ライフサイエンスコーパス: SNARE complex

1 s in multiple intermediate steps towards the SNARE complex.

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

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

4 configuration during assembly of the ternary SNARE complex.

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

6 ion compatible to interact with the complete SNARE complex.

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

8 involve different interaction modes with the SNARE complex.

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

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

11 a cooperative interaction with the neuronal SNARE complex.

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

13 and VAMP2, leading to the dysfunction of the SNARE complex.

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

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

16 molecules on average to disassemble a single SNARE complex.

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

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

19 f Doc2 proteins to Syt1 binding sites in the SNARE complex.

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

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

22 lipid unsaturation on the orientation of the SNARE complex.

23 closed complex with Munc18 into the ternary SNARE complex.

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

25 e the assembly-disassembly cycle of neuronal SNARE complexes.

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

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

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

29 l division plane, transformed into fusogenic SNARE complexes.

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

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

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

33 complex with properties resembling canonical SNARE complexes.

34 er release and compete with Syt1 for binding SNARE complexes.

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

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

37 promoting the formation of membrane-bridging SNARE complexes.

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

39 the multisubunit tethering complexes and the SNARE complexes.

40 the concurrent binding of complexin to trans-SNARE complexes.

41 c18 from the membrane, allowing it to engage SNARE complexes.

42 and directly interacted with late endosomal SNARE complexes.

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

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

45 These SNARE complexes affect surface targeting of AMPA or GABA

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

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

48 Ca(2+)-free synaptotagmin-1 binds to SNARE complexes anchored on PIP(2)-containing nanodiscs.

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

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

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

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

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

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

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

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

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

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

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

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

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

62 The SNARE complex applies attractive forces to overcome the

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

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

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

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

67 d its lipid interactions, before forming the SNARE complex, are not fully understood at the molecular

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

69 le FRET, to address the relationship between SNARE complex assembly and rapid (micro-millisecond) fus

70 8-1:syntaxin complex, followed by productive SNARE complex assembly and vesicle priming.

71 rtant for priming because they mediate trans-SNARE complex assembly and/or because they prevent trans

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

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

74 ls and its interweaving within the events of SNARE complex assembly for exocytosis remains unclear.

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

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

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

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

79 Spontaneous quaternary SNARE complex assembly is very slow.

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

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

82 HOPS can 'template' SNARE complex assembly through SM recognition of R- and

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

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

85 rane-bound Ypt7 activates HOPS to catalyze 4-SNARE complex assembly when it is on the same membrane a

86 c-SNARE SNAP33 in the Qa-SNARE transition to SNARE complex assembly with the R-SNARE VAMP721.

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

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

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

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

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

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

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

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

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

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

97 This region is needed for normal SNARE complex assembly.

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

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

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

101 s that can function as templates to catalyze SNARE complex assembly.

102 is to either the R- or Qa-SNARE to stimulate SNARE complex assembly.

103 utionarily conserved role of Cpx upstream of SNARE complex assembly.

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

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

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

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

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

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

110 lexible loop and the membrane environment in SNARE-complex assembly at the residue level, which helps

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

112 We further proved that SNARE-complex assembly efficiency decreased when we disr

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

114 ting that the SNAP25 loop region facilitates SNARE-complex assembly through promoting prefusion SNARE

115 competes with synaptobrevin-2/VAMP2 for the SNARE-complex assembly.

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

117 op region of SNAP25 plays important roles in SNARE-complex assembly.

118 ilitates its interaction with syntaxin-1 and SNARE-complex assembly.

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

120 ries of stages that lead to the formation of SNARE complexes between cellular compartment membranes t

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

122 nsmitter release requires formation of trans-SNARE complexes between the synaptic vesicle and plasma

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

124 es elucidated three distinct synaptotagmin-1-SNARE complex binding modes involving 'polybasic', 'prim

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

126 release, disrupt and enhance synaptotagmin-1-SNARE complex binding, respectively.

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

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

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

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

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

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

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

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

135 ynaptic membrane, driven by the formation of SNARE complexes composed of the vesicular (v)-SNARE syna

136 ensitive factor attachment protein receptor (SNARE) complex comprises synaptosome-associated protein

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

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

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

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

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

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

143 The Ca(2+) sensor synaptotagmin-1 and the SNARE complex cooperate to trigger neurotransmitter rele

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

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

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

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

148 x assembly and/or because they prevent trans-SNARE complex disassembly by NSF-alphaSNAP, which can le

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

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

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

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

153 or precluding de-priming by preventing trans-SNARE complex disassembly; in this model, complexin-1 al

154 SNAP-25 is an essential component of SNARE complexes driving fast Ca(2+)-dependent exocytosis

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

156 720 can activate vesicular synaptobrevin for SNARE complex formation and enhance exocytosis in neuroe

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

158 as a gatekeeper for both binary and ternary SNARE complex formation by locking the syntaxin-1 in a c

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

160 heir interactors are important regulators of SNARE complex formation during vesicle fusion.

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

162 escence resonance energy transfer to measure SNARE complex formation in real time.

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

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

165 Here we show that trans-SNARE complex formation in the presence of NSF-alphaSNAP

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

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

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

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

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

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

172 Although SNARE complex formation was unaffected, we found that C8

173 1 can be rescued by increasing SYP41-SYP61 t-SNARE complex formation, implicating TNO1 as a tethering

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

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

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

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

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

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

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

181 evolution is tightly coupled to progressive SNARE complex formation.

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

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

184 syntaxin-1-SNAP-25 heterodimers, precluding SNARE complex formation; and binding to trans-SNARE comp

185 8-1 and Munc13-1 orchestrate assembly of the SNARE complex formed by syntaxin-1, SNAP-25 and synaptob

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

187 Sec18 functions by disrupting SNARE complexes formed in cis, on the same membrane.

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

189 SNARE complexes have been shown to act cooperatively to

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

191 his process depends on Ulk1, Rab GTPases and SNARE complexes implicated in secretory but not degradat

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

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

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

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

196 -1 contribute to maintaining assembled trans-SNARE complexes in the presence of NSF-alphaSNAP.

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

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

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

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

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

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

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

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

205 It is believed that the formation of the SNARE complex is a key step during membrane fusion.

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

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

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

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

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

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

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

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

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

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

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

217 These findings suggest that MCTP-SNARE complex-mediated endosomal trafficking is essentia

218 The SNARE complex mediates neurotransmitter release in respo

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

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

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

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

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

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

225 yo-electron microscopy structure of the Syt1-SNARE complex on anionic-lipid containing membranes.

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

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

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

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

230 At the top of the cycle, inactive cis-SNARE complexes on a single membrane are activated, or p

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

232 ensitive factor-attachment protein receptor (SNARE)] complexes or viral fusogenic proteins that activ

233 ur findings suggest that synaptobrevin-based SNARE complexes play a critical role in conferring Ca(2+

234 se findings suggest that synaptobrevin-based SNARE complexes play critical roles in conferring Ca(2+)

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

236 NARE complex formation; and binding to trans-SNARE complexes, preventing fusion.

237 ology domain, interacts with plasma membrane SNARE complex proteins via a central linker region, and

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

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

240 eimide-sensitive factor attachment receptor (SNARE) complex proteins in Th17 cells that enable a vesi

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

242 thering supports the assembly of new, active SNARE complexes rather than enhancing the function of th

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

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

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

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

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

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

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

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

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

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

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

254 Zippering of SNARE complexes spanning docked membranes is essential f

255 ition by receptors that work directly on the SNARE complex, such as 5-hydroxytryptamine (serotonin) 5

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

257 SNARE proteins are essential by forming the SNARE complex that drives vesicular membrane fusion.

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

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

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

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

262 ormation of an intermediate: committed trans-SNARE complexes that form large, stable pores.

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

264 Assembly of SNARE complexes that mediate neurotransmitter release re

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

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

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

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

269 Synaptotagmin-1 binds to the SNARE complex through the polybasic and primary interfac

270 ta suggest that synaptotagmin-1 binds to the SNARE complex through the primary interface and that Ca(

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

272 ond, the direct binding of Gbetagamma to the SNARE complex to displace synaptotagmin downstream of ca

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

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

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

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

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

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

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

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

281 lowed for predicting the number of tethering SNARE complexes upon loose docking and the size of the i

282 1 can simultaneously interact with a ternary SNARE complex via the central domain and a binary SNARE

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

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

285 bind and clamp a limited number of 'central' SNARE complexes via the primary interface and introduce

286 e we present the structure of a second SM-Qa-SNARE complex, Vps45-Tlg2.

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

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

289 nhancing the function of the fusion-inactive SNARE complexes which had spontaneously formed in the ab

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

291 Ca(2+) entry is the binding of Gbetagamma to SNARE complexes, which facilitate the fusion of vesicles

292 nd therefore their ability to enter the same SNARE complex, will depend on the relative orientation o

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

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

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

296 here that full-length amisyn forms a stable SNARE complex with syntaxin-1 and SNAP-25 through its C-

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