ライフサイエンスコーパス: actin monomer

1 metry at saturation of 1:4 (mol AtFim1 : mol actin monomer).

2 lex by two VCA molecules, each delivering an actin monomer.

3 nity for free CA than VCA cross-linked to an actin monomer.

4 logy 2 (WH2) domains, each of which binds an actin monomer.

5 , and significant shifts in the twist of the actin monomer.

6 mpete with one another for a limited pool of actin monomers.

7 C-B dimerization and recruitment of multiple actin monomers.

8 ze sequential steps in recycling cofilin and actin monomers.

9 cofilin, which severs F-actin and sequesters actin monomers.

10 promote nucleotide exchange (ATP for ADP) on actin monomers.

11 to thin filaments resulting in rotations of actin monomers.

12 of thymosin beta4 (Tbeta4) binding to MgATP-actin monomers.

13 largest fraction of polymerization-competent actin monomers.

14 nce resonance energy transfer (FRET) between actin monomers.

15 tracts, and binds to and sequesters purified actin monomers.

16 ered bundles with one bound fascin per 25-60 actin monomers.

17 , and the capacity to bind and sequester two actin monomers.

18 the nucleotide-bound state of the component actin monomers.

19 filament end, inhibiting addition or loss of actin monomers.

20 data is that caldesmon binds tightly to 2-3 actin monomers.

21 , causing caldesmon to cover approximately 7 actin monomers.

22 was no change in the concentration of ADP-G-actin monomers.

23 RF to sense changes in the cellular level of actin monomers.

24 in A prevents actin assembly by sequestering actin monomers.

25 to nucleus depends on its dissociation from actin monomers.

26 nus at a stoichiometry of one MLCK per three actin monomers.

27 ion and structural dynamics ("breathing") of actin monomers.

28 which is greater for CaATP-actin than MgATP-actin monomers.

29 nediamine (AEDANS) conjugated to Cys(374) of actin monomers.

30 a length to span only four instead of seven actin monomers.

31 proteins, actin filaments and NPF-recruited actin monomers.

32 tion and are sequestered in the cytoplasm by actin monomers.

33 lymerization assays containing only INF2 and actin monomers.

34 control the pool of polymerization-competent actin monomers.

35 efficiently promotes nucleotide exchange on actin monomers.

36 ilaments, Spire can sever them and sequester actin monomers.

37 regulatory units (SUs) of thin filaments (7 actin monomers : 1 tropomyosin : 1 troponin complex) on

38 ulatory units (RU-RU cooperativity; 1 RU = 7 actin monomers+1 troponin complex+1 tropomyosin molecule

39 nt elongation by maintaining a large pool of actin monomers above the critical concentration for poly

40 n organization or dynamics [5-8] or in vitro actin-monomer affinity [9] has been perplexing, given th

41 cle is nucleotide exchange of ADP for ATP on actin monomers after release from the INF2/actin complex

42 icient for catalyzing nucleotide exchange on actin monomers, although the adjacent WH2 domain is not

43 This second interacting region sequesters actin monomers, an activity that is dependent on a WASP

44 n states are compared with those of Mg-ATP-G-actin (monomers) analyzed previously.

45 They bring together an actin monomer and Arp2/3 complex in solution or on the s

46 lts suggest greater flexibility of the yeast actin monomer and filament compared with muscle actin.

47 ty, including decreasing gelsolin binding to actin monomer and increasing gelsolin binding to phospha

48 e control of the structural integrity of the actin monomer and the actin filament and provide insight

49 ion between the conformational changes of an actin monomer and the structural and mechanical properti

50 arrays with a mole ratio of one dimer to 1.3 actin monomers and a 3.1 microm K(d).

51 bits actin filament assembly by sequestering actin monomers and capping filament barbed ends.

52 Striated muscle tropomyosin spans seven actin monomers and contains seven quasi-repeating region

53 Tropomyosin (Tm) spans seven actin monomers and contains seven quasi-repeating, loose

54 volved in filopodia formation, binds to both actin monomers and cortactin.

55 actin turnover by releasing cofilin from ADP-actin monomers and enhances the ability of profilin to s

56 are complex; they depend on interactions of actin monomers and filaments with numerous other protein

57 tail has low-affinity interactions with both actin monomers and filaments.

58 molar to millimolar) have been identified on actin monomers and filaments.

59 the unique ability of Tbeta(4) to sequester actin monomers and inhibit nucleotide exchange.

60 application of latrunculin B, which binds to actin monomers and inhibits actin polymerization, also b

61 raction of actophorin with Mg-ADP- or Mg-ATP-actin monomers and Mg-ADP-actin filaments, so Ser1 phosp

62 tion reduces the nucleotide-exchange rate on actin monomers and modestly accelerates the assembly of

63 disrupted attachment of myosin molecules to actin monomers and muscle fibre atrophy.

64 imilar to its vertebrate homologue, bound to actin monomers and nucleated and bundled filaments.

65 presence of ADF/cofilin, AtCAP1 can recharge actin monomers and presumably provide a polymerizable po

66 und ADP-actin monomers to profilin bound ATP-actin monomers and recycling cofilin for new rounds of f

67 ed muscle thin filaments contain hundreds of actin monomers and scores of troponins and tropomyosins.

68 f catalyzes dissociation of cofilin from ADP-actin monomers and stimulates nucleotide exchange.

69 As an application example, actin monomers and structural subdomains are located in

70 rate that MsrB2 selectively reduces oxidized actin monomers and thereby counteracts MICAL1, an enzyme

71 hine; and (3) formins nucleate by recruiting actin monomers and therefore are more similar to other n

72 bilities of Srv2 to recycle cofilin from ADP-actin monomers and to promote nucleotide exchange (ATP f

73 winholide depolymerize actin by sequestering actin monomers and, in addition, swinholide can sever ex

74 Bud6 and found that it binds specifically to actin monomers and, like profilin, promotes rapid nucleo

75 c beta- and gammacyto-actin (but not alphask-actin) monomers and prevent polymerization under physiol

76 ng constant, chain persistence length nu (in actin monomers), and chain kink energy A from a single b

77 l in which one activated Arp2/3 complex, one actin monomer, and an actin filament combine into a prea

78 /3 complex, nucleation-promoting factors, an actin monomer, and the mother filament.

79 ment elongation rate by blocking addition of actin monomers, and increases the dissociation rate of a

80 A, which disrupts actin filaments by binding actin monomers, and wortmannin, an inhibitor of phosphat

81 Actin monomers antagonize side binding but promote high

82 FH1 is necessary for nucleation when actin monomers are profilin bound.

83 All other nucleators are known to recruit actin monomers as a central part of their mechanisms.

84 protein with a role in binding and recycling actin monomers ascribed to domains in its C-terminus (C-

85 Actin monomers assemble into semiflexible polymers that

86 In actin monomer assembly reactions, VopL/F exclusively nuc

87 ly, we observed lateral interactions between actin monomers associated with Spir-ABCD, suggesting tha

88 mal motions are rectified by the addition of actin monomers at the end of growing filaments.

89 During assembly from Mg-ATP-actin monomers, AtCP eliminates the initial lag period f

90 sembled to recycle and replenish the pool of actin monomers available for polymerization.

91 Profilin's differential affinities for actin monomers, barbed ends and polyproline are thus tun

92 communication through subdomain 1 within the actin monomer between the N and C termini.

93 w that profilin controls the partitioning of actin monomers between competing actin networks assemble

94 embrane is generated by the intercalation of actin monomers between the membrane and actin filament e

95 ent depolymerization (cofilin and Aip1), and actin monomer binding (profilin and cyclase-associated p

96 embly by a hybrid mechanism involving tandem actin monomer binding and Arp2/3 complex activation.

97 face and that nucleating activity depends on actin monomer binding and pointed end-capping activities

98 structure of the C-terminal dimerization and actin monomer binding domain (C-CAP) reveals a highly un

99 sociated protein (CAP or Srv2p) is a modular actin monomer binding protein that directly regulates fi

100 Profilin is an actin monomer binding protein that, depending on the con

101 as a proline-rich FH1 domain that binds the actin monomer binding protein, profilin, and other ligan

102 interfaces on actin, one distinct from other actin monomer binding proteins, and two potential bindin

103 In this work, we show that actin monomer binding to the DAD of INF2 competes with t

104 effects of nucleotide and divalent metal on actin monomer binding, in pH-dependent severing, in enha

105 N-terminal domain of Tmod3 is essential for actin monomer binding.

106 end-capping and nucleation without altering actin monomer binding.

107 Arp2/3 complex, and a subset was tested for actin monomer binding.

108 The evolutionarily conserved small actin-monomer binding protein profilin is believed to be

109 ond alpha-helix of Tmod3, decreases both its actin monomer-binding and -nucleating activities.

110 osin beta4 (Tbeta4/Tmsb4x), which encodes an actin monomer-binding protein implicated in cell migrati

111 Interaction of the actin monomer-binding protein profilin with the FH1 doma

112 eletion of sites required for binding of the actin monomer-binding protein profilin, a known ligand o

113 hosphoinositide PI(3,4,5)P3 and involves the actin monomer-binding protein profilin.

114 Profilin is an abundant actin monomer-binding protein with critical actin regula

115 The actin monomer-binding protein, profilin, influences the

116 psis thaliana) PROFILIN1 (PRF1), a conserved actin monomer-binding protein, to actin organization and

117 his study, we show that NAC1 functions as an actin monomer-binding protein.

118 Finally, we identify the actin monomer-binding proteins profilin and thymosin bet

119 In vitro, the actin monomer-binding region of ActA is critical for sti

120 WASP family proteins: an acidic stretch, an actin monomer-binding region, and a cofilin homology seq

121 onclude that efficient severing utilizes two actin monomer-binding sites, and that the length of the

122 Elimination of an actin monomer-binding WASP homology 2 domain and a profi

123 P) recruitment by ActA can bypass defects in actin monomer-binding.

124 A new study reports that the actin-monomer-binding protein profilin 1 dictates protru

125 ciation, the FH1 domains-in concert with the actin-monomer-binding protein profilin-increase the rate

126 ex suggests that during activation the first actin monomer binds at the barbed end of Arp2.

127 The actin monomer bound at the GAB domain is proposed to be

128 ge of ADP for ATP, refilling the pool of ATP-actin monomers bound to profilin, ready for elongation.

129 the ability to initiate actin filaments from actin monomers bound to profilin.

130 Actin monomers bound to the WH2 domains block binding of

131 y does phalloidin promote nucleation of pure actin monomers but it also dramatically stimulates branc

132 and C-terminal regions of Sca2 interact with actin monomers but only weakly, whereas the full-length

133 found that yeast and mammalian formins bind actin monomers but that this activity requires their C-t

134 icrom), profilin accelerated the off-rate of actin monomers by a factor of four to six.

135 hing experiments, the rapid sequestration of actin monomers by uncaged Tbeta4 and the consequent redu

136 represent a potential conformation that the actin monomer can adopt on the pathway to polymerization

137 These results suggest that free actin monomers can serve as INF2 activators by competing

138 Actin monomers change orientation because myosin cross-b

139 ltage, which causes local enhancement of the actin monomer concentration and mixing with Mg(2+).

140 ip1 is important for establishment of normal actin monomer concentration in cells and efficiently con

141 ly stages of actin polymerization (where the actin monomer concentration is high) cross-linked antipa

142 orders of magnitude higher than the in vitro actin monomer concentration required to support the obse

143 Similarly, the predicted effect of actin monomer concentration was experimentally verified

144 ll with experimental results over a range of actin monomer concentrations.

145 However, the number of actin monomers constituting a site was variable.

146 Binding of profilin to actin monomers creates profilin-actin complexes, which t

147 energy transfer to acceptors on neighboring actin monomers (cross-transfer).

148 ly different surfaces on the exterior of the actin monomer, current models of the actin filament lack

149 laments, one molecule spanning four to seven actin monomers, depending on the isoform.

150 modelling, here the authors show that local actin monomer depletion and network architecture can tun

151 by ongoing actin-filament assembly uses free actin monomer derived from filament disassembly, in pref

152 provides a full stochastic treatment of the actin monomer diffusion and polymerization of each indiv

153 els were incorporated, including discretized actin monomer diffusion, Monte-Carlo filament kinetics,

154 nces positioned N-terminal to WH2 could feed actin monomers directly to WH2, thereby playing a role i

155 , we engineered a chimeric formin that binds actin monomers directly via covalent attachment of profi

156 Whereas many of these proteins bind actin monomers directly, formins use the actin-binding p

157 Such a cross-linked globular actin monomer does not form filaments, suggesting nuclea

158 a model for the diffusion and consumption of actin monomers during actin-based particle propulsion to

159 ed from the rate of change of orientation of actin monomers during muscle contraction.

160 cell contains two nearly identical copies of actin monomers, each bound to Lmod2's ABS2 and WH2 domai

161 canals also dramatically reduced the rate of actin monomer exchange.

162 he combination of all three factors produces actin monomers faster than any two factors alone.

163 r a reaction mechanism in which Tbeta4 binds actin monomers following a two-step mechanism in which t

164 nformational change and recruiting the first actin monomer for the daughter branch.

165 n, and WASP-homology 2 (WH2) domains recruit actin monomers for nucleation.

166 the extreme periphery of subdomain-1 of each actin monomer forming a bridge to the periphery of subdo

167 d, excess cytosolic actin assembly prevented actin monomer from rapid translocation to and efficient

168 n actin monomers from ADP to ATP and recycle actin monomers from actin-depolymerizing factor (ADF)/co

169 teins, which catalyze nucleotide exchange on actin monomers from ADP to ATP and recycle actin monomer

170 lament ends, and (ii) promoting shuttling of actin monomers from profilin-actin complexes onto nearby

171 mers, and increases the dissociation rate of actin monomers from the filament end.

172 lation of thymosin-beta4 (Tbeta4) binding to actin monomer (G-actin) coordinates actin polymerization

173 e explore the conformational mobility of the actin monomer (G-actin) in a coarse-grained subspace usi

174 Each actin monomer (G-actin) is coarse-grained into four site

175 Addition of actin monomer (G-actin) to growing actin filaments (F-ac

176 Oxidation of actin monomer (G-actin) with copper o-phenanthroline res

177 eparately, competition for a limited pool of actin monomers (G-actin) helps to regulate their size an

178 we report that spatiotemporal enrichment of actin monomers (G-actin) in dendritic spines regulates s

179 are in homeostasis, whereby competition for actin monomers (G-actin) is critical for regulating F-ac

180 Affinity columns using actin monomers (globular actin, G-actin) or actin filame

181 , we find that both nucleotide states of the actin monomer have significantly less twist than their c

182 ies consistent with each motif binding to an actin monomer in the filaments.

183 annexin 2 reduces the polymerisation rate of actin monomers in a dose-dependent manner.

184 Sp homology 2 (WH2)-like sequence that binds actin monomers in a manner that is competitive with othe

185 The VCD organizes three actin monomers in a spatial arrangement close to that fo

186 hown to bundle actin filaments and sequester actin monomers in an activity-dependent manner.

187 ity by (i) bringing polymerization-competent actin monomers in proximity to growing filament ends, an

188 nits tend toward conformations that resemble actin monomers in solution, while contacts with neighbor

189 ible force-induced chemical state changes of actin monomers in the filament.

190 the thick filaments and the alignment of the actin monomers in the thin filaments are improved as a r

191 hey are assumed to assemble exclusively from actin monomers in vivo.

192 r beta- and gammacyto-actin (but not alphask-actin) monomers in the absence of TMs suggests a novel f

193 rtually abolished cytochalasin D-inhibitable actin monomer incorporation at the fast-growing barbed e

194 lamellipodium of motile cells that indicate actin monomer incorporation into the actin filament netw

195 Employing GFP-tagged actin monomer incorporation, we identify several distinc

196 he fluorescence, and how profilin binding to actin monomers increases the fluorescence.

197 As little as 1 FLNa to 800 polymerizing actin monomers induces a sharp concentration-dependent i

198 Binding of AtCAP1 to ATP-actin monomers inhibits polymerization, consistent with

199 Complexes consisting of APC, mDia1, and actin monomers initiated actin filament formation, overc

200 en initiates nucleus assembly by bringing an actin monomer into proximity of the primed complex.

201 This fragment recruits actin monomers into a polymerization nucleus.

202 depolymerization by covalently cross-linking actin monomers into dimers, trimers, and higher multimer

203 The assembly of actin monomers into filaments and networks plays vital r

204 eta-actin demonstrates that incorporation of actin monomers into filaments is required for localizati

205 The rate of incorporation of actin monomers into filaments was fastest at the wound m

206 lability, and profilin-1 directs unallocated actin monomers into microvillar core bundles during ente

207 ation of actin dynamics: SALS-WH2 sequesters actin monomers into non-polymerizable complexes and enha

208 tin cytoskeleton by covalently cross-linking actin monomers into oligomers.

209 e structure shows that the structure with an actin monomer is a good model for an actin filament cap.

210 around 40 amino acids corresponding to the 7 actin monomers it interacts with.

211 oncentrations of profilin (10-100 microm) on actin monomer kinetics at the barbed end.

212 tudy shows that assembly factors compete for actin monomers, leading to homeostasis between different

213 They show that actin monomer levels are elevated in spines upon activit

214 ine whether enterocytes were resource (i.e., actin monomer) limited in assembling this domain.

215 y the TPM, resulting in the strengthening of actin monomer-monomer contacts along the filament axis.

216 rowding increases the local concentration of actin monomers near the filament ends and hence accelera

217 These mutant cofilins bound actin monomers normally, but bound and severed ADP-actin

218 transmission of the conformational change to actin monomers not in direct contact with troponin I.

219 actin, and forms a bridge to the neighboring actin monomer of the adjacent long pitch helical strand

220 formational changes and delivering the first actin monomer of the daughter filament.

221 are consistent with heads bound on adjacent actin monomers of a filament, under strain, similar to p

222 The ability of troponin to switch actin monomers "on" and "off" at high and low Ca(2+), re

223 binding protein profilin to dynamically load actin monomers onto their flexible Formin Homology 1 (FH

224 ( approximately 10 x 10(6) M(-1) s(-1)) for actin monomer or Profilin.Actin.

225 rp2/3 complex activators, Dip1 does not bind actin monomers or filaments, and it interacts with the c

226 together, our data indicate that Tmod3 binds actin monomers over an extended interface and that nucle

227 .69 s(-1)) polymerases that deliver multiple actin monomers per barbed end-binding event and effectiv

228 aching saturation at a stoichiometry of 12:1 actin monomers per betaCaMKII holoenzyme with a binding

229 mM ionic strength was best described with 7 actin monomers per site.

230 In many tissues, actin monomers polymerize into actin (thin) filaments of

231 chiometrically and maintains the bulk of the actin monomer pool in metazoan cells.

232 filamentous actin (F-actin) networks from an actin monomer pool is important for a variety of cellula

233 PA, allowing rapid filament assembly from an actin monomer pool that is buffered with profilin.

234 rved even at low stoichiometries of WAVE1 to actin monomers, precluding an effect from monomer seques

235 tructure and functions as an intermediate in actin monomer processing, converting cofilin bound ADP-a

236 controlled minimal protein system containing actin monomers, profilin, the Arp2/3 complex and capping

237 ts its actin nucleation function by blocking actin monomer recruitment.

238 splakinolide is amplified in the presence of actin-monomer sequestering proteins such as thymosin bet

239 Treatment of terminals with the actin monomer-sequestering agent latrunculin-A completel

240 tin depolymerizing factor (TgADF) has strong actin monomer-sequestering and weak filament-severing ac

241 effect is counteracted by treatment with the actin monomer-sequestering drug latrunculin B.

242 gcs1Delta was hypersensitive to the actin monomer-sequestering drug, latrunculin-B.

243 on dynamics in response to latrunculin A, an actin monomer-sequestering drug.

244 imilarity with the N-terminal portion of the actin monomer-sequestering thymosin beta domain (Tbeta).

245 ly to proteins that control the processes of actin monomer sequestration, filament severing, capping,

246 11 nm; tail step, 32 +/- 10 nm), likely one actin monomer short of its preferred binding site.

247 rs actin dimers) and Lat B (which sequesters actin monomers) similarly increase outflow facility.

248 Thymosin-beta(4) (Tbeta(4)) binds actin monomers stoichiometrically and maintains the bulk

249 t rates, which depend on the availability of actin monomers, suggest an active transport mechanism in

250 e attenuated by increasing concentrations of actin monomers, suggesting competition between actin and

251 e experiments with varying concentrations of actin monomers, taking advantage of the fact that the nu

252 n polymer is due to collisional complexes of actin monomers that are in equilibrium with the polymer

253 d on different assumptions for the number of actin monomers that constitute a caldesmon binding site.

254 three mutations affected the folding of the actin monomer, the velocity at which skeletal myosin mov

255 . pombe profilin have similar affinities for actin monomers, the FH1 domain of fission yeast formin C

256 At high concentrations of free actin monomers, the mean size of the unhydrolyzed ATP-ca

257 In addition, INF2 binds actin monomers through its diaphanous autoregulatory dom

258 ucleotide and facilitates the addition of an actin monomer to a growing filament.

259 a bound nucleation-promoting factor, and an actin monomer to an actin filament, has a rate constant

260 -linked actin dimer or trimer reacts with an actin monomer to produce a competent nucleus for filamen

261 Arp2 does not prevent VCA from recruiting an actin monomer to the complex.

262 Thus, recruitment of actin monomers to a cortactin-activated Arp2/3 complex l

263 ctin is a weak NPF because it cannot recruit actin monomers to Arp2/3 complex.

264 "mother" actin filaments, while WASP donates actin monomers to Arp2/3-generated "daughter" filament b

265 myosin binding sites on several neighboring actin monomers to become open for myosin binding.

266 6 promotes filament nucleation by recruiting actin monomers to Bni1.

267 2 repeats within Spire bind four consecutive actin monomers to form a novel single strand nucleus for

268 em W domains that tie together three to four actin monomers to form a polymerization nucleus.

269 ends and processively stepping onto incoming actin monomers to incorporate them into the filament.

270 ated at an approximate stoichiometry of nine actin monomers to one mXinalpha.

271 n to previously proposed local conversion of actin monomers to polymers, we demonstrate a surprising

272 mer processing, converting cofilin bound ADP-actin monomers to profilin bound ATP-actin monomers and

273 d6 and profilin generate a local flux of ATP-actin monomers to promote actin assembly.

274 hrough a phosphorylation cycle that shuttles actin monomers to regions of new actin filament assembly

275 ught to act by liberating cofilin from ADP.G-actin monomers to restore cofilin activity.

276 lium undergoes elongation due to addition of actin monomers to the barbed ends of the filaments.

277 WASP recruits actin monomers to the complex and stimulates movement of

278 This has been attributed to funneling of actin monomers to the filament ends that remain uncapped

279 hymosin beta4 as key molecules that localize actin monomers to the leading edge of lamellipodia for t

280 opodial length is diffusional transport of G-actin monomers to the polymerizing barbed ends.

281 distributions are coupled to the delivery of actin monomers toward the tip, even the concentration bu

282 n of sparsely incorporated rhodamine-labeled actin monomers, using polarized total internal reflectio

283 affinity in a Ca(2+)-resistant manner, bound actin monomer via a WASP (Wiskott-Aldrich syndrome prote

284 dence that catalyzing nucleotide exchange on actin monomers via the beta-sheet domain is the most hig

285 he vitamin D-binding protein (DBP) traps the actin monomers, which accelerates their clearance.

286 observed significant diffusional noise of G-actin monomers, which leads to smaller G-actin flux alon

287 cient to catalyze nucleotide-exchange of ADP-actin monomers, while in the presence of cofilin this ac

288 icromolar affinity but has weak affinity for actin monomers, while INF2-DAD binds CAP/K50Q-actin 5-fo

289 ctin produces a conformational change in the actin monomer with the result that interaction at differ

290 ctomyosin VI show the two heads bound to the actin monomers with a broad distribution of distances, i

291 usly characterized tropomodulins, sequesters actin monomers with an affinity similar to its affinity

292 lin-binding sites, and it interacts with ATP-actin monomers with high affinity through its WH2 domain

293 Wsp1-VCA binds both Arp2/3 complex and actin monomers with high affinity.

294 y, whereas the full-length protein binds two actin monomers with high affinity.

295 rties at low and high concentrations of free actin monomers with some deviations near the critical co

296 milarity to WASP homology 2 domains bind two actin monomers with submicromolar affinity.

297 of the monomer pool, and the association of actin monomers with thymosin and profilin in the kidney

298 G-actin can be ascribed to the existence of actin monomers with very little, if any, dimer.

299 nts accompanied by structural transitions of actin monomers within cTFs.

300 resolution achieved is sufficient to resolve actin monomers within the filaments.