ライフサイエンスコーパス: SNARE

1 SNARE assembly occurs by stepwise zippering of the vesic

2 SNARE mutations have been associated with numerous disea

3 SNARE proteins are the core of the cell's fusion machine

4 SNARE proteins play a crucial role in intracellular traf

5 SNARE-domain zippering draws the bilayers into immediate

6 SNAREs can be disassociated by Sec 17/Sec 18/ATP, comple

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

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

9 2) a HOPS:R:Qa:Qc trans-complex, 3) a HOPS:4-SNARE trans-complex, 4) an engagement with Sec17, and 5)

10 affected by downregulation of syntaxin 17, a SNARE promoting autophagosome-lysosome fusion and cargo

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

12 Dense-core vesicle (DCV) exocytosis is a SNARE (soluble N-ethylmaleimide-sensitive fusion attachm

13 Complexin-1 is a SNARE effector protein that decreases spontaneous neurot

14 also function as recycling signal to sort a SNARE into COPI vesicles in a non-degradative pathway.

15 Syntaxin 3 (Stx3), a SNARE protein located and functioning at the apical plas

16 However, whether a SNARE such as STX11, which lacks a transmembrane domain,

17 granules fuse with GUVs containing activated SNAREs with only few milliseconds delay between docking

18 t remains unclear how these mutations affect SNARE zippering, partly due to difficulties to quantify

19 leaflets of the supported bilayers affected SNARE-mediated fusion.

20 xocytosis of lysosomes using the exocyst and SNARE SNAP-29 to form a large protrusion that invades vu

21 iological protein levels, the slow HOPS- and SNARE-dependent fusion which occurs upon complete SNARE

22 mains that bind to phospholipids, Ca(2+) and SNAREs.

23 mode of interaction between SM proteins and SNAREs is debated, as contrasting binding modes have bee

24 -SNARE complex assembly in trans, as well as SNARE engagement by the SNARE-binding chaperone Sec17/al

25 s orchestrated by synaptic proteins, such as SNAREs, synaptotagmin, and complexin, but the molecular

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

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

28 st entirely dissipated, with fully assembled SNARE motifs but uncomplexed linker domains.

29 by catalyzing membrane fusion, but assigning SNAREs to specific intracellular transport routes is cha

30 iled-coil tail binds to the Golgi-associated SNARE, Sed5.

31 stepwise zippering of the vesicle-associated SNARE (v-SNARE) onto a binary SNARE complex on the targe

32 s the binding of Vamp8 to the autophagosomal SNARE Syntaxin 17 to modulate the fusion of autophagosom

33 Fusion involves complex formation between SNARE proteins anchored to adjacent membranes.

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

35 wild-type Gbetagamma were also shown to bind SNAREs at a higher affinity than wild type in a lipid en

36 e-grained model that retains key biophysical SNARE properties such as the zippering energy landscape

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

38 molecular mechanism of the disease caused by SNARE mutations.

39 nderlying initial plasma membrane contact by SNARE proteins, which subsequently become palmitoylated

40 Multiple membrane-fusion events mediated by SNARE molecules have been postulated to promote autophag

41 on membrane trafficking mediated in part by SNAREs.

42 teins of the Sec 1/Munc18 family to catalyze SNARE assembly into trans-complexes.

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

44 ether, these data indicate that the cellular SNARE system is involved in AcMNPV infection and that NS

45 Here, we examined the cellular SNARE system, which mediates the fusion of vesicles in h

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

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

48 resynaptic compartments, but does not cleave SNARE proteins nor impair spontaneous neurotransmitter r

49 ctivating syntaxin-4 (STX-4) to bind cognate SNARE proteins to form a SNARE complex that mediates exo

50 ow that lipid-anchored STX11 and its cognate SNARE proteins mainly support exchange of lipids but not

51 ion compatible to interact with the complete SNARE complex.

52 -dependent fusion which occurs upon complete SNARE zippering is stimulated by Sec17 and Sec18:ATP wit

53 The core SNARE protein syntaxin-1a (syn1a) was expressed by murin

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

55 zed cytosolic cargo receptor and a dedicated SNARE system.

56 Munc13-4 is a Ca(2+)-dependent SNARE (soluble N-ethylmaleimide-sensitive factor attachm

57 impair synaptic exocytosis by destabilizing SNARE assembly, rather than stabilizing SNARE assembly a

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

59 alk between Rab GTPases and tethers to drive SNARE-mediated lipid bilayer mixing.

60 HOPS binding to Ypt7-GTP then drives SNARE-mediated fusion, which is fully GTP-dependent.

61 reby coordinating K(+) channel gating during SNARE assembly and vesicle fusion.

62 Each SNARE assembles into this complex relying on the others,

63 Rab GTPases, their effectors, SNAREs of the R, Qa, Qb, and Qc families, and SM SNARE-b

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

65 However, insertion of early endosomal SNARE proteins suffices to convert liposomes into traffi

66 and directly interacted with late endosomal SNARE complexes.

67 With few exceptions, SNAREs are tail-anchored (TA) proteins, bearing a C-term

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

69 t1 undergoes competition with Gbetagamma for SNARE-binding sites in lipid environments.

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

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

72 downstream of the Rab-GTPase Ypt7 needed for SNARE-mediated lipid bilayer merger.

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

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

75 720 can activate vesicular synaptobrevin for SNARE complex formation and enhance exocytosis in neuroe

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

77 r which tethering does not coenrich the four SNAREs.

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

79 erlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type

80 crystal structures of the primed pre-fusion SNARE-complexin-synaptotagmin-1 complex.

81 l division plane, transformed into fusogenic SNARE complexes.

82 However, in secretory cells, Gbetagamma, SNAREs, and synaptotagmin interact in the lipid environm

83 portance of these regions for the Gbetagamma-SNARE interaction and show that the target of Gbetagamma

84 erging picture of the ubiquity of Gbetagamma/SNARE interactions in regulating synaptic transmission t

85 ric Golgi (COG) complex and with intra-Golgi SNARE proteins.

86 ng is driven by the assembly of heterologous SNARE proteins orchestrated by the binding of Sec1/Munc1

87 Here, we explore how SNARE regulators operate on discrete zippering states.

88 y have been identified as priming factors in SNARE-dependent exocytosis.

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

90 multifunctional protein that participates in SNARE-mediated membrane fusion events.

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

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

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

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

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

96 s that Syn-2 could function as an inhibitory SNARE protein that, when relieved, could promote exocyto

97 How and in what form interacting SNARE proteins reach their sites of action is virtually

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

99 ked exocytosis in retinal ribbon synapses is SNARE-dependent; where vesicles higher up on the synapti

100 um-sensitive scaffolding protein, localizing SNARE proteins proximal to the calcium channel so as to

101 we modeled exocytosis using plasma membrane SNARE-containing planar-supported bilayers and purified

102 mes initially containing the plasma membrane SNAREs syntaxin-1 and soluble NSF attachment protein (SN

103 our knowledge, a new platform for monitoring SNARE-mediated docking and fusion between giant unilamel

104 mplexes, t-SNARE heterodimers, and monomeric SNAREs, competing with synaptotagmin 1(syt1) for binding

105 irus (AcMNPV), the transcript levels of most SNARE genes initially were upregulated.

106 s found capable of interacting with multiple SNARE and Cav1.3 proteins simultaneously, forming a hete

107 Synaptotagmin, complexin, and neuronal SNARE (soluble N-ethylmaleimide sensitive factor attachm

108 re highly potent toxins that cleave neuronal SNARE proteins required for neurotransmission, causing f

109 to the fully assembled four-helical neuronal SNARE core complex as revealed in competing molecular mo

110 ntaining single mutations I67T/N in neuronal SNARE synaptosomal-associated protein of 25kDa (SNAP-25B

111 region (5RK) of the plasma membrane neuronal SNARE, syntaxin 1A (Syx), in vesicle exocytosis, althoug

112 The minimal system, consisting of neuronal SNAREs and synaptotagmin-1, produced point and long-cont

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

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

115 transmission by endoproteolytic cleavage of SNARE proteins.

116 /Sec 18/ATP, completing a catalyzed cycle of SNARE assembly and disassembly.

117 re important tools to analyze the details of SNARE-mediated fusion processes.

118 Exocytosis depends on cytosolic domains of SNARE proteins but the function of the transmembrane dom

119 5 (STX5), a member of the syntaxin family of SNARE proteins.

120 embrane fusion is sensitive to inhibition of SNARE priming, the initial stages of autophagosome bioge

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

122 s to quantify the energetics and kinetics of SNARE assembly.

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

124 s two Rab bindings to determine the place of SNARE assembly and thus fusion at endomembranes.

125 livery of large stoichiometric quantities of SNARE proteins required for forming the partitioning mem

126 , advancing our understanding of the role of SNARE function in the localization of proteins that driv

127 Zippering of SNARE complexes spanning docked membranes is essential f

128 We find that there is no critical number of SNAREs required for fusion, but instead the fusion rate

129 ter expected to be altered by recruitment of SNAREs at fusion sites.

130 te function in downstream priming depends on SNARE-binding, Ca(2+)-binding to the C2B-domain of Doc2B

131 for secretion of digestive enzymes relies on SNARE-mediated exocytosis.

132 Once SNAREs are partially zipped, Sec17 promotes fusion in ei

133 Membrane tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to ca

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

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

136 gy through interaction with Atg14L and other SNAREs in starved cells.

137 Thus, Vps33/HOPS promotes productive SNARE assembly in the presence of otherwise inhibitory S

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

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

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

141 y Lobe A of the COG complex and the purified SNARE proteins Gos1, Sed5 and Sft1.

142 ed R-SNARE on one membrane and an anchored Q-SNARE on the other.

143 RE or one of the three integrally anchored Q-SNAREs were incubated with the tethering/SM protein comp

144 liposomes containing exocytic or endosomal Q-SNAREs and directly interacted with late endosomal SNARE

145 n, has conserved grooves that bind R- and Qa-SNARE domains.

146 HOPS, lipid membranes to which the R- or Qa-SNARE and Ypt7:GTP are integrally bound, and each of the

147 lone, at physiological concentrations the Qa-SNARE heptad-repeat domain alone has almost no fusion ac

148 omoted by very high concentrations of the Qa-SNARE heptad-repeat domain alone, at physiological conce

149 te for rapid fusion after addition of the Qb-SNARE and Sec17 proteins.

150 The N-domain of the Qb-SNARE was completely dispensable for fusion.

151 lar Rabs for tethering, another binds the Qc SNARE, and a fourth HOPS subunit, an SM protein, has con

152 ill assemble with HOPS and the R, Qa, and Qc SNAREs, and that this assembly undergoes rapid fusion up

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

154 Spontaneous quaternary SNARE complex assembly is very slow.

155 Fusion required a transmembrane-anchored R-SNARE on one membrane and an anchored Q-SNARE on the oth

156 pression of Tomosyn-1 (Tomo-1), a soluble, R-SNARE domain-containing protein, significantly affects b

157 ccurs independently of Tomo-1's C-terminal R-SNARE domain.

158 and that this receptor interacts with the R-SNARE Sec22b to recruit cargo to the LC3-II(+) sequestra

159 bearing a Rab:GTP and either the vacuolar R-SNARE or one of the three integrally anchored Q-SNAREs w

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

161 ize spontaneous fusion while enabling rapid, SNARE-dependent fusion upon demand.

162 eimide-sensitive factor attachment receptor (SNARE) proteins into a parallel four-helix bundle to dri

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

164 ensitive factor attachment protein receptor (SNARE) protein syntaxin-1 adopts a closed conformation w

165 ensitive factor attachment protein receptor (SNARE) protein that is known to participate in the regul

166 ensitive factor attachment protein receptor (SNARE) proteins are key players in cellular trafficking

167 ensitive factor activating protein receptor (SNARE) proteins are the main catalysts for membrane fusi

168 ve factor (NSF) attachment protein receptor (SNARE) proteins comprise the minimal machinery that trig

169 ensitive factor attachment protein receptor (SNARE) proteins play a major role in membrane fusion and

170 ensitive factor attachment protein receptor (SNARE) Vamp8.

171 -ethylmaleimide attachment protein receptor (SNARE)-mediated exocytosis, assembled SNARE complexes an

172 nsitive factor-attachment protein receptors (SNAREs) constitute the core machinery for membrane fusio

173 nsitive factor attachment protein receptors (SNAREs)].

174 Atget lines, possibly as a result of reduced SNARE biogenesis.

175 ation of both Atg9 and the autophagy-related SNARE protein syntaxin17 with the autophagosome remained

176 vin-2 for the 1:1 complex, thereby retarding SNARE assembly and vesicle docking in vitro.

177 h also are similar to those of the secretory SNARE mutant, syp121 The syp121 and chc mutants have imp

178 Es of the R, Qa, Qb, and Qc families, and SM SNARE-binding proteins catalyze intracellular membrane f

179 phosphorylation cycles in controlling SNAP23 SNARE function in homotypic SG fusion.

180 eved by just four soluble factors: a soluble SNARE (Vam7), a guanine nucleotide exchange factor (GEF,

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

182 otein complex HOPS and the two other soluble SNAREs (lacking a transmembrane anchor) or their SNARE h

183 zing SNARE assembly, rather than stabilizing SNARE assembly as previously proposed.

184 7 (alpha-SNAP) either inhibits or stimulates SNARE-mediated fusion.

185 n receptor) heptad-repeats are well studied, SNAREs also have upstream N-domains of indeterminate fun

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

187 lacking the C-terminus of the synaptobrevin SNARE motif (SNAREDelta60) suggested that an 'accessory'

188 Comparisons with the synaptotagmin1-SNARE show that both proteins contact the same SNAP25 su

189 c1/Munc18 (SM) proteins to specific syntaxin SNARE proteins.

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

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

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

193 mma binds to both ternary SNARE complexes, t-SNARE heterodimers, and monomeric SNAREs, competing with

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

195 ARE complex on the target plasma membrane (t-SNARE).

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

197 synaptotagmin 1(syt1) for binding sites on t-SNARE.

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

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

200 The PSMs harbor the t-SNARE DeltaN49-complex to investigate the dynamics and f

201 ng exocytosis, directly interacts with the t-SNARE protein Sso2.

202 rin-coated vesicles and interacts with the t-SNARE, Syntaxin3.

203 NAREpins") with target membrane-associated t-SNAREs, a zippering-like process releasing approximately

204 interacts specifically with lipid-embedded t-SNAREs consisting of full-length syntaxin 1 and SNAP-25B

205 ectopically expressing cognate, 'flipped' t-SNAREs.

206 le-associated v-SNAREs and target membrane t-SNAREs, but the mechanisms governing the subsequent pore

207 ynaptogenesis, within 1-4 DIV upon loss of t-SNAREs (syntaxin-1, SNAP-25) or Munc18-1, but not v-SNAR

208 e local interactions of fluorescently tagged SNARE proteins in live cells.

209 In contrast, when complete C-terminal SNARE zippering is prevented, fusion strictly requires S

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

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

212 closed complex with Munc18 into the ternary SNARE complex.

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

214 configuration during assembly of the ternary SNARE complex.

215 ex formation, whereas FRET with other tested SNAREs was unaltered.

216 ited Ca(2+)-stimulated interactions with TGN SNAREs, and underwent Ca(2+)-stimulated TGN recruitment.

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

218 ental and computational results suggest that SNARE availability may be pivotal in determining whether

219 The SNARE domain is thought to wrap around this structure wh

220 The SNARE protein syntaxin4 (Stx4) is involved in the format

221 The SNARE SYP121 of Arabidopsis thaliana that facilitates ve

222 el's intracellular C-terminus domain and the SNARE (soluble N-ethylmaleimide-sensitive factor activat

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

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

225 in trans, as well as SNARE engagement by the SNARE-binding chaperone Sec17/alphaSNAP.

226 alphaSNAP, the adaptor molecule for the SNARE-priming enzyme N-ethylmaleimide-sensitive factor (

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

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

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

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

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

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

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

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

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

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

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

238 ry DNA strands to model the formation of the SNARE four-helix bundle that mediates synaptic vesicle f

239 98 region of Qa, immediately upstream of the SNARE heptad-repeat domain, is required for normal fusio

240 emonstrated that a general disruption of the SNARE machinery significantly inhibited the production o

241 for FcepsilonRI-triggered association of the SNARE protein SNAP23 with the SGs.

242 The TMD of the SNARE protein synaptobrevin2/VAMP2 contains two highly c

243 ed that genes encoding the components of the SNARE system are highly conserved in yeast, insect, and

244 expression of NSF, the key regulator of the SNARE system, significantly affected infectious AcMNPV p

245 Genetic deletion of the SNARE-binding protein complexin dramatically increases s

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

247 our results reveal that B-cells rely on the SNARE protein Vamp-7 to promote the local exocytosis of

248 rtheless sufficient to partially promote the SNARE priming required for autophagy.

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

250 ndings are the first to demonstrate that the SNARE system is required for efficient entry of BV and n

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

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

253 Recent studies suggest revisions to the SNARE paradigm of membrane fusion.

254 The SNAREs SNAP25 and SNAP23 are proteins that are initially

255 in families (reviewed in [2]), including the SNAREs [3], SM proteins [4, 5], ion channels [6, 7], and

256 017) demonstrate that Unc13 ensures that the SNAREs assemble into functional subcomplexes.

257 Es (lacking a transmembrane anchor) or their SNARE heptad-repeat domains.

258 ntegrally bound, and each of the other three SNAREs.

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

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

261 onclude that after initial contact in trans, SNAREs alone can complete fusion at a rate close to fast

262 e context of membrane, Ypt7, HOPS, and trans-SNARE assembly and serves as a functional intermediate f

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

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

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

266 The tripartite SNARE-complexin-synaptotagmin-1 complex at a synaptic ve

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

268 Using SNARE-decorated proteoliposomes that cannot fuse on thei

269 E copies and was far from saturating at 15 v-SNARE copies per face, the NLP capacity.

270 Snc1 is a v-SNARE that drives fusion of exocytic vesicles with the p

271 REs per NLP face, and further increases in v-SNARE copy numbers did not affect nucleation rate.

272 of pore dilation increased with increasing v-SNARE copies and was far from saturating at 15 v-SNARE c

273 in the recycling of the synaptobrevin-like v-SNARE Snc1 from early endosomes.

274 eimide factor attachment protein receptor (v-SNARE) called cellubrevin/vesicle-associated membrane pr

275 zippering of the vesicle-associated SNARE (v-SNARE) onto a binary SNARE complex on the target plasma

276 Here we show that the v-SNARE protein Vamp-7 is associated with Lamp-1(+) lysoso

277 viously identified Syp1 cargo Mid2 and the v-SNARE Snc1.

278 large unilamellar vesicles doped with the v-SNARE synaptobrevin 2 by means of spinning-disc confocal

279 the dilation of single fusion pores using v-SNARE-reconstituted 23-nm-diameter discoidal nanolipopr

280 tro fusion assays using full-length t- and v-SNAREs embedded in liposomes, Gbetagamma inhibited Ca(2+

281 uires zippering between vesicle-associated v-SNAREs and target membrane t-SNAREs, but the mechanisms

282 usion is catalyzed when vesicle-associated v-SNAREs form trans-SNARE complexes ("SNAREpins") with tar

283 (syntaxin-1, SNAP-25) or Munc18-1, but not v-SNAREs (synaptobrevins/VAMP1/2/3 using tetanus neurotoxi

284 ansmission, exploiting the large number of v-SNAREs available in synaptic vesicles.

285 Pore nucleation required a minimum of two v-SNAREs per NLP face, and further increases in v-SNARE co

286 ion and to a lesser extent on VTI11 vacuolar SNARE activity.

287 OPS-tethered membranes and all four vacuolar SNAREs formed a complex that underwent an even more dram

288 lso has specific affinities for the vacuolar SNAREs and catalyzes SNARE complex assembly, but the ord

289 The assembly of yeast vacuolar SNAREs into complexes for fusion can be studied in chemi

290 formational displacement between the VAMP721 SNARE and longin domains.

291 Binding to the VAMP721 SNARE domain suppressed channel gating.

292 teoliposomes containing the synaptic vesicle SNARE synaptobrevin (with or without the Ca(2+) sensor s

293 targeted the non-canonical synaptic vesicle SNAREs Vps10p-tail-interactor-1a (vti1a) and vesicle-ass

294 f SNARE complexes that include the vesicular SNARE, synaptobrevin 2, and that the participation of 5R

295 cuit, confirming the role of these vesicular SNAREs in setting synaptic strength.

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

297 In vitro, SNAREs are sufficient to mediate effective fusion of bot

298 Whereas SNARE (soluble N -ethylmaleimide-sensitive factor attach

299 In a reconstituted fusion assay with SNAREs, complexin, and synaptotagmin, inclusion of both

300 ial for trafficking of a ubiquitinated yeast SNARE (Snc1).