbed end and modulate filament elongation.

64 ments, whereas capping protein (CP) binds to barbed ends and arrests polymerization.

65 Capping protein (CP) is known to regulate barbed ends and control actin assembly in cells.

66 at Lpd delivers Ena/VASP proteins to growing barbed ends and increases their polymerase activity by t

67 homology 2 (FH2) domain that binds filament barbed ends and is critical for polymerization and depol

68 s associate processively with actin-filament barbed ends and modify their rate of growth.

69 has shown that FH2 domains bind to filament barbed ends and move processively at the barbed end as t

70 mechanism by which Spire and Fmn2 compete at barbed ends and the role of FSI in orchestrating this co

71 ctin polymerisation rates in the presence of barbed-end and pointed-end cappers, we further demonstra

72 , AIP1 actively disassembles filaments, caps barbed ends, and binds to the side of filaments.

73 tivating Arp2/3, N-WASP binds actin-filament barbed ends, and both N-WASP and barbed ends are tightly

74 resulting from addition of monomers to free barbed ends, and one with slow turnover dynamics with po

75 duce a rapid biphasic increase in actin free barbed ends, and we found both phases absent in fibrobla

76 rates and the critical concentration at the barbed end are intimately related to cap structure and d

77 s revealed an aster of actin filaments whose barbed ends are focalized near the plasma membrane.

78 nched actin network, in which actin filament barbed ends are oriented toward the CCS.

79 rsing melanosomes along actin tracks whose +/barbed ends are oriented toward the plasma membrane.

80 ccurs only at low activation rates, when few barbed ends are produced.

81 in-filament barbed ends, and both N-WASP and barbed ends are tightly clustered in these invasive stru

82 ent barbed ends and move processively at the barbed end as the filament elongates.

83 In addition, FSI binds actin at filament barbed ends as a weak capper and plays a role in displac

84 has a small but measurable affinity for the barbed end, as inferred from previous studies and kineti

85 te, and bundle filaments by associating with barbed ends, as well as in their use of WH2 motifs and o

86 G-actin in 1:2 complexes that participate in barbed end assembly.

87 clustered N-WASP affects Arp2/3-independent barbed-end assembly.

88 in complexes and deliver them rapidly to the barbed end associated with the FH2 domain.

89 ology 1 (FH1) domain from one formin and the barbed-end associated FH2 domain from the other formin,

90 lin-actin with the FH1 domain as well as the barbed-end associated FH2 domain.

91 Saturating phosphate increases the barbed end association rate constant of Mg-ADP-actin 15%

92 ation for the actin filament's growth at the barbed end, assuming the sequential release of phosphate

93 cofilin can sever actin filaments to create barbed ends at invadopodia to support Arp2/3-dependent a

94 Newly generated actin free barbed ends at the front of motile cells provide sites f

95 zed filaments shrink rapidly, primarily from barbed ends, at 1.8/s, but as they age they switch to a

96 ding but promote high affinity (K(d) = 9 nM) barbed end attachment.

97 rs to be unable to bind to CP that is on the barbed end, based on the observations that V-1 had no ac

98 how two actin regulators, capping protein, a barbed end binding protein, and the Arp2/3 complex, a po

99 Surprisingly, neither mutation abolishes barbed end binding, as judged by pyrene-actin and total

100 he mutation strongly inhibits all effects of barbed end binding, but affects FRL1 much less strongly.

101 t FRL1-mediated bundling is competitive with barbed end binding, whereas mDia2-mediated bundling is n

102 Point mutagenesis reveals that reducing the barbed-end binding activity of FRL1 and mDia2 greatly en

103 ses that deliver multiple actin monomers per barbed end-binding event and effectively antagonize fila

104 ith a requirement of accelerated assembly on barbed-end bundling.

105 by itself associates very poorly to filament barbed ends but is rapidly recruited to Spire-capped bar

106 ng influence on dissociation of formins from barbed ends but only a weak effect on elongation rates.

107 nd PI(3,4,5)P(3), prevent CP from binding to barbed ends, but three different assays showed that none

108 Further, mDia1 displaced from the barbed end by CP can randomly slide along the filament a

109 nd modulates formin-dependent capping of the barbed end by relieving inhibition of elongation by FRL1

110 filopodia of uniform thickness with aligned barbed ends by a unique mechanistic cycle.

111 d lamellipodial assembly features capping of barbed ends by CP, and the formation of filopodia is pro

112 Precapped filament barbed ends can also be uncapped by addition of PA, allo

113 vitro; instead, they were proposed to act as barbed end cappers or filament bundlers.

114 hese results can explain how V-1 inactivates barbed end capping by CP and why V-1 is incapable of unc

115 Here we show that in the mouse cochlea the barbed end capping protein twinfilin 2 is present at the

116 K113E actin polymerization, consistent with barbed end capping.

117 evering, whereas G1 and G2 were required for barbed end capping.

118 omain regulate actin assembly and processive barbed-end capping by the FH2 domain.

119 CapZ and cytochalasin D (CytoD), a barbed-end capping drug, strongly inhibit bursting disas

120 /CD2AP and a previously unrecognized role of barbed-end capping in junctional actin dynamics.

121 has not been defined, although severing and barbed-end capping of actin filaments have been proposed

122 Mena, an actin barbed-end capping protein antagonist, is expressed as v

123 iated protein (FSGS3/CD2AP) as a novel actin barbed-end capping protein responsible for actin stabili

124 way substrate 8 (Eps8; an actin bundling and barbed-end capping protein) and actin-related protein 3

125 orescence microscopy, we found that ABP29, a barbed-end capping protein, competes with FH1-FH2 at the

126 rk assembly at the leading edge by promoting barbed-end capping there.

127 able alterations in actin disassembly and/or barbed end-capping activities, suggesting that both acti

128 e we show that this interaction inhibits the barbed end-capping activity of CP.

129 d actin polymerization protein Arp3, and the barbed end-capping and bundling protein Eps8, illustrati

130 dent actin depolymerization factor and not a barbed-end-capping factor as was previously thought.

131 Individual barbed ends captured by WWCA domains grow at or below th

132 ow that CAH3 binds CP already present on the barbed end, causing a 300-fold increase in the dissociat

133 Two important regulators of free barbed ends, cofilin and Arp2/3, have been shown to work

134 ong electrostatic binding site for CP on the barbed end compete for this basic patch on CP.

135 3 increased, with the half-time of CP at the barbed end decreasing from approximately 30 min without

136 V, VC, and VCA enhance barbed end depolymerization like profilin but neither nu

137 We show that myosin 15-S1 is a barbed-end-directed motor that moves actin filaments in

138 Moreover, in these processes, barbed ends directly push onto the load, as in a convent

139 berrant regulation of F-actin and actin free barbed ends dynamics.

140 runs, allowing them to catch up with leading barbed ends efficiently.

141 ofilin with the FH1 domain speeds processive barbed end elongation by FH2 domains.

142 combined inhibition of actin nucleation and barbed end elongation by profilin and SpTm.

143 tary mechanisms that regulate actin filament barbed end elongation in Arp2/3-derived networks.

144 atial and temporal control of actin filament barbed end elongation is crucial for force generation by

145 inus inhibits actin polymerization and slows barbed end elongation with moderate affinity.

146 over actin subunits through a combination of barbed end elongation, severing, and WH2 motif-mediated

147 ional proteins that work together to inhibit barbed end elongation.

148 ers and displays high affinity inhibition of barbed end elongation.

149 ex with cortactin that blocks actin filament barbed end elongation.

150 reated by complex exchange slows the rate of barbed-end elongation by rapidly associating with, and d

151 concentrations (0.5-25 microM), the rate of barbed-end elongation increases with the number of polyp

152 at the N-terminal ABD1 blocks actin filament barbed-end elongation, whereas ABD2 and ABD3 do not show

153 that interact with each other for processive barbed-end elongation.

154 other and together accelerate actin filament barbed-end elongation.

155 inding protein profilin-increase the rate of barbed-end elongation.

156 lament, whereas profilin:actin only supports barbed-end elongation.

157 ersistently associated with the fast-growing barbed end, enabling rapid insertion of actin subunits w

158 assay for Drosophila embryos, which revealed barbed end enrichment at junctions.

159 Cytochalasin-D inhibition of barbed-end exchange reduces rhodamine-actin incorporatio

160 e filaments are largely organized with their barbed ends facing the cell tip, where for3p is thought

161 tes dissociation of FH2 domains from growing barbed ends, FH2 domains must pass through a state that

162 ruitment of actin-capping protein, revealing barbed-end filament capping at endocytic sites to be a r

163 ts Fmn2 and facilitates its association with barbed ends, followed by rapid processive assembly and r

164 y remaining processively associated with the barbed end for an average of approximately 10 s in solut

165 ivity of cofilin, a protein that creates new barbed ends for actin filament elongation, amplifies and

166 may explain the inhibitory effects of PKD on barbed end formation as well as on directed cell migrati

167 ion to activate cofilin, promotes actin free barbed end formation, accelerates actin turnover, and en

168 After barbed end formation, cortactin is dephosphorylated, whi

169 small inhibitory RNA abrogates enhanced free barbed end formation, increased actin polymerization, an

170 bsequent Rac activation increases actin free barbed end formation.

171 tactin phosphorylation and cofilin-dependent barbed-end formation at invadopodia, leading to a signif

172 profilin-actin is transferred rapidly to the barbed end from multiple profilin binding sites in formi

173 ctin assembly and protected growing filament barbed ends from capping protein.

174 for estimation of the concentration of free barbed ends from pyrene intensity curves.

175 New growth at barbed ends generated by severing was blocked specifical

176 Rapid polymerization of actin filament barbed ends generates protrusive forces at the cell edge

177 n by promoting actin polymerization via free barbed end generation and centripetal elongation of an F

178 The C helix is likely to bind to the barbed end groove of Arp3 in a position for VCA to deliv

179 nts of the phosphate clamp, cleft mouth, and barbed-end groove, providing a way for changes in the nu

180 Dissociation of formins from barbed ends growing in the presence of profilin is propo

181 in polymerization ~18 times faster than free-barbed-end growth while simultaneously enhancing protect

182 alphaE-catenin ABD binding limits barbed-end growth, especially in actin filament bundles.

183 GSNL-1 severs actin filaments and caps the barbed end in a calcium-dependent manner similar to that

184 SNL-1 severed actin filaments and capped the barbed end in a calcium-dependent manner.

185 s remarkably slow and restricted to filament barbed ends in a small tip compartment, with minimal acc

186 etes with capping protein for actin filament barbed ends in cells.

187 ament length and for the capture of filament barbed ends in cells.

188 otein (CP), a major capper of actin filament barbed ends in cells.

189 Ena-associated trailing barbed ends in Fascin-bundled actin filaments have appro

190 drive the processive elongation of filament barbed ends in membrane protrusions or at the surface of

191 rotein may slowly replace Cdc12p on filament barbed ends in preparation for filament disassembly duri

192 embly in which any cluster of actin filament barbed ends in proximity to the plasma membrane, either

193 actin cytoskeletal polarity by developing a barbed end incorporation assay for Drosophila embryos, w

194 sembly of actin filaments that grow at their barbed ends, independent of eukaryotic factors.

195 Each FH1 domain transfers actin to the barbed end independently of the other and structural evi

196 ns tunes the processive association with the barbed end, indicating that this is a general role for f

197 es showed that the binding of formins to the barbed end induces conformational transitions in actin f

198 WCA mutants, and that capping actin filament barbed ends inhibited endosome motility but not endocyti

199 The affinity of fission yeast CP for barbed ends is a thousandfold less than mouse CP, becaus

200 The regulation of free barbed ends is central to the control of dynamic actin a

201 itate the localized generation of free actin barbed ends, leading to membrane protrusion.

202 force, interactions between WH2 domains and barbed ends may locally amplify signals for dendritic ac

203 ting from one end and developing towards the barbed end might be involved in force generation and dir

204 s actin filament assembly and remains at the barbed end, modulating elongation.

205 opodial base and diffuse toward the filament barbed ends near the tip.

206 They attach to the barbed end of a filament and prevent polymerization, lea

207 sis shows how the binding of profilin to the barbed end of actin causes a rotation of the small domai

208 heads swing forward alternately towards the barbed end of actin driven by ATP hydrolysis.

209 formin, AtFH14, processively attaches to the barbed end of actin filaments as a dimer and slows their

210 s, function as homodimers that bind with the barbed end of actin filaments through a ring-like struct

211 CP binds with high affinity to the barbed end of actin filaments, blocking the addition and

212 of the actin cytoskeleton by binding to the barbed end of actin filaments.

213 ittle effect on Capu once it is bound to the barbed end of an elongating filament.

214 ivation the first actin monomer binds at the barbed end of Arp2.

215 ently inhibits nucleation and binding to the barbed end of elongating filaments by the C-terminal hal

216 brin inhibits depolymerization mainly at the barbed end of F-actin.

217 n the same strand but probably closer to the barbed end of F-actin.

218 It binds to the barbed end of filaments with high affinity and modulates

219 elerate elongation, although it binds to the barbed end of filaments.

220 ofilin-actin from the cellular pool onto the barbed end of growing filaments.

221 %) associate for approximately 25 s with the barbed end of preassembled filaments, inhibiting their e

222 The probe angle relative to the barbed end of the actin (beta) averaged 128 degrees whil

223 expressed, 62-kDa heterodimer that binds the barbed end of the actin filament with approximately 0.1

224 heterodimeric 62-kDa protein that binds the barbed end of the actin filament with high affinity to b

225 and the molecular basis for how CP binds the barbed end of the actin filament, we have used a combina

226 fidelity of information communicated at the barbed end of the actin filament.

227 and cell motility by binding tightly to the barbed end of the actin filament.

228 rmin Homology 2 (FH2) domain dimers with the barbed end of the filament, allowing subunit addition wh

229 P interacts with both actin protomers at the barbed end of the filament, and the amphipathic helix at

230 in complexes into contact with the FH2-bound barbed end of the filament, thereby enabling direct tran

231 in is proposed to be in position to join the barbed end of the growing filament concurrently with the

232 he cell allow capping protein to bind to the barbed ends of actin filaments and Arp2/3 complex to bin

233 concentration of capping protein, which caps barbed ends of actin filaments and prevents elongation,

234 muscles near or on sarcomere Z lines, where barbed ends of actin filaments are anchored.

235 ing proteins bind to and dissociate from the barbed ends of actin filaments by observing single muscl

236 The barbed ends of actin filaments in striated muscle are an

237 e interaction of N-WASP with GRB2 and/or the barbed ends of actin filaments increases its exchange ra

238 min proteins associate processively with the barbed ends of actin filaments through many rounds of ac

239 also demonstrate that Aip1 does not cap the barbed ends of actin filaments, as was previously though

240 VASP induces and maintains clustering of the barbed ends of actin filaments, which putatively corresp

241 nding inhibited the ability of CP to cap the barbed ends of actin filaments.

242 The alpha/beta-heterodimer caps the barbed ends of an actin filament and restricts its growt

243 Myosin-5 walks toward the barbed ends of F-actin, traveling to sites of actin poly

244 Aip1 does not cap the barbed ends of filaments severed by cofilin.

245 Capping protein (CP) binds to barbed ends of growing actin filaments and inhibits elon

246 ngly, a loss of the uniform alignment of the barbed ends of the actin filaments.

247 ion due to addition of actin monomers to the barbed ends of the filaments.

248 ing nurse cell dumping, Enabled localizes to barbed ends of the nurse cell actin filaments, suggestin

249 the cleft separating domains 1 and 3 at the barbed-end of actin.

250 Localization of Fhos to the barbed-ends of the arrays, achieved via a novel N-termin

251 nd Arp2/3 can each generate a large pulse of barbed ends on their own, but have little synergy; high

252 equilibrates between two bound states at the barbed end: one permitting monomer binding and the other

253 st G-actin compared with muscle actin in the barbed end pivot region and areas in subdomains 1 and 2

254 een inferred that the regulation of filament barbed ends plays a central role in choreographing actin

255 or DCC, interacts with and ubiquitinates the barbed-end polymerase VASP to modulate filopodial stabil

256 rsion between these states allows processive barbed-end polymerization and depolymerization in the pr

257 patially distributed model, both synergy and barbed-end production are significant over a range of ac

258 Furthermore, barbed-end production is greatest when Arp2/3 activation

259 and promotes its displacement from filament barbed ends providing insight into possible modes of coo

260 athway where filaments grow transiently from barbed ends, rapidly terminate growth to enter a long-li

261 The barbed end rate constants for mouse capping protein (CP)

262 by interacting directly with actin filament barbed ends, recruiting profilin-actin, and blocking cap

263 We specifically consider key barbed-end regulators such as capping protein and formin

264 gonizes capping protein but dissociates from barbed ends relatively quickly.

265 We show that by capping filament barbed ends, Spire recruits Fmn2 and facilitates its ass

266 drugs that release mDia1 from actin filament barbed ends, stimulated stable MT formation in serum-sta

267 depolymerization of the pointed end than the barbed end, suggesting a weak affinity of phosphate near

268 Binding of open II vinculin to the barbed-end suggests this conformation allows for vinculi

269 Proteins that cap the barbed end terminate this elongation.

270 ly less effective at processively elongating barbed ends than most well studied formins.

271 Capping protein (CP) binds to free barbed ends, thereby arresting microfilament growth and

272 tivity, and elevated formation of actin free barbed ends, thus restoring normal beta(2) integrin func

273 nal tail from a hydrophobic groove at Arp3's barbed end to destabilize the inactive state, providing

274 and it subsequently displaces Spire from the barbed end to elicit rapid processive assembly from prof

275 e along the filament and later return to the barbed end to re-form the complex.

276 Cdc12p allows barbed ends to elongate in the presence of excess cappin

277 ment by transiently attaching actin filament barbed ends to the membrane.

278 ulin restricts the position of thin filament barbed ends to the Z-disc via a direct interaction with

279 filaments are uniformly oriented with their barbed ends toward stereocilia tips.

280 a population of reversed filaments with the barbed-end toward the cell center.

281 ne-dimensional diffusion, and (3) processive barbed end tracking.

282 eas several proteins cap the rapidly growing barbed end, tropomodulin (Tmod) is the only protein know

283 While several proteins cap the barbed end, tropomodulins (Tmods), a family of four clos

284 tment of peripheral filaments and continuous barbed-end turnover.

285 ults offer a mechanistic explanation for the barbed end uncapping activity of CARMIL, and they identi

286 ts by interacting with both S1 and S3 of the barbed-end, using the surface of Vt normally occluded by

287 recently demonstrated how Spire, which caps barbed ends via its WH2 domains, activates Fmn2.

288 nds but is rapidly recruited to Spire-capped barbed ends via the KIND domain, and it subsequently dis

289 in-profilin interface, Ala(167) of the actin barbed end W-loop and His(372) near the C terminus form

290 ation during translocation along the growing barbed end, we propose that the flexible linker influenc

291 Ena/VASP proteins regulate actin dynamics at barbed ends, we monitored individual actin filaments gro

292 strating its role in length maintenance; the barbed ends were unaffected.

293 otein, competes with FH1-FH2 at the filament barbed end, where its binding is mutually exclusive with

294 Drosophila Fhod binds tightly to barbed ends, where it slows elongation in the absence of

295 tue of its ability to cap the actin filament barbed end, which promotes Arp2/3-dependent filament nuc

296 processively associated with the elongating barbed end while driving the addition of profilin-actin.

297 processively associated with the elongating barbed end while facilitating the addition of profilin-a

298 d, with mDia1 moving processively on growing barbed ends while APC remained at the site of nucleation

299 eing rapidly polymerized by formins at their barbed ends while simultanteously being stochastically s

300 arms to processively track growing filament barbed ends while three G-actin-binding sites (GABs) on