ライフサイエンスコーパス: myosin V

1 r characterized myosins (e.g., myosin-II and myosin-V).

2 grain structure of the dimeric, linear motor myosin V.

3 is essential for processive myosins, such as myosin V.

4 ein independently of its putative linkage to myosin V.

5 n intensity when bound to the active site of myosin V.

6 consistent with a 37-nm forward step size of myosin V.

7 ead promotes highly selective and processive myosin V.

8 IQ4, allowed building a model of the LCBD of myosin V.

9 he transport of multiple distinct cargoes by myosin V.

10 n, regulation, and molecular interactions of myosin V.

11 We also used SHREC to study the motion of myosin V.

12 he leading lever arm in the waiting state of myosin V.

13 increase the degree of processive motion of myosin V.

14 processive motor from the myosin superfamily myosin V.

15 hat this loop plays in the kinetic tuning of myosin V.

16 ceptor for Myo2p, a Saccharomyces cerevisiae myosin V.

17 opposite direction to that seen with intact myosin V.

18 DdMII), and nonmuscle myosin IIA, as well as myosin V.

19 tch II with the gamma phosphate of ATP, into myosin V.

20 ormational changes at the nucleotide site of myosin V.

21 and contrast the motility of myosin-VI with myosin-V.

22 and cytoplasmic dynein, and an actin motor, myosin-V.

23 sity but was not affected by the presence of myosin-V.

24 Myosin V, a double-headed molecular motor, transports or

25 o the ring by a combination of myosin II and myosin V activities.

26 icted Cdk1 sites in other organelle-specific myosin V adaptors suggests that the inheritance of other

27 Time courses of myosin V-ADP binding and release are biphasic, consisten

28 Myosin V and myosin V-ADP binding to actin was assayed from the quenc

29 Phosphate dissociation from myosin V-ADP-Pi (inorganic phosphate) and actomyosin V-A

30 rate of the hydrolysis step (myosin V-ATP-->myosin V-ADP-Pi) were all approximately 10-fold slower i

31 By contrast, while the velocity of myosin V also saturates under assisting loads, the motor

32 itching can be tuned via combinations of 1-4 myosin V and 1-4 dynein-dynactin engaged motors through

33 nalyzing the properties of chimeras of mouse myosin V and a non-processive class V myosin from yeast

34 Time courses of MgmantADP dissociation from myosin V and actomyosin V are biphasic with fast observe

35 The [Mg(2+)] dependence of ADP binding to myosin V and actomyosin V was measured from the fluoresc

36 m regulates the kinetics of ADP release from myosin V and actomyosin V.

37 ch transcribes varying DNA sequences, and to myosin V and cytoplasmic dynein, which may advance by va

38 ersections in a minimal system with purified myosin V and dynein-dynactin motors bound to beads.

39 otor forces scale with the number of engaged myosin V and dynein-dynactin motors.

40 Here we use a coarse-grained model of myosin V and generate a structure-based free energy surf

41 ar to or slightly faster in S217A than in WT myosin V and mechanochemical gating of the rates of diss

42 Myosin V and myosin V-ADP binding to actin was assayed f

43 ell short of the 36-nm step-size observed in myosin V and myosin VI that corresponds to the actin pse

44 developing photoreceptors and asked here if myosin V and the Drosophila Rab11 interacting protein, d

45 ectly observe Smy1-3GFP being transported by myosin V and transiently pausing at the neck in a manner

46 8-A cryoEM reconstruction of this state for myosin V and used molecular dynamics flexed fitting for

47 Myosin V and VI are antagonistic motors that cohabit mem

48 ectory, shapes for scaffolds containing both myosin V and VI are dominated by the myosin with a stiff

49 Single myosin V and VI dimers display similar skewed trajectori

50 an be finely-tuned by the relative number of myosin V and VI motors on each scaffold.

51 ifferences in observed behavior of groups of myosin V and VI motors.

52 These data indicate that myosin V and VI play related but distinct roles in regul

53 two-dimensional actin-myosin interface using myosin V and VI precisely patterned on DNA nanostructure

54 Contrary to the high duty ratio motors myosin V and VI, the ADP release rate constant from acto

55 of the single-molecule vesicle transporters myosin V and VI.

56 long stress fiber bundles, while motility of myosin V and X are suppressed.

57 myosin and formin) and membrane trafficking (myosin-V and exocyst) were dynamic during cytokinesis.

58 lated protein can function intimately with a myosin-V and its receptor in the transport of a specific

59 ral studies show several differences between myosin-V and VI, including a significant difference in t

60 nts of phosphate (fast) and ADP (slow) as in myosins V and VI.

61 approximately 8-10 times slower than that of myosin V, and its step size is 30 nm, which is consisten

62 transition, and the processive run length of myosin V, and thus, it is important to understand how ca

63 al dwell-time distributions of single-headed myosin V, and were able to use a single kinetic scheme t

64 Using both dimeric myosin V- and myosin VI-labelled nanotubes, we find that

65 The IQs of myosin V are distributed into three pairs.

66 When kinesin and myosin V are present on the same cargo, kinesin interact

67 have shown how the structure and kinetics of myosin V are specialized to produce a highly processive

68 The detailed dynamics of the cycle of myosin-V are explored by simulation approaches, examinin

69 cule experiments indicate that myosin-VI and myosin-V are processive molecular motors, but travel tow

70 lmodulins of the light-chain domain (LCD) of myosin V as myosin V moves along actin.

71 -ADP-Pi and the rate of the hydrolysis step (myosin V-ATP-->myosin V-ADP-Pi) were all approximately 1

72 re dependence of the maximum actin-activated myosin V ATPase rate is similar to the pocket opening st

73 chimera containing yeast loop 2 in the mouse myosin V backbone.

74 ze the central position of the CR and resist myosin V-based forces to promote the fidelity of cell di

75 acts electrostatically with actin to enhance myosin V-based transport in vitro [2].

76 ion is not as robust as that of kinesin-1 or myosin-V because dynein moves only a limited distance (a

77 alog increases when the MV.SLADP complex (MV=myosin V) binds to actin, implying an opening of the act

78 We found that whole myosin II and myosin V both twirl actin with a relatively long (approx

79 n XI shares a similar structure with that of myosin V, but has evolved plant-specific cargo binding m

80 vates the ATPase activity of tissue-purified myosin V, but not that of shorter expressed constructs.

81 We generated two mutants of myosin V by altering loop 2, a surface loop in the actin

82 e studied the structural dynamics of chicken myosin V by combining the localization power of fluoresc

83 ch actin accelerates the release of ADP from myosin V by reducing the magnesium affinity of a myosin

84 the dynamics of the actin binding region of myosin V by using fluorescence resonance energy transfer

85 onal perturbation of the switch 1 structure, myosin V can be converted into a low duty ratio motor th

86 The kinetics of detachment indicate that myosin V can detach from actin at two distinct points in

87 provide a mechanism whereby a single type of myosin V can move diverse cargoes to distinct destinatio

88 The enzymatic and mechanical functions of myosin V can, therefore, be modulated both by calcium-de

89 The myosin V carboxyl-terminal globular tail domain is essen

90 The hrs/actinin-4/BERP/myosin V (CART [cytoskeleton-associated recycling or tra

91 The LCBD of myosin V consists of six tandem IQ motifs, which constit

92 tion and that loss of regulation renders the myosin V constitutively active.

93 The kinetics of monomeric myosin V containing a single IQ domain (MV 1IQ) differ f

94 he upper 50-kDa domain (residues 292-297) of myosin V containing a single IQ domain (MV 1IQ), allowin

95 the result of the energetics of the complete myosin-V cycle and is not the source of directional moti

96 with simulations and is applied to in vitro myosin V data where a small 10 nm population of steps is

97 ults should be generally applicable to other myosin-V delivery cycles.

98 Direct measurements of phosphate release in myosin V demonstrate that Mg(2+) reduces actin affinity

99 Our comparison between vertebrate and fly myosin V demonstrates that the well preserved function o

100 ay from the cell middle during anaphase in a myosin V-dependent manner.

101 a critical step in the spatial regulation of myosin V-dependent organelle transport and may reveal co

102 I-dependent), contractile vacuole activity (myosin V-dependent), and phagocytosis (myosin VII-depend

103 An additional effect of myosin V depletion was an increase in mitochondrial leng

104 t increase in mitochondrial transport during myosin V depletion.

105 tes the processive run length of full-length myosin V (dFull) and a truncated dimeric construct (dHMM

106 epancy by comparing an expressed full-length myosin V (dFull) to three shorter constructs.

107 nd its regulation, as well as revealing that myosin V diffuses on microtubules.

108 cular interactions including the motion of a myosin-V dimer "walking" on an actin fibre, RNA stem-loo

109 gation complex") and one with kinesin II and myosin V ("dispersion complex"), and that the removal of

110 Unlike myosin V, either subdomain of myosin XI alone was target

111 The tail of the yeast myosin V encoded by Myo2p is known to bind several recep

112 There are three distinct members of the myosin V family in vertebrates, and each isoform is invo

113 een unknown as to whether all members of the myosin V family share a common, evolutionarily conserved

114 The myosin-V family of molecular motors is known to be under

115 We find that myosin V follows a narrower path on both structures, wal

116 significantly decreased both the affinity of myosin V for actin and the processive run length.

117 ed to correspondingly change the affinity of myosin V for actin in the weak binding state, without ch

118 long microtubules and then shifts control to myosin V for delivery on actin filaments to the cell mem

119 Here we show that myosin V from Drosophila has a strikingly different moto

120 p) bound to the IQ2-IQ3 fragment of Myo2p, a myosin V from Saccharomyces cerevisiae.

121 at this is a general mechanism that detaches myosin V from select cargoes.

122 used these studies to develop a model of how myosin V functions as a transport motor.

123 To assess the function of the single myosin V gene in Drosophila (MyoV), we have characterize

124 The myosin V globular tail domain (MyoV-GTD) interacts direc

125 report the crystal structure at 2.2 A of the myosin V globular tail.

126 ta6IQ), or deletion of MYO4 (the other yeast myosin V), had no effect on mitochondrial morphology, co

127 Thus, myosin V harnesses its fluctuating environment to extend

128 The processive motor myosin V has a high affinity for actin in the weak bindi

129 The processive motor myosin V has a relatively high affinity for actin in the

130 e seen with myosin II, despite the fact that myosin V has dramatically altered kinetics.

131 The highly processive motor, myosin V, has an extremely long neck containing six calm

132 A recombinant myosin V heavy meromyosin fragment that is missing the d

133 In the laser trap, applied load slows myosin V heavy meromyosin stepping and increases the pro

134 cultured Xenopus melanophores is mediated by myosin V, heterotrimeric kinesin-2, and cytoplasmic dyne

135 te of product release from the double-headed myosin V-HMM using a new ATP analogue, 3'-(7-diethylamin

136 tion strategy halting growth by immobilizing myosin V in a newly described state on selectively stabi

137 organelle movements in plants, analogous to myosin V in animals and fungi.

138 reconstructions provide the atomic models of myosin V in both weak and strong actin bound states.

139 two IQ complex to provide an atomic model of myosin V in the presence of calcium.

140 Thus, spatial and temporal regulation of myosin V in vivo by a head-to-tail interaction is critic

141 cargo, defining a new rigor-like state of a myosin V in vivo.

142 strong support for a straight-neck model of myosin V in which the lever arm of the leading head is t

143 Here we define the in vivo delivery cycle of myosin-V in its essential function of secretory vesicle

144 our knowledge of the roles and regulation of myosin-Vs in cytokinesis is limited.

145 For myosin V, internal strain produced when both heads of ar

146 These myosin V IQ mutants were fluorescently labeled by exchan

147 Myosin V is a cellular motor protein, which transports c

148 Myosin V is a double-headed molecular motor involved in

149 Myosin V is a homodimeric motor protein involved in traf

150 Myosin V is a molecular motor that transports a variety

151 Myosin V is a processive actin-based motor protein that

152 Myosin V is a single-molecule motor that moves organelle

153 These data demonstrate that the step-size of myosin V is affected by the length of its neck and is no

154 Myosin V is an actin-based motor protein involved in int

155 Myosin V is an efficient processive molecular motor.

156 Myosin V is biomolecular motor with two actin-binding do

157 The long neck of unconventional myosin V is composed of six tandem "IQ motifs," which ar

158 of chemical energy to directional motion in myosin V is examined by careful simulations that include

159 Processivity in myosin V is mediated through the mechanical strain that

160 Myosin V is molecular motor that is capable of moving pr

161 The interdomain coupling in myosin V is studied with restrained targeted molecular d

162 Myosin V is the best characterized vesicle transporter i

163 We show that myosin-V is activated by binding a secretory vesicle and

164 Myosin-V is an actin-associated processive molecular mot

165 vestigated and a detailed sensitivity map of myosin-V is thus obtained.

166 little is known about the function of other myosin V isoforms (Vb and Vc) at a molecular level.

167 cts a higher ADP affinity than seen in other myosin V isoforms.

168 ing pathways through recruitment of multiple myosin V isoforms.

169 -binding states, unlike the other vertebrate myosin V isoforms.

170 ansporter by different mechanisms from other myosin V isoforms.

171 ite different from those of other vertebrate myosin V isoforms.

172 -I isoforms (Myo3p and Myo5p) and one of two myosin-V isoforms (Myo4p).

173 tionality of the motor core, we attached the myosin V lever arm to myosin VI, with and without the un

174 myosin VI lever arm for the relatively rigid myosin V lever increases trajectory skewness, and vice v

175 A myosin V may move multiple cargoes to distinct places at

176 in V by reducing the magnesium affinity of a myosin V-MgADP intermediate.

177 The two myosin V-MgADP states are of comparable energies, as ind

178 Two myosin V-MgADP states that are in reversible equilibrium

179 The double-headed myosin V molecular motor carries intracellular cargo pro

180 Myosin V molecular motors move cargoes on actin filament

181 use myosin Va) and nonprocessive (Drosophila myosin V) molecular motors.

182 ws, our results show that the two heads of a myosin V molecule communicate, not through any one mecha

183 d constructs reveal that a single Drosophila myosin V molecule spends most of its mechanochemical cyc

184 s approach, the individual heads of a single myosin V molecule were observed taking 72-nm steps as th

185 forward or backward force on a single-headed myosin V molecule, hypothesized to simulate forces exper

186 Processive myosin V molecules sometimes shifted from the top to the

187 y to study the structural dynamics of single myosin V molecules that had been labeled with bifunction

188 s at the molecular level, we observed single myosin V molecules that were differentially labeled with

189 this coordination, processive runs of single myosin V molecules were perturbed by varying nucleotide

190 Tropomyosin promotes myosin-V motility along actin cables.

191 A theoretical study of myosin-V motility is presented following an approach use

192 is mediated by interaction between the yeast myosin V motor Myo2 and organelle-specific adaptors.

193 The myosin V motor Myo2 attaches to these vesicles through i

194 In Saccharomyces cerevisiae, the myosin V motor Myo2 binds the vacuole-specific adapter V

195 For the yeast vacuole, the myosin V motor, Myo2, and its vacuole-specific cargo ada

196 -EPSC was via a mechanism dependent on actin/myosin V motor-based transport of AMPA receptors, which

197 istribution of additional cargoes moved by a myosin-V motor.

198 Myosin V motors are among the most conserved organelle m

199 Myosin V motors are believed to contribute to cell polar

200 Here we report how Spir actin nucleators and myosin V motors coordinate their specific membrane recru

201 hermore, we also see different velocities of myosin V motors in central regions of S2 cells, suggesti

202 nstrates that the well preserved function of myosin V motors in cytoplasmic transport can be accompli

203 New work on single myosin V motors provides insight into this switching and

204 Mammalian myosin V motors transport cargo processively along actin

205 tethering multiple myosin VI motors, but not myosin V motors, modifies their movement trajectories on

206 ontrast, tethering myosin VI motors, but not myosin V motors, progressively straightens the trajector

207 autoinhibition, and regulatory mechanisms in myosin V motors.

208 tions in a minimal system with kinesin-2 and myosin-V motors bound to beads.

209 We investigate how the combined system of myosin-V motors plus actin filaments is used to transpor

210 udies have shown that melanosomes carried by myosin V move 35 nm in a stepwise fashion in which the s

211 the light-chain domain (LCD) of myosin V as myosin V moves along actin.

212 To further investigate how myosin V moves processively on actin filaments, we alter

213 Compared with yeast myosin-II and myosin-V, muscle myosin-II activity was very sensitive t

214 Interestingly, the 8IQ myosin V mutant gave a broad distribution of step-sizes

215 of elevated levels to suppress a conditional myosin-V mutation (myo2-66), but its function with Myo2

216 f cells in late anaphase bearing exocyst and myosin V mutations show that both vesicle transport and

217 ated by binding a secretory vesicle and that myosin-V mutations that compromise vesicle binding rende

218 cle myosin subfragment 1 (S1) and non-muscle myosin V (MV).

219 The essential budding yeast myosin V Myo2 actively segregates most organelles along

220 releases yeast vacuoles and peroxisomes from myosin V (Myo2) and terminates organelle transport from

221 The yeast myosin V, Myo2, binds the vacuole-specific adaptor Vac17

222 min) depletes ATP levels and that the yeast myosin V, Myo2, responds by relocalizing to actin cables

223 novel interaction between Sro7 and the yeast myosin V, Myo2.

224 t interaction between Ypt31/32 and the yeast myosin V, Myo2.

225 hondrial inheritance: Arp2/3 complex and the myosin V Myo2p (together with its Rab-like binding partn

226 ted and characterized mutations in the yeast myosin V Myo2p to reveal that it is regulated by a head-

227 Further, the myosin-V Myo2p regulates the tethering time in a mechani

228 t, secretory vesicles are transported by the myosin-V Myo2p to sites of cell growth.

229 opsis, based on the known structure of yeast myosin V (Myo2p) globular tail.

230 Yeast myosin-II (Myo1p) and myosin-V (Myo2p) accommodate the reduced N-terminal char

231 Here, we report that the myosin-V Myo51 affects contractile ring assembly and sta

232 of an unconventional myosin-II (Myp2) and a myosin-V (Myo51) that are also present in the contractil

233 Here we show that in myosin V (myo52 myo51) null cells, actin cables are curl

234 k suggested, however, that the fission yeast myosin-V (Myo52p) is a nonprocessive motor whose activit

235 The molecular motor myosin V (MyoV) exhibits a wide repertoire of pathways d

236 Calcium can affect myosin V (myoV) function in at least two ways.

237 Unconventional myosin V (myoV) is an actin-based molecular motor that h

238 Myosin V (MyoV) motors have been implicated in the intra

239 Here we show that Ca(2+)-activated Myosin V (MyoV) pulls pigment granules to the rhabdomere

240 e present a kinetic model for the walking of myosin V on actin under conditions of zero external forc

241 ystem towards the unidirectional movement of myosin V on the actin filament.

242 hat most secretory vesicles are delivered by myosin-V on linear actin cables in fission yeast cytokin

243 ow that, at realistic concentrations of ATP, myosin-V operates in the regime which maximizes motor ve

244 that Rab11 and the associated motor protein Myosin V play essential roles in both endogenous and ect

245 e eGFPs, confirm the hand-over-hand model of myosin V procession, and when combined with previous dat

246 an example, we consider the case of a single myosin-V protein transporting a cargo and show that, at

247 ta cells and predict the effect of increased myosin V pulling.

248 When myosin V pulls loads inside the cell in a highly viscous

249 n of cargo attachment are organelle-specific myosin V receptors.

250 ro motility assays, double-headed Drosophila myosin V requires high surface concentrations to exhibit

251 r in the S217A mutant than in wild type (WT) myosin V, resulting in a slower steady-state rate of bas

252 probably by cargo binding itself, regulates myosin V's ability to transport cargo in the cell.

253 We directly observed myosin V's alternating heads while it walked hand-over-h

254 of the hand-over-hand model, thus confirming myosin V's mode of walking along an actin filament.

255 Run lengths of mouse myosin V showed little salt dependence, whereas those of

256 ity curve shows that under an external load, myosin-V slows down.

257 elease rate constant is reduced by Mg(2+) in myosin V, smooth muscle myosin, nonmuscle myosin IIA, CM

258 nalysis support the closed conformation as a myosin V state that is detached from actin.

259 As a control, we also tracked myosin V stepping along actin filaments and fascin-actin

260 support a model in which the coordination of myosin V stepping is mediated by strain-generated inhibi

261 We observed 35-nm myosin V steps in melanophores containing no IFs.

262 We find that myosin V steps occur faster in the absence of IFs, indic

263 Biochemical data for mammalian myosin V suggest that a head-to-tail autoinhibitory inte

264 myosin Va than for nonprocessive Drosophila myosin V, suggesting that this elastic tether between th

265 sfer studies confirmed that Rab10 binding to myosin V tails in vivo required the alternatively splice

266 lized by the expression of dominant-negative myosin V tails.

267 ning which of the several potential pathways myosin V takes in the process of ADP release and how act

268 Unconventional myosin V takes many 36-nm steps along an actin filament

269 tein complex containing actinin-4, BERP, and myosin V that is necessary for efficient TfR recycling b

270 We have developed a FRET system in myosin V that uses three donor-acceptor pairs to examine

271 , TgMyoF, which has structural similarity to myosin V, the prototypical cargo transporter.

272 Unlike previously studied vertebrate myosin Vs, the rate-limiting step in the actomyosin Vc A

273 For both kinesin and myosin V this behavior is implied remarkably well by sim

274 Unlike myosin V, this tail-induced restriction occurs independe

275 il domain is essential for the attachment of myosin V to all known cargoes.

276 the duty ratio from approximately 0.85 in WT myosin V to approximately 0.25 in S217A and produces a m

277 Thus, loop 2 is important for allowing myosin V to bind to actin with a relatively high affinit

278 s or IAEDANS-labeled actin and FlAsH-labeled myosin V to examine the conformation of the nucleotide-

279 actin allows the detached head of a stepping myosin V to find its next actin binding site more quickl

280 main-swapping approach with the nonselective myosin V to identify the selectivity module of myosin X.

281 However, if linking myosin V to melanosomes was Mlpha's sole function, eleva

282 nophilin function is that melanophilin links myosin V to melanosomes.

283 elements of myosin V work together to allow myosin V to step along actin for multiple ATPase cycles

284 ese data, we infer that P(i) release commits myosin V to undergo a highly load-dependent transition f

285 e test whether this feature is essential for myosin V to walk processively along an actin filament.

286 These tracks are used by myosin Vs to deliver secretory vesicles for cell growth,

287 In Schizosaccharomyces pombe, Myosin Vs transport secretory vesicles along actin cable

288 This is mediated by myosin Vs transporting cargos along F-actin bundles know

289 dynamics of the light chain domain of brain myosin V using a single-molecule fluorescence polarizati

290 d diverse directionalities of myosin motors (myosin V & VI).

291 The cargoes attach to the globular tail of myosin V via cargo-specific receptors.

292 A new study reports that a yeast myosin V walks on only a select few actin filaments - th

293 Single molecule experiments revealed that myosin-V walks in a stepwise fashion with occasional bac

294 The myosin V was labeled with bifunctional rhodamine on one

295 tural changes associated with ADP release in myosin V, which is thought to be a strain-sensitive step

296 iple motors including kinesin-2, dynein, and myosin-V, which drive switching between microtubules and

297 uggest that PTC1 promotes the association of myosin-V with its organelle-specific adaptor proteins.

298 ndings reveal how the structural elements of myosin V work together to allow myosin V to step along a

299 ng FIRST/FRODA starting with three different myosin V X-ray crystal structures to examine intrinsic f

300 st motor domain on the neck and rod of mouse myosin V (Y-MD) showed longer run lengths than mouse wil