ライフサイエンスコーパス: barbed end

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

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

3 ments as well as transient aggregates at the barbed end.

4 end sides of cofilactin clusters than at the barbed end.

5 cts compete to deliver profilin-actin to the barbed end.

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

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

8 filaments or by dissociating Cdc12p from the barbed end.

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

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

11 1-mediated transfer of actin subunits to the barbed end.

12 w that tropomyosin regulates dynamics at the barbed end.

13 AtFH14 moves processively on the elongating barbed end.

14 ing the rate of monomer incorporation at the barbed end.

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

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

17 of the formin mDia1 simultaneously bind the barbed end.

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

19 gather and simultaneously elongate multiple barbed ends.

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

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

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

23 nishing the filament subpopulation with free barbed ends.

24 rization of actin filaments by capping their barbed ends.

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

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

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

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

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

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

31 in-mediated processive elongation of growing barbed ends.

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

33 ermediates with lowered affinity for CapZ at barbed ends.

34 oated surfaces via interactions with growing barbed ends.

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

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

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

38 cement of filament growth from newly created barbed ends.

39 mote flux of subunits through actin filament barbed ends.

40 hange and delivery of subunits onto filament barbed ends.

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

42 estering actin monomers and capping filament barbed ends.

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

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

45 and restraining elongation to remaining free barbed ends.

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

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

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

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

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

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

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

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

54 In all cases, binding at the barbed end also occurred in a configuration similar to t

55 The ends are reeled in by barbed end-anchored actin filaments in adjacent segments

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

57 fission yeast, ring tension originates from barbed-end anchoring of actin filaments to the plasma me

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

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

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

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

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

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

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

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

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

67 differential affinities for actin monomers, barbed ends and polyproline are thus tuned to adaptively

68 unbranched actin filaments by binding their barbed ends and processively stepping onto incoming acti

69 We found that Spire is sufficient to bind barbed ends and retain pointed ends of actin filaments n

70 dly elongating filaments with mDia1 at their barbed ends and SPIN90-Arp2/3 at their pointed ends.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

95 laments near beads and we identified Spire's barbed-end binding domain.

96 Loss of barbed-end binding increases nucleation by Spire and syn

97 y the loss-of-function mutant indicates that barbed-end binding is not necessary for oogenesis.

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

99 Additional barbed end bound states were seen when the incoming subu

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

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

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

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

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

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

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

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

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

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

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

111 K113E actin polymerization, consistent with barbed end capping.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

127 3 increased, with the half-time of CP at the barbed end decreasing from approximately 30 min without

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

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

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

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

132 tin delivery and FH2-regulated gating of the barbed end effectively limits the elongation rate, there

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

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

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

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

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

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

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

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

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

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

143 ongly inhibiting both F-actin nucleation and barbed-end elongation at equimolar concentrations to act

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

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

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

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

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

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

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

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

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

153 merization for the ATP and ADP growth at the barbed end exactly matches experimental results.

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

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

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

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

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

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

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

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

162 After barbed end formation, cortactin is dephosphorylated, whi

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

164 bsequent Rac activation increases actin free barbed end formation.

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

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

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

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

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

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

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

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

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

174 By stopping barbed end growth, CP favors nucleation of daughter fila

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

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

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

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

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

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

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

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

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

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

185 favored by whatever means over the growth of barbed ends in the network.

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

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

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

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

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

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

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

193 that Ena's enhanced processivity on trailing barbed ends is specific to fascin bundles, with no enhan

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

213 %) associate for approximately 25 s with the barbed end of preassembled filaments, inhibiting their e

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

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

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

217 ced dynamics at the edge oriented toward the barbed end of the actin filament.

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

219 Subunits at the barbed end of the filament are likely to be in this favo

220 Rapid treadmilling, where the barbed end of the filament grows and the pointed end shr

221 Conversely, the barbed end of the filament takes on a conformation nearl

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

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

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

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

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

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

228 pping protein (CP) binds the rapidly growing barbed ends of actin filaments and prevents the addition

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

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

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

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

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

234 ive activity of lamellipodia, depends on the barbed ends of actin filaments, and requires both the LI

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

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

237 motility is driven by actin assembly at the barbed ends of core bundles, which in turn is linked to

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

239 threefold longer processive runs on trailing barbed ends of fascin-bundled F-actin.

240 Moreover, enhanced processivity on trailing barbed ends of fascin-bundled filaments is an evolutiona

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

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

243 atory factors IRTKS and EPS8 localize to the barbed ends of motile microvilli, where they control the

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

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

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

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

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

249 e formation of a ternary complex at filament barbed ends, or by nucleation and interaction at filamen

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

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

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

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

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

255 Barbed ends, protected by Cappuccino, grow away from the

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

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

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

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

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

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

262 les direct delivery of profilin-actin to the barbed end, speeding the rate of filament elongation.

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

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

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

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

267 ce explains why filaments grow faster at the barbed end than the pointed end.

268 ts elongate and shorten much faster at their barbed end than their pointed end, but the molecular bas

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

270 At the barbed end the terminal subunit is loosely tethered by i

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 By regulating the availability of the barbed end, we propose that profilin binding establishes

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

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

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