ライフサイエンスコーパス: SNARE

1 SNARE (soluble N-ethylmaleimide sensitive factor attachm

2 SNARE protein's functionality is further regulated by a

3 SNARE proteins are essential for exocytosis, mediating t

4 SNARE proteins zipper to form complexes (SNAREpins) that

5 SNARE-mediated membrane fusion requires Sec1/Munc18-fami

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

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

8 aining nanodiscs, disrupting synaptotagmin-1-SNARE interactions.

9 mplex intermediate containing Munc18-1 and 2 SNARE proteins-syntaxin 1 and VAMP2.

10 Also, the syb-2 SNARE motif and, in particular, the linker domain show t

11 ence of stimulation and extracellular Ca(2+) SNARE perturbations demonstrate different mechanisms for

12 -SNAREs yields a rapid-fusion complex with 3 SNAREs in a trans-assembly.

13 f membranes bearing R-SNARE to those with 3Q-SNAREs far more than it enhances their trans-SNARE pairi

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

15 n one, alpha-syn binds to VAMP2, acting as a SNARE chaperone-but with no effect on neurotransmission-

16 Among these, Complexin3 (Cplx3), a SNARE regulator at ribbon synapses, was downregulated fi

17 Syntaxin 6 is a SNARE family protein known to play an important role in

18 Syntaxin 17 (Stx17), a SNARE with major roles in autophagy, was recently shown

19 isyn, a 24-kDa brain-enriched protein with a SNARE motif.

20 uired for Sec18 to bind to PA or to activate SNAREs.

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

22 The exo70A1 mutant affected SNARE distribution and suppressed vesicle traffic simila

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

24 Syntaxins are a family of membrane-anchored SNARE proteins that are essential components required fo

25 D-mediated support of membrane curvature and SNARE force-generated membrane bending promote fusion po

26 Interactions between exocyst and SNARE protein complexes are known, but their functional

27 by alphaSNAP, which inhibits exocytosis and SNARE-dependent liposome fusion.

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

29 hment protein receptor (SNARE) proteins, and SNARE chaperones of the Sec1/Munc18 (SM), Sec17/alpha-SN

30 n and vacuole protein sorting) tethering and SNARE-assembly complex, and the Rab Ypt7, bound to membr

31 ne domains (TMDs) of fusion proteins such as SNARE molecules drastically lower the free energy of bot

32 COPI coat and at the other to ER-associated SNAREs.

33 eport that syntaxin17 (Stx17), an autophagic SNARE protein interacts with CFTR under nutritional stre

34 by impeding the action of the autophagosomal SNAREs.

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

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

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

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

39 We observed that IPA blocks SNARE priming and competes for PA binding to Sec18.

40 Synapotagmin-1 (Syt1) interacts with both SNARE proteins and lipid membranes to synchronize neurot

41 rane while simultaneously ensuring that both SNAREs are in open conformations, with their SNARE motif

42 promoting the formation of membrane-bridging SNARE complexes.

43 s and relies on membrane fusion catalyzed by SNARE proteins.

44 It is completed by SNARE-mediated fusion of the autophagosome and endolysos

45 sicles with the plasma membrane is driven by SNARE protein interactions.

46 Exocytosis in platelets is mediated by SNARE proteins, and in most mammalian cells this process

47 h KRAS localization to the PM facilitated by SNAREs but antagonized by SNORD50A/B.

48 al interactions between subsets of so-called SNARE (soluble N-ethylmaleimide-sensitive factor attachm

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

50 cally activate the bound HOPS for catalyzing SNARE assembly, even if none of the SNAREs are membrane

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

52 unc13-1 and Munc18-1 cooperatively chaperone SNARE folding and assembly, thereby regulating synaptic

53 ering factors play a key role in chaperoning SNARE assembly; however, the underlying molecular mechan

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

55 at directs COG-bound vesicles toward cognate SNAREs on the Golgi membrane.

56 The highly conserved SNARE protein SEC22B mediates diverse and critical funct

57 Here, we identify the conserved SNARE regulator Complexin (Cpx) in an in vivo screen for

58 ane protein 2 (VAMP2/synaptobrevin2), a core SNARE protein residing on synaptic vesicles (SVs), forms

59 signaling, and tumorigenesis, and disrupting SNARE-enabled KRAS function represents a potential thera

60 ompanied by partial rescue of the downstream SNARE defects and the pathological hallmark of lipofusci

61 ay crystallography to investigate these Dsl1-SNARE interactions in greater detail.

62 changes that occur in hexameric Sec18 during SNARE priming.

63 S thus tethers membranes and recognizes each SNARE, assembling R+Qa or R+QbQc rapid fusion intermedia

64 his compound could help to further elucidate SNARE-priming dynamics.

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

66 h leg bind N-terminal Habc domains of the ER SNAREs Sec20 (a Qb-SNARE) and Use1 (a Qc-SNARE).

67 ural and functional similarity to eukaryotic SNAREs.

68 In neuronal exocytosis, SNARE assembly into a stable four-helix bundle drives me

69 their conformational changes, and facilitate SNARE assembly.

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

71 mplate complex is functionally important for SNARE assembly and neurotransmitter release.

72 Furthermore, we discover a critical role for SNARE proteins and their adaptors during early stages of

73 now report that HOPS binds each of the four SNAREs.

74 hat Sec18 monomers are sequestered away from SNAREs by binding phosphatidic acid (PA).

75 ) binds Sec18 and thereby sequesters it from SNAREs and that PA dephosphorylation dissociates Sec18 f

76 to the templated SNAREs and subsequent full SNARE assembly.

77 G(i/o)-coupled GPCRs through the Gbetagamma-SNARE interaction is a crucial component of numerous phy

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

79 et merger using arresting point mutations in SNARE proteins, but the nature of these states remained

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

81 ng nerve endings, they cleave and inactivate SNARE proteins, which are essential for neurotransmitter

82 Inactive SNARE bundles are reactivated by hexameric N-ethylmaleim

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

84 on of tail-anchored (TA) proteins, including SNAREs required for retrograde transport.

85 ure components from yeast vacuoles including SNAREs, the HOPS (homotypic fusion and vacuole protein s

86 Although PA can inhibit SNARE priming, it binds other proteins and thus cannot b

87 c13-1 collaborates with Munc18-1 to initiate SNARE assembly, thereby priming vesicles for fast calciu

88 re shown to be very versatile to investigate SNARE-mediated fusion on the single-particle level.

89 holds Tlg2 in an open conformation, with its SNARE motif disengaged from its Habc domain and its link

90 ced SNARE protein syntaxin 1a (STX1A), a key SNARE component.

91 man pseudoislets showed reduced Stx1a, a key SNARE component.

92 However, the key SNAREs involved remain highly controversial; syntaxin-3

93 rocesses are the vesicular fusion machinery (SNARE proteins) and the regulatory proteins, Synaptotagm

94 AREs that broaden the landscape of the mAtg8-SNARE interactions.

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

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

97 elucidate further details of Sec18-mediated SNARE priming.

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

99 nd preferentially to cognate plasma membrane SNAREs, notably SYP121 and VAMP721.

100 rameric RQaQbQc complexes between membranes; SNARE chaperones of the SM, Sec17/alphaSNAP, and Sec18/N

101 f the K(+) channels, is a nexus for multiple SNARE interactions.

102 sicles to target membranes, recruit multiple SNARE proteins, trigger their conformational changes, an

103 large pre-fusion complex, including multiple SNAREs and accessory proteins.

104 lly driven expression of a dominant-negative SNARE protein (dnSNARE) increased baroreflex sensitivity

105 t was found that Munc18-1 catalyzes neuronal SNARE assembly through an obligate template complex inte

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

107 s in reconstitution assays with the neuronal SNAREs, using syntaxin-1-SNAP-25-containing liposomes an

108 Assembly of SNARE complexes that mediate neurotransmitter release re

109 Vesicle fusion is mediated by assembly of SNARE proteins between opposing membranes.

110 king vesicles is mediated by the assembly of SNARE proteins into membrane-bridging complexes.

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

112 o investigate the conformational dynamics of SNARE/Munc18-1 complexes in multiple intermediate steps

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

114 se data are best explained by a hierarchy of SNARE recruitment to the exocyst at the plasma membrane,

115 and sheds light on the spatial regulation of SNARE assembly.

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

117 le previous work suggested an active role of SNARE transmembrane domains (TMDs) in promoting membrane

118 ese results underscore the critical roles of SNARE N-terminal domains in mediating interactions with

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

120 To demonstrate the utility of SNARE-seq, we generated joint profiles of 5,081 and 10,3

121 nd is precisely regulated by the assembly of SNAREs and accessory proteins.

122 rolysis drives the mechanical disassembly of SNAREs into individual coils, permitting a new cycle of

123 EACC affects the translocation of SNAREs Stx17 and SNAP29 on autophagosomes without impedi

124 t ability to bind calcium, phospholipids, or SNARE proteins.

125 pose a working model where tethering orients SNARE domains for parallel, active assembly.

126 es in this process by interacting with other SNARE and associated proteins.

127 SNAP25 structure and interactions with other SNAREs in aqueous buffer and in the membrane.

128 cts with STX3 as well as other photoreceptor SNAREs, and our findings indicate that STX3 is an essent

129 As in other eukaryotes, in plants, SNARE-mediated membrane traffic influences the density o

130 n Munc18-1 plays a critical role for precise SNARE assembly with the help of Munc13-1, but the underl

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

132 complex assembly through promoting prefusion SNARE binary complex formation.

133 evolution is tightly coupled to progressive SNARE complex formation.

134 n requires Sec1/Munc18-family (SM) proteins, SNARE chaperones that can function as templates to catal

135 is saturable at low concentrations of each Q-SNARE, showing binding site functionality.

136 The missing Q-SNARE then induces sudden fusion.

137 actor protein attachment protein receptor (Q-SNARE), SYNTAXIN OF PLANTS121 (SYP121), interacts with Q

138 COG) complex and multiple retrograde Golgi Q-SNAREs (where SNARE is soluble NSF-attachment protein re

139 proteins [VAMPs]) and the target membrane (Q-SNAREs).

140 Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS.

141 HOPS catalyzes fusion when the Q-SNAREs are not pre-assembled, ushering them into a funct

142 R-SNARE, and proteoliposomes with any two Q-SNAREs yields a rapid-fusion complex with 3 SNAREs in a

143 c-SNARE proteoliposomes in the absence of Qa-SNARE, awaiting Qa for fusion.

144 pacity of Ypt7 in cis to either the R- or Qa-SNARE to stimulate SNARE complex assembly.

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

146 Though the Qa-SNARE is essential for spontaneous SNARE assembly, HOPS

147 ically, the SM protein Munc18-1 traps the Qa-SNARE protein syntaxin-1 in an autoinhibited closed conf

148 he R-SNARE proteoliposomes but not on the Qa-SNARE proteoliposomes.

149 ry protein SEC11 is critical to prime the Qa-SNARE SYP121.

150 zing role for the Qbc-SNARE SNAP33 in the Qa-SNARE transition to SNARE complex assembly with the R-SN

151 same membrane as the R-SNARE but not the Qa-SNARE, thus explaining the asymmetric need for Ypt7 for

152 ly into RQaQbQc complexes when the R- and Qa-SNAREs are concentrated in the same micelles or in cis o

153 assembly through SM recognition of R- and Qa-SNAREs.

154 A HOPS SM-family subunit binds the R- and Qa-SNAREs.

155 s demonstrate that SM proteins can engage Qa-SNAREs using at least two different modes, one in which

156 ion between proteoliposomes bearing R- or Qa-SNAREs shows a strict requirement for Ypt7 on the R-SNAR

157 al Habc domains of the ER SNAREs Sec20 (a Qb-SNARE) and Use1 (a Qc-SNARE).

158 ults indicate a stabilizing role for the Qbc-SNARE SNAP33 in the Qa-SNARE transition to SNARE complex

159 s a rapid-fusion complex between R- and QbQc-SNARE proteoliposomes in the absence of Qa-SNARE, awaiti

160 yzed by conserved proteins R, Qa, Qb, and Qc SNAREs, which form tetrameric RQaQbQc complexes between

161 ER SNAREs Sec20 (a Qb-SNARE) and Use1 (a Qc-SNARE).

162 -associated membrane protein 8 (VAMP8), an R-SNARE found on late endosomes, could increase tau secret

163 increases the fusion of membranes bearing R-SNARE to those with 3Q-SNAREs far more than it enhances

164 ncubation of HOPS, proteoliposomes bearing R-SNARE, and proteoliposomes with any two Q-SNAREs yields

165 S subunit VPS33A and the cognate lysosomal R-SNARE VAMP8.

166 ps45 is unfurled, exposing the presumptive R-SNARE binding site to allow template complex formation.

167 Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS.

168 t at the plasma membrane, dominated by the R-SNARE and plausibly with the VAMP721 longin domain as a

169 bly when it is on the same membrane as the R-SNARE but not the Qa-SNARE, thus explaining the asymmetr

170 shows a strict requirement for Ypt7 on the R-SNARE proteoliposomes but not on the Qa-SNARE proteolipo

171 nsition to SNARE complex assembly with the R-SNARE VAMP721.

172 contain specific cargo, they have certain R-SNAREs for fusion, and they are endowed with a variety o

173 SNARE) proteins from the vesicle membrane (R-SNAREs or vesicle-associated membrane proteins [VAMPs])

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

175 eimide-sensitive factor attachment receptor (SNARE)-dependent fusion processes.

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

177 ensitive factor attachment protein receptor (SNARE) molecule vesicle-associated membrane protein 4 (V

178 ensitive factor attachment protein receptor (SNARE) protein in spontaneous neurotransmission.

179 ensitive factor attachment protein receptor (SNARE) protein that has been extensively studied in its

180 of soluble NSF attachment protein receptor (SNARE) proteins from the vesicle membrane (R-SNAREs or v

181 ensitive factor attachment protein receptor (SNARE) proteins, and SNARE chaperones of the Sec1/Munc18

182 ensitive factor attachment protein receptor (SNARE) proteins.

183 ensitive factor attachment protein receptor (SNARE)-mediated membrane fusion in all eukaryotes.

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

185 Synaptobrevin-2, a snap receptor (SNARE) protein, participates in this process by interact

186 nsitive factor attachment protein receptors (SNAREs) are conserved in fungi, plants and animals.

187 nsitive factor attachment protein receptors (SNAREs) mediate the formation of these dynamic structure

188 nsitive factor attachment protein receptors (SNAREs), that catalyze membrane fusion, and homotypic fu

189 e factor (NSF) attachment protein receptors (SNAREs).

190 Reconstituted SNAREs are constitutively active, so a major focus has b

191 cells and human pseudoislets showed reduced SNARE protein syntaxin 1a (STX1A), a key SNARE component

192 econstitution approach and compare regulated SNARE-mediated fusion of purified synaptic and dense cor

193 tors via exocytosis, a process that requires SNARE proteins, including syntaxins (Stxs).

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

195 SYP132 is a low-abundant, secretory SNARE that primarily localizes to the plasma membrane.

196 ccessibility and mRNA expression sequencing (SNARE-seq), a method that can link a cell's transcriptom

197 ed LC3-interacting regions (LIRs) in several SNAREs that broaden the landscape of the mAtg8-SNARE int

198 agonism between SNORD50A/B RNAs and specific SNARE proteins thus controls KRAS localization, signalin

199 gh the Qa-SNARE is essential for spontaneous SNARE assembly, HOPS also assembles a rapid-fusion compl

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

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

202 lization and consequent loss of its synaptic SNARE-chaperoning function.

203 ans the C-terminal half of the synaptobrevin SNARE motif.

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

205 r (v)-SNARE synaptobrevin and the target (t)-SNAREs Snap-25 and syntaxin-1.

206 A t-SNARE, synaptosome-associated protein of 25 kDa (SNAP-25

207 AP-25 linker: First, linker motifs support t-SNARE interactions and accelerate ternary complex assemb

208 ired for correct localization of the SYP61 t-SNARE.

209 thering factor that interacts with the TGN t-SNARE SYP41 and is required for correct localization of

210 nly in the free syntaxin-1 but also in the t-SNARE (syntaxin-1/SNAP-25) complex.

211 sed with lipid-labeled PSMs containing the t-SNARE acceptor complex DeltaN49 prepared on gold-coated

212 The t-SNARE acceptor complex DeltaN49 was reconstituted into P

213 rongly interacts with two syntaxins of the t-SNARE family (Glyma.12G194800 and Glyma.16G154200) in ye

214 reduced resistance to SCN, confirming that t-SNAREs are critical to resisting SCN infection.

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

216 ex enhances SNAP-25 binding to the templated SNAREs and subsequent full SNARE assembly.

217 yntaxin-1 and SNAP-25 through its C-terminal SNARE motif and competes with synaptobrevin-2/VAMP2 for

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

219 These results suggest that certain tether-SNARE interaction within Golgi stack may play a role in

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

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

222 Recent evidence suggests that SNARE fusion machinery play critical roles in postsynapt

223 Here we report that SNAREs are essential for the final step of this process,

224 5)P(2) However, unlike synaptrobrevin-2, the SNARE motif of amisyn is not sufficient to account for t

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

226 Both the pleckstrin homology domain and the SNARE motif are needed for its inhibitory function.

227 lin responsive aminopeptidase (IRAP) and the SNARE protein Syntaxin 6.

228 Oppositely, slowing of pore kinetics by the SNARE-regulator complexin-2 withstands the curvature-dri

229 releases the SNARE motif and facilitates the SNARE assembly.

230 x bundles with syntaxin-1 and SNAP25 for the SNARE assembly.

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

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

233 Here, the SNARE proteins are essential by forming the SNARE comple

234 response to lysosomal stress by impeding the SNARE protein ykt6.

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

236 ge of ER morphogenic proteins, including the SNARE protein syntaxin-18.

237 The C2B domain concurrently interacts the SNARE bundle via the 'primary' interface and is position

238 8-1 and Munc13-1 orchestrate assembly of the SNARE complex formed by syntaxin-1, SNAP-25 and synaptob

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

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

241 lipid unsaturation on the orientation of the SNARE complex.

242 that found in the "cis" interactions of the SNARE motifs after fusion when they co-localize in the p

243 S-Acylation of the SNARE protein SNAP25 (synaptosome-associated protein of

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

245 forces between the two membranes and/or the SNARE motifs and the membranes, helping to destabilize t

246 ion of VAMP2 SNARE motif, which releases the SNARE motif and facilitates the SNARE assembly.

247 Prior to the SNARE assembly, the structure of VAMP2 is unclear.

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

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

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

251 notably by inhibiting KRAS proximity to the SNARE vesicular transport proteins SNAP23, SNAP29, and V

252 s in multiple intermediate steps towards the SNARE complex.

253 least two different modes, one in which the SNARE is closed and one in which it is open.

254 ly, we find that septin 7 interacts with the SNARE protein syntaxin 11 and facilitates its interactio

255 cooperation between synaptotagmin-1 and the SNAREs in membrane fusion to trigger release.

256 talyzing SNARE assembly, even if none of the SNAREs are membrane bound.

257 the carriers, GARP promotes assembly of the SNAREs.

258 SNAREs are in open conformations, with their SNARE motifs available for assembly.

259 rom keratinocytes to sensory neurons through SNARE-mediated (syntaxin1) vesicle release.

260 mitters stored in secretory vesicles through SNARE-mediated exocytosis.

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

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

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

264 Auxin regulates abundance of the trafficking SNARE SYP132 over the time course of root growth and gra

265 ,5)P(2) inhibited vacuole fusion after trans-SNARE pairing.

266 -1 contribute to maintaining assembled trans-SNARE complexes in the presence of NSF-alphaSNAP.

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

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

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

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

271 SNAREs far more than it enhances their trans-SNARE pairings.

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

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

274 ed "linker" domain that concatenates the two SNARE motifs within SNAP-25.

275 The proximity of the two SNARE motifs, and therefore their ability to enter the s

276 ing factor, the Dsl1 complex, bound with two SNARE proteins, revealing new insights into how tetherin

277 n with the co-opted the syntaxin18-like Ufe1 SNARE protein within the TBSV replication compartments.

278 NARE complexes composed of the vesicular (v)-SNARE synaptobrevin and the target (t)-SNAREs Snap-25 an

279 The Vam7 gene encodes a v-SNARE protein that involved in vesicle trafficking in fu

280 We demonstrate a v-SNARE requirement in our tethering assay and increased v

281 20, and retromer that retrieve an exocytic v-SNARE from the endocytic pathway to the Golgi.

282 ement in our tethering assay and increased v-SNARE binding to exocyst gain-of-function complexes.

283 Here, we show that naturally-occurring v-SNARE TMD variants differentially regulate fusion pore d

284 large unilamellar vesicles containing the v-SNARE synaptobrevin 2, which were docked and fused with

285 xocyst that exposes a binding site for the v-SNARE.

286 Thus, v-SNARE TMDs and phospholipids cooperate in supporting mem

287 The budding yeast v-SNARE, Snc1, mediates fusion of exocytic vesicles to the

288 We now show that yeast vacuolar SNAREs assemble spontaneously into RQaQbQc complexes whe

289 sion, and recent studies with yeast vacuolar SNAREs uncovered asymmetry in the results of lipid mixin

290 be the dynamic membrane association of VAMP2 SNARE motif in mammalian cells, and the structural chang

291 ly weakens the membrane association of VAMP2 SNARE motif, which releases the SNARE motif and facilita

292 s" interactions between the synaptic vesicle SNARE protein synaptobrevin 2 and the plasma membrane sy

293 When SNAREs are free in solution or are tethered to distinct

294 nd multiple retrograde Golgi Q-SNAREs (where SNARE is soluble NSF-attachment protein receptor).

295 pairs of optically trapped beads coated with SNARE-free synthetic membranes to investigate Syt1-induc

296 calcium-binding proteins that interact with SNARE proteins and phospholipids.

297 al a broad direct interaction of mAtg8s with SNAREs with impact on membrane remodeling in eukaryotic

298 , H(+)-ATPase traffic, its relationship with SNAREs, and its regulation by auxin have remained enigma

299 rely a tether, as it supports fusion without SNARE recognition.

300 unction of FolVam7, a homologue of the yeast SNARE protein Vam7p in Fusarium oxysporum f. sp. lycoper