ライフサイエンスコーパス: SNARE complex

1 closed complex with Munc18 into the ternary SNARE complex.

2 essed XFEL data set of the synaptotagmin-1 / SNARE complex.

3 a cooperative interaction with the neuronal SNARE complex.

4 rmations of complexin-1 bound to the ternary SNARE complex.

5 n apparently new coarse-grained model of the SNARE complex.

6 hibited the assembly of the binary Sso1-Sec9 SNARE complex.

7 molecules on average to disassemble a single SNARE complex.

8 domains to pseudo four-fold symmetry of the SNARE complex.

9 ease by inserting into the C-terminus of the SNARE complex.

10 and K201, adjacent to layers 7 and 8 of the SNARE complex.

11 um-mediated stabilization of the C2 domain.t-SNARE complex.

12 on by inhibiting the assembly of the ternary SNARE complex.

13 earrangement into an activated half-zippered SNARE complex.

14 icle-trafficking protein that is part of the SNARE complex.

15 ral entry by assembling a specific fusogenic SNARE complex.

16 or alpha-SNAP to first bind to the assembled SNARE complex.

17 mp mutant bound to a synaptobrevin-truncated SNARE complex.

18 ole for SYP61 and SYP121, possibly forming a SNARE complex.

19 simply increasing the amount of total trans-SNARE complex.

20 n secretion by limiting the formation of the SNARE complex.

21 ht to suppress assembly of syntaxin into the SNARE complex.

22 re region of complexin-1, which binds to the SNARE complex.

23 aptobrevin-2 and SNAP-25 to form the ternary SNARE complex.

24 unfolding of the C-terminal region in the t-SNARE complex.

25 configuration during assembly of the ternary SNARE complex.

26 ucture when not assembled with SYP121 in the SNARE complex.

27 ion compatible to interact with the complete SNARE complex.

28 downstream of VGCC, is the membrane-embedded SNARE complex.

29 involve different interaction modes with the SNARE complex.

30 ility of Cpx to prevent full assembly of the SNARE complex.

31 ns are dependent on distinct Rab GTPases and SNARE complexes.

32 complex with properties resembling canonical SNARE complexes.

33 e NSF/SNAP species can act on many different SNARE complexes.

34 brium docked state varies with the number of SNARE complexes.

35 binary Sec9-Sso1 and ternary Sec9-Sso1-Snc2 SNARE complexes.

36 the multisubunit tethering complexes and the SNARE complexes.

37 tagmin to compete with Gbetagamma binding to SNARE complexes.

38 ion, then hydrolyzing ATP to disassemble cis-SNARE complexes.

39 ctive loading of Sly1 and Vps33 onto cognate SNARE complexes.

40 resulting from a decrease in fusogenic STX-4 SNARE complexes.

41 ng vesicle formation at the TGN revealed cis-SNARE complexes.

42 and directly interacted with late endosomal SNARE complexes.

43 l division plane, transformed into fusogenic SNARE complexes.

44 ve zones of chemical synapses is executed by SNARE complexes.

45 x), whereas the C-terminal SNARE motif forms SNARE complexes.

46 ensitive fusion attachment protein receptor (SNARE) complexes.

47 ring differs for yeast (13 kBT) and neuronal SNARE complexes (27 kBT), and is concentrated at the C-t

48 he interaction of native complexins with the SNARE complex, a peptide consisting of the highly conser

49 Thus, the t-SNARE complex acted as a switch to enable fast and contr

50 fusion with the plasma membrane and ternary SNARE complex activity.

51 These SNARE complexes affect surface targeting of AMPA or GABA

52 We suggest that binding of alpha-SNAP to the SNARE complex affects the ability of the SNARE complex t

53 leimide-sensitive factor (NSF) (disassembles SNARE complexes after each membrane fusion event), and t

54 terface between synaptotagmin-1 and both the SNARE complex and complexin.

55 entral helix (CH) directly binds the ternary SNARE complex and is required for all known CPX function

56 ntral residues which bind the 0-layer of the SNARE complex and its N-terminal apolar loop.

57 as well as on complexins, which bind to the SNARE complex and play active and inhibitory roles.

58 Tomosyn recognizes the t-SNARE complex and prevents its pairing with the v-SNARE,

59 ytosolic protein, Complexin (Cpx), binds the SNARE complex and restricts spontaneous exocytosis by ac

60 t of complexin beginning with the acceptor t-SNARE complex and the subsequent activation of the clamp

61 ARE) complexes between the plasma membrane t-SNARE complex and the vesicle v-SNARE or VAMP.

62 a set from crystals of the synaptotagmin-1 / SNARE complex and to determine the structure at 3.5 A re

63 ein Munc18-1 promotes the zippering of trans-SNARE complexes and accelerates the kinetics of SNARE-de

64 We demonstrate that disruption of SNARE complexes and vesicle priming with botulinum C tox

65 eptor (SNARE)-mediated exocytosis, assembled SNARE complexes and vesicles adjacent to the plasma memb

66 ensitive factor attachment protein receptor (SNARE) complex and is essential for neurotransmission.

67 ensitive factor attachment protein receptor (SNARE) complexes and is regulated by tomosyn, a SNARE-bi

68 r machinery for synaptic vesicle fusion (the SNARE complex) and modulate transmitter release at conve

69 t studies have accumulated evidence that the SNARE complex, and more specifically the SNAP25 protein,

70 ks the complex, allows full zippering of the SNARE complex, and triggers membrane fusion.

71 The SNARE complex applies attractive forces to overcome the

72 of proteins involved in the formation of the SNARE complex are tightly regulated for efficient exocyt

73 Membrane-bridging SNARE complexes are critical for fusion, but their spont

74 are available per vesicle, only one to three SNARE complexes are minimally needed for a fusion reacti

75 eadily releasable pool size and formation of SNARE complexes are reduced.

76 amics, the transmembrane domains (TMDs) of t-SNARE complexes are shown to form aggregates leading to

77 ensitive factor attachment protein receptor (SNARE) complexes are the core molecular machinery of mem

78 orce spectroscopy, we modeled the synaptic t-SNARE complex as a parallel three-helix bundle with a sm

79 We found that all SNARE complexes assemble by the same step-wise zippering

80 8-1:syntaxin complex, followed by productive SNARE complex assembly and vesicle priming.

81 synaptic vesicle docking, priming, and trans-SNARE complex assembly are the respective morphological,

82 HOPS was essential to mediate SNARE complex assembly at physiological SNARE concentrat

83 we demonstrate that alpha-synuclein promotes SNARE complex assembly at the presynaptic plasma membran

84 s also monomeric, and whether chaperoning of SNARE complex assembly by alpha-synuclein involves its c

85 at Ca(2+)-CaM regulation of V100 may control SNARE complex assembly for a subset of synaptic vesicles

86 PS dimerization may be coupled to oligomeric SNARE complex assembly for vesicle docking and priming.

87 ertial protein unbinding associated with the SNARE complex assembly immediately after vesicle priming

88 Munc13s open Syntaxin-1, orchestrating SNARE complex assembly in an NSF-SNAP-resistant manner t

89 M) function to catalyze R-, Qa-, Qb-, and Qc-SNARE complex assembly in trans, as well as SNARE engage

90 Spontaneous quaternary SNARE complex assembly is very slow.

91 mplex relying on the others, suggesting four-SNARE complex assembly rather than direct binding of eac

92 We report an assay of SNARE complex assembly that does not rely on fusion and

93 Thus, Vps33 appears to catalyze SNARE complex assembly through specific SNARE motif reco

94 Munc18-1 orchestrates SNARE complex assembly together with Munc13-1 to mediate

95 s of strong and weak cooperative coupling of SNARE complex assembly where each mode implicates differ

96 Putative partial SNARE complex assembly with the SNARE motif mutant Stx1A

97 odel whereby Munc18-1 acts as a template for SNARE complex assembly, and autoinhibition of synaptobre

98 ARE complex, the early rate-limiting step in SNARE complex assembly, and stimulates membrane fusion.

99 ur study reveals an activation mechanism for SNARE complex assembly, and uncovers a role of the exocy

100 nities for the vacuolar SNAREs and catalyzes SNARE complex assembly, but the order of their assembly

101 ding sites on VAMP721, one also required for SNARE complex assembly, implies a well-defined sequence

102 s suggest a new model in which Sec6 promotes SNARE complex assembly, similar to the role proposed for

103 However, Syt-7-KD did not disrupt SNARE complex assembly.

104 nge-loop controls syntaxin-1A and subsequent SNARE complex assembly.

105 nd fusion competence, probably by initiating SNARE complex assembly.

106 the K(+) channels are nucleation points for SNARE complex assembly.

107 es to complete membrane merging by promoting SNARE complex assembly.

108 he bound syntaxin, probably preparing it for SNARE complex assembly.

109 transmission, can either promote or inhibit SNARE complex assembly.

110 or the transition of closed-to-open Syx1a in SNARE complex assembly.

111 which, together with Munc18-1, orchestrates SNARE complex assembly.

112 HOPS is required in this assay for rapid SNARE complex assembly.

113 unc13 may be related to regulation of proper SNARE complex assembly.

114 This region is needed for normal SNARE complex assembly.

115 nes soluble NSF attachment protein receptor (SNARE) complex assembly and may also perform other funct

116 ensitive factor attachment protein receptor (SNARE) complex assembly, and second, it boosts spike-evo

117 ensitive factor activating protein receptor (SNARE) complex assembly, thereby clamping fusion in the

118 ensitive factor attachment protein receptor (SNARE)-complex assembly.

119 is enhanced to examine the relation between SNARE-complex assembly and neurotransmitter release.

120 alpha-Synuclein physiologically chaperones SNARE-complex assembly at the synapse but pathologically

121 We show that enhancing SNARE-complex assembly dramatically increases the speed

122 ct role for SEC/MUNC18 proteins in promoting SNARE-complex assembly in vivo and suggest that STXBP2 R

123 ntaxin-1 is rendered constitutively open and SNARE-complex assembly is enhanced to examine the relati

124 SNARE-complex assembly mediates synaptic vesicle fusion

125 a-helical multimeric species that chaperones SNARE-complex assembly.

126 control presynaptic plasticity by regulating SNARE-complex assembly.

127 g energy and kinetics of four representative SNARE complexes at a single-molecule level using high-re

128 and Sec9 prevented the assembly of premature SNARE complexes at sites of exocytosis.

129 aperone to direct the assembly of productive SNARE complexes at the sites of membrane fusion.

130 e through inhibition of the formation of the SNARE complexes between synaptic vesicles and the plasma

131 ensitive factor attachment protein receptor (SNARE) complexes between the plasma membrane t-SNARE com

132 oth synaptotagmins bound to SNARE complexes; SNARE complex binding was reduced by the top-loop mutati

133 ect on the rate of the FRET at N-terminus of SNARE complex both with and without Ca(2+), indicating C

134 of Sec17 did not affect the levels of trans-SNARE complex but triggered sudden fusion of trans-SNARE

135 ) did not stimulate Sec18 to disassemble cis-SNARE complex but triggered the fusion of trans-SNARE pa

136 The formation of the SNARE complex by the vesicle SNARE synaptobrevin 2 (syb2

137 ensitive factor attachment protein receptor (SNARE) complexes by SNARE proteins syntaxin-1 (Stx1), sy

138 (1B)Rs) liberate Gbetagamma to interact with SNARE complex C terminals with no effect on Ca(2+) entry

139 en a loose and tightly zippered state at the SNARE complex C terminus.

140 ein known for its role in dismantling faulty SNARE complexes can also help to maintain complexes that

141 smission to or from neurons by targeting the SNARE complex, causing the characteristic paralyses of b

142 only the latter but not the former acts as a SNARE complex chaperone at the presynaptic terminal, and

143 l, and membrane-bound species that acts as a SNARE-complex chaperone over a monomeric, natively unfol

144 ptic vesicle fusion requires assembly of the SNARE complex composed of SNAP-25, syntaxin-1, and synap

145 complex via the central domain and a binary SNARE complex consisting of syntaxin-1A and SNAP-25A via

146 The t-SNARE complex consists of Syntaxin4 and SNAP23, and wher

147 The SNARE complex consists of the three proteins synaptobrev

148 measure the assembly energy and kinetics of SNARE complexes containing single mutations I67T/N in ne

149 g did not involve complexin, which activates SNARE complexes containing syntaxin-1 or -3, but not com

150 brane is mediated by formation of functional SNARE complexes containing syntaxin4, SNAP23, and VAMP2.

151 2)-containing proteoliposomes and acceptor t-SNARE complex-containing planar supported bilayers was e

152 MD simulations of the Drosophila Cpx-SNARE complex demonstrated that Cpx's interaction with t

153 t fusion, although it has an effect on the t-SNARE complex, depending on the presence of other factor

154 tor protein that mediates NSF binding to the SNARE complex, did not interact with septin-2, indicatin

155 el whereby binding of synaptotagmin-1 to the SNARE complex directly or indirectly causes a rearrangem

156 ophobic loop, fully supported Sec18-mediated SNARE complex disassembly but had lost the capacity to s

157 In vitro, Sly1 and Vps33 impede SNARE complex disassembly by Sec18 and ATP.

158 and the molecular mechanism of NSF-mediated SNARE complex disassembly remained unclear until recentl

159 lphaSNAP trimer that supports more efficient SNARE complex disassembly than monomeric alphaSNAP.

160 After vesicle fusion and subsequent SNARE complex disassembly, a prompt switch in syntaxin1a

161 at three molecules of alphaSNAP are used for SNARE complex disassembly.

162 ensitive factor attachment protein receptor (SNARE) complex drives the majority of intracellular and

163 requires a microarchitecture provided by the SNARE complex during vesicle priming.

164 es, facilitating assembly of plasma membrane SNARE complexes for cytotoxic granule fusion.

165 ARP binding regulates VAMP7 participation in SNARE complex formation and can therefore influence VAMP

166 720 can activate vesicular synaptobrevin for SNARE complex formation and enhance exocytosis in neuroe

167 studied in relation to its participation in SNARE complex formation and its interaction with phospho

168 ontrast to Munc18, however, Sly1 facilitates SNARE complex formation by loosening the closed conforma

169 e that insulin brings about this increase in SNARE complex formation by mobilizing a pool of syntaxin

170 erefore controls syntaxin-1A engagement into SNARE complex formation during priming.

171 A peptide inhibitor of SNARE complex formation failed to block exocytosis from

172 n causes an increase in syntaxin4-containing SNARE complex formation in adipocytes.

173 ndings support the hypothesis of upregulated SNARE complex formation in schizophrenia OFC, possibly f

174 region induced by Munc13-1 initiates ternary SNARE complex formation in the neuronal system.

175 This interaction is essential for SNARE complex formation in vitro and synaptic vesicle pr

176 ce and neurotransmitter release and complete SNARE complex formation is required for vesicle fusion a

177 Furthermore, we show that SNARE complex formation is required for vesicle fusion,

178 required for vesicle fusion, whereas partial SNARE complex formation is sufficient for vesicle dockin

179 vesicle fusion and priming, whereas partial SNARE complex formation is sufficient for vesicle dockin

180 found that Munc18c, like Munc18a, slows down SNARE complex formation through high-affinity binding to

181 Calmodulin promotes spontaneous release and SNARE complex formation via its interaction with the V0

182 Key components in the regulation of SNARE complex formation, and ultimately fusion, are the

183 N-peptide of syntaxin 1a, thereby inhibiting SNARE complex formation, Munc18b and -c, which have a mo

184 usion complex components, preventing ectopic SNARE complex formation, readying the synapse for subseq

185 at the plasma membrane, indicating increased SNARE complex formation, whereas FRET with other tested

186 uitination of Syn5 in early mitosis disrupts SNARE complex formation.

187 e-associated membrane protein 2), leading to SNARE complex formation.

188 ads to synaptobrevin-2/VAMP2 interaction and SNARE complex formation.

189 ol 4,5-bisphosphate (PIP2) and is related to SNARE complex formation.

190 ined their fusion competency with respect to SNARE complex formation.

191 ng its transition from "closed" state to the SNARE complex formation.

192 syntaxins and are thought to instead promote SNARE complex formation.

193 ensitive factor attachment protein receptor (SNARE) complex formation.

194 Neurotransmitter release depends on the SNARE complex formed by syntaxin-1, synaptobrevin and SN

195 , SM proteins Sly1 and Vps33 directly shield SNARE complexes from Sec17- and Sec18-mediated disassemb

196 lting primed state, with partially assembled SNARE complexes, fusion is inhibited by Synaptotagmin-1

197 SNARE complexes have been shown to act cooperatively to

198 Binding studies with soluble SNARE complexes have shown that Gbetagamma binds to both

199 ormational switch and collapse onto a single SNARE complex in a cis-binding mode to activate vesicle

200 Although the importance of a SNARE complex in neurotransmitter release is widely acce

201 er but can indeed bind simultaneously to the SNARE complex in solution.

202 unit a1 (V100) can regulate the formation of SNARE complexes in a Ca(2+)-Calmodulin (CaM)-dependent m

203 e applicability of FRET-FLIM for visualizing SNARE complexes in live cells with subcellular spatial r

204 ssembly pathway and molecular arrangement of SNARE complexes in membrane fusion reactions are not wel

205 does not insert into synaptobrevin-truncated SNARE complexes in solution, and electrophysiological da

206 ensitive factor attachment protein receptor (SNARE) complexes in conjunction with soluble N-ethylmale

207 small synaptic proteins that cooperate with SNARE-complexes in the control of synaptic vesicle (SV)

208 naptic vesicle cohort was not blocked by the SNARE complex-inhibiting peptide, whereas a later phase

209 usion, including a C2B surface implicated in SNARE complex interaction that is required for rapid syn

210 evoked release triggering, depend on direct SNARE complex interaction.

211 Transient knockdown of each component of the SNARE complex interfered with surface delivery of NMDA r

212 le NSF attachment protein), disassembles the SNARE complex into its protein components, making indivi

213 aughter cells in eukaryotic cytokinesis, the SNARE complexes involved are not known.

214 there is no universally conserved number of SNARE complexes involved as revealed by our observation

215 leading to the assembly of a fusogenic trans-SNARE complex involving vesicle-associated membrane prot

216 We find that a single SNARE complex is able to bring a typical synaptic vesicl

217 The coarse-grained model of the SNARE complex is calibrated by comparison with all-atom

218 After fusion, the SNARE complex is disassembled by the AAA-ATPase N-ethylm

219 However, how the assembly of the SNARE complex is initiated is unknown.

220 osis of NMDA receptors, suggesting that this SNARE complex is involved in excitatory synaptic transmi

221 ive, and binding to the prefusion acceptor t-SNARE complex is stronger than to the postfusion core co

222 ly, but the order of their assembly into a 4-SNARE complex is unclear.

223 Our results revealed that SNARE complexing is a key regulatory step for cytokine p

224 ensitive factor attachment protein receptor (SNARE) complexes known to mediate exocytosis of newcomer

225 d 'superclamp' mutation bound to a truncated SNARE complex lacking the C-terminus of the synaptobrevi

226 SF) perform ATP-dependent disassembly of cis-SNARE complexes, liberating SNAREs for subsequent assemb

227 This partially assembled SNARE complex locks the C-terminal (CTD) portion of the

228 plexin-1 induced conformation of the ternary SNARE complex may be related to a conformation that is j

229 The SNARE complex mediates neurotransmitter release in respo

230 leimide-sensitive factor attachment protein (SNARE) complex mediating fast Ca(2+)-triggered release o

231 eres with the zippering of membrane-anchored SNARE complexes midway through the zippering reaction, a

232 ins but also Munc-18-1 (stabilizes assembled SNARE complexes), N-ethylmaleimide-sensitive factor (NSF

233 that these two vesicle pools have formed the SNARE complexes necessary for fusion.

234 complexin binds to the 1:1 plasma membrane t-SNARE complex of syntaxin-1a and SNAP-25 while simultane

235 -ethylmaleimide attachment protein receptor (SNARE) complex of the vesicle fusion apparatus.

236 ropose a model in which Sec17 binds to trans-SNARE complexes, oligomerizes, and inserts apolar loops

237 TG14 directly binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8

238 in, and stabilizes the STX17-SNAP29 binary t-SNARE complex on autophagosomes.

239 cle-associated SNARE (v-SNARE) onto a binary SNARE complex on the target plasma membrane (t-SNARE).

240 formation of an activated binary target (t)-SNARE complex on the target plasma membrane, which then

241 xes between synaptotagmin-1 and the neuronal SNARE complex, one of which was determined with diffract

242 Phospho-SNAP23 stabilizes SNARE complexes orchestrating ERC-phagosome fusion, enri

243 r data indicate that the number of assembled SNARE complexes per vesicle during fusion determines the

244 The t-SNARE complex plays a central role in neuronal fusion.

245 The SNARE complex plays a vital role in vesicle fusion arisi

246 following cleavage of the C terminus of the SNARE complex protein SNAP-25 with botulinum A toxin.

247 blished players include the Rab GTPases, the SNARE complex proteins, and others, which function toget

248 re the light-chain endopeptidase cleaves the SNARE complex proteins, subverting the synaptic exocytos

249 -associated vesicles can form intervesicular SNARE complexes, providing mechanistic insight into comp

250 However, the t-SNARE complex readily misfolds, and its structure, stabi

251 Complexins (Cplxs) are SNARE complex regulators and photoreceptor ribbon synaps

252 Complexins (Cplxs) are SNARE complex regulators controlling the speed and Ca(2+

253 SH and AWC(ON) is differentially affected by SNARE-complex regulators that are present in both neuron

254 olipid metabolite, promotes formation of the SNARE complex required for membrane fusion and also incr

255 y been suggested that the oligomerization of SNARE complexes required for cooperative action in fusio

256 One hypothesis is that the SNARE complex's ability to bring membranes into contact

257 Thus, SNARE complexes share a conserved zippering pathway and

258 Further addition of SNARE complexes shortens this distance, but an overdocke

259 Both synaptotagmins bound to SNARE complexes; SNARE complex binding was reduced by th

260 when vesicle-associated v-SNAREs form trans-SNARE complexes ("SNAREpins") with target membrane-assoc

261 Here we show that the initial association of SNARE complexes, SNAREpins, is far too slow to support t

262 Zippering of SNARE complexes spanning docked membranes is essential f

263 also disassemble an engineered double-length SNARE complex, suggesting a processive unwinding mechani

264 shown that Gbetagamma binds to both ternary SNARE complexes, t-SNARE heterodimers, and monomeric SNA

265 -4) to bind cognate SNARE proteins to form a SNARE complex that mediates exocytosis in many cell type

266 brane-proximal C-terminal end of the ternary SNARE complex that specifically depends on the N-termina

267 Membrane fusion is induced by SNARE complexes that are anchored in both fusion partner

268 y a central role in membrane fusion, forming SNARE complexes that bridge the vesicle and plasma membr

269 e show that CDO occurs following assembly of SNARE complexes that include the vesicular SNARE, synapt

270 tes the formation of an Sso2-Sec9 'binary' t-SNARE complex, the early rate-limiting step in SNARE com

271 from the Munc18-1/syntaxin-1 complex to the SNARE complex, the molecular mechanism is unclear.

272 spring to prevent premature zippering of the SNARE complex, thereby reducing the likelihood of fusion

273 cycles SNAREs after fusion by binding to the SNARE complex through an adaptor protein, alphaSNAP, and

274 study, with estimates ranging from a single SNARE complex to 15.

275 , which in turn enables the formation of the SNARE complex to allow exosomes release.

276 the SNARE complex affects the ability of the SNARE complex to harness energy or transmit force to the

277 Peptide binding to the CTD activated the t-SNARE complex to initiate NTD zippering with the v-SNARE

278 specific complexin, acting as a brake on the SNARE complex to prevent spontaneous fusion in the absen

279 es the transition from a partially assembled SNARE complex to the fusion-competent SNAREpin.

280 hanics that couple C terminal zipping of the SNARE complex to the opening of the fusion pore.

281 twice in the fusion cycle, binding to trans-SNARE complexes to accelerate fusion, then hydrolyzing A

282 homodimers promote assembly of higher-order SNARE complexes to catalyze membrane fusion.

283 bits release and was proposed to insert into SNARE complexes to prevent their full assembly.

284 and at any given time, there are sufficient SNARE complexes to support the fusion of the entire ribb

285 le for FAK in the progression from assembled SNARE complexes to vesicle fusion in developing murine n

286 1 can simultaneously interact with a ternary SNARE complex via the central domain and a binary SNARE

287 olecule interacts with the other side of the SNARE complex via the previously identified primary inte

288 at complexin cross-links multiple pre-fusion SNARE complexes via a trans interaction to function as a

289 tudies indicated Cpx may cross-link multiple SNARE complexes via a trans interaction to function as a

290 of alphaSNAP binds to a soluble form of the SNARE complex, we find that three molecules of alphaSNAP

291 These inactive cytokinetic SNARE complexes were already assembled at the endoplasmi

292 ytic transmitter release is regulated by the SNARE complex, which contains a vesicular protein, synap

293 (Syx) is a central protein component of the SNARE complex, which underlies neurotransmitter release.

294 SNAPs interact with the SNARE complex with an opposite structural twist, suggest

295 e two parts, the coarse-grained model of the SNARE complex with membrane mechanics, we study how the

296 ociated with mature MDVs and forms a ternary SNARE complex with SNAP29 and VAMP7 to mediate MDV-endol

297 ng that all VAMP isoforms form SDS-resistant SNARE complexes with Syntaxin4/SNAP23 in vitro, a combin

298 Such long-distance trafficking of inactive SNARE complexes would also facilitate directional growth

299 cids at the SNAP-25 C terminus promote tight SNARE complex zippering and are required for high releas

300 py, we find that GTPase activation and trans-SNARE complex zippering have opposing effects on fragmen