ライフサイエンスコーパス: v-SNARE

1 v-SNAREs but not resident proteins were concentrated in

2 v-SNAREs were thought to ensure specificity in membrane

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

4 Although VAMP-8 (v-SNARE) and SNAP-23 (a t-SNARE class) are important for

5 disassembly, showing that Hceb can act as a v-SNARE in platelets.

6 transmembrane anchor and so cannot act as a v-SNARE in this complex.

7 restricted by design to function either as a v-SNARE or as part of a t-SNARE complex.

8 We propose that AtVTI1a functions as a v-SNARE responsible for targeting AtELP-containing vesic

9 the prevacuolar compartment and AtVTI1a as a v-SNARE that interacts with AtPEP12p.

10 , we identified the yeast protein Vti1p as a v-SNARE that is involved in two transport reactions.

11 h Vti1a has previously been reported to be a v-SNARE localized in the trans-Golgi network, treatment

12 t example of a Ca(2+)-ATPase regulation by a v-SNARE protein involved in membrane fusion reactions.

13 In this work, we report that cellubrevin, a v-SNARE functioning in endosomal recycling and implicate

14 The DdSnc1, a v-SNARE protein, accumulates at the inner side of ring c

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

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

17 ontrolling the localization of endobrevin, a v-SNARE required for cell abscission.

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

19 Furthermore, Sec22p, a v-SNARE implicated in forward transport from ER to Golgi

20 s significant sequence homology to Sec22p, a v-SNARE in Saccharomyces cerevisiae required for transpo

21 owever when t-SNARE vesicles were added to a v-SNARE membrane, SNAREs assembles in a ring pattern and

22 Finally we show that Vti1p, a v-SNARE required for the delivery of both CPY and ALP to

23 a-Syn(FL) accessed v-SNARE within the trans-SNARE complex to form an inhibi

24 e that two mutations in the vesicle-anchored v-SNARE selectively impair the ability of Munc18-1 to pr

25 embled by recombinant t-SNARE Sso1p/Sec9 and v-SNARE Snc2p, which are involved in post-Golgi traffick

26 hat monitor lipid mixing between t-SNARE and v-SNARE vesicles in bulk solution exhibit remarkably slo

27 is dependent on the presence of t-SNAREs and v-SNARE in opposing bilayers.

28 sition is highly conserved across the t- and v-SNARE families, and it was recently suggested that a 3

29 n this process, t-SNAREs BNIP1 and USE1, and v-SNARE YKT6.

30 a soluble cargo molecule (alpha-factor) and v-SNAREs (Sec22p and Bet1p) into COPII vesicles.

31 ng to simultaneously visualize receptors and v-SNAREs in real time in individual fusion events, we id

32 Even when t- and v-SNAREs are on separate membranes, Sec17p and Sec18p ac

33 Thus, t- and v-SNAREs are required to reside in opposing bilayers to

34 t biophysical studies have shown that t- and v-SNAREs can assemble in multiple stages from the N-term

35 vitro fusion assays using full-length t- and v-SNAREs embedded in liposomes, Gbetagamma inhibited Ca(

36 een target SNAREs and vesicle SNAREs (t- and v-SNAREs) are required for membrane fusion in intracellu

37 tion through direct contact with both t- and v-SNAREs.

38 The assembled v-SNARE/t-SNARE complex consists of a bundle of four hel

39 ure and concentration of membrane-associated v-SNARE molecules into synthetic COPII vesicles.

40 ing fluorescently labeled vesicle-associated v-SNARE (soluble N-ethylmaleimide-sensitive factor attac

41 Vesicle-associated v-SNARE and target membrane t-SNARE proteins are also in

42 The vesicle-associated v-SNARE engages with its partner t-SNAREs on the target

43 is needed to package the membrane-associated v-SNAREs and Emp24p than is needed to package the solubl

44 equires zippering between vesicle-associated v-SNAREs and target membrane t-SNAREs, but the mechanism

45 Fusion is catalyzed when vesicle-associated v-SNAREs form trans-SNARE complexes ("SNAREpins") with t

46 Association between vesicle-associated (v-) SNARE and target membrane (t-) SNARE results in the

47 Vesicle-associated (v-) SNARE associates with a target membrane (t-) SNARE t

48 Vesicle-associated (v-) SNARE intertwines with target membrane (t-) SNARE to

49 ane-attached (t-SNARE) and vesicle-attached (v-SNARE) proteins that zipper together to form a coiled-

50 The interaction between v-SNAREs on transport vesicles and t-SNAREs on target me

51 romiscuity characteristic of pairing between v-SNAREs and t-SNAREs extends to the formation of homo-o

52 karyotic cells relies on recognition between v-SNAREs on transport vesicles and t-SNAREs on target me

53 teractions require the participation of both v-SNAREs, indicating that, unlike post-Golgi membrane tr

54 eliminated by removal of either one or both v-SNAREs.

55 re holds vesicles at an active zone to bring v-SNAREs and t-SNAREs, the proteins that mediate vesicle

56 proteins that reside on vesicular carriers (v-SNARE) and target organelles (t-SNARE).

57 OG complex-dependent (CCD) vesicles carrying v-SNAREs GS15 and GS28 and cis-Golgi glycoprotein GPP130

58 identified a novel Saccharomyces cerevisiae v-SNARE (Vti1p) encoded by the essential gene, VTI1.

59 the interaction between Syn5 and the cognate v-SNARE Bet1 but increases its binding to p47, the adapt

60 to the membrane-proximal half of the cognate v-SNARE, and binds reversibly to the cognate region of t

61 neuronal t-SNARE that pairs with the cognate v-SNARE.

62 e the light chains, and whose unique cognate v-SNARE is Sft1.

63 isolated single flickering pores connecting v-SNARE-reconstituted nanodiscs to cells ectopically exp

64 erated from Golgi-enriched membranes contain v-SNAREs as well as Emp47p as cargo.

65 d for the packaging or the function of COPII v-SNAREs.

66 in/VAMP-3 has been proposed to be a critical v-SNARE for human platelet exocytosis; however, data rep

67 Furthermore, we demonstrate that efficient v-SNARE/t-SNARE interactions require the participation o

68 tg20, and retromer that retrieve an exocytic v-SNARE from the endocytic pathway to the Golgi.

69 We show that the ubiquitously expressed v-SNARE cellubrevin localizes to the basolateral membran

70 Multicopy plasmids expressing v-SNAREs Gos1p or Ykt6p, but not other v- and t-SNAREs,

71 Here we identify Vti1p as the first v-SNARE protein found to be required for biosynthetic tr

72 main predicted to increase accessibility for v-SNARE interaction.

73 COPII selects the free v-SNARE form of Bet1 because the LxxLE sequence is seque

74 for anchors of v- and t-SNAREs to function: v-SNAREs require anchors capable of spanning both leafle

75 ze the binding of GATE-16 to GOS-28, a Golgi v-SNARE, in a manner that requires ATP but not ATP hydro

76 ocytes, where it interacts with a post-Golgi v-SNARE protein, VAMP1, and acetylated microtubules.

77 e form of the endoplasmic reticulum to Golgi v-SNARE is a heteromeric complex.

78 rexpression of each of the known ER to Golgi v-SNAREs (Bet1p, Bos1p, Sec22p, and Ykt6p).

79 Here, two ER to Golgi v-SNAREs, Bet1p and Bos1p, were shown to interact specif

80 n of Cpx with the SNARE bundle that hindered v-SNARE unraveling by Cpx, thus compromising clamping.

81 To identify v-SNAREs in platelets, we used a polymerase chain reacti

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

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

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

85 SNARE that localizes to the ER, but no known v-SNAREs.

86 oteoliposomes reconstituted with full-length v-SNAREs (synaptobrevin) into planar lipid bilayers cont

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

88 erate primers to amplify potential VAMP-like v-SNAREs.

89 find that exocytosis mediated by the Longin v-SNARE TI-VAMP/VAMP7 is activated by tonic treatment wi

90 The molecular mechanism leading to Longin v-SNARE activation is largely unknown.

91 REs SNAP-23 and syntaxin 4 and the lysosomal v-SNARE TI-VAMP/VAMP7.

92 s lead us to propose that VAMP2 is the major v-SNARE involved in GLUT4 trafficking to the surface of

93 c Reticulum SNARE of 24 kD), a new mammalian v-SNARE implicated in vesicular transport between the ER

94 ylation and recycling of the plasma membrane v-SNARE Snc1.

95 Tlg1p also binds the plasma membrane v-SNARE Snc1p.

96 receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs).

97 incorporation of purified vesicle membrane (-v) SNARE and target membrane (t-) SNARE proteins into se

98 by SNAREs (located on the vesicle membrane [v-SNARE] and the target membrane [t-SNARE]).

99 of the membrane-proximal region of neuronal v-SNARE into the bilayer.

100 ing a domain that is related to the neuronal v-SNARE synaptobrevin.

101 small unilamellar vesicles bearing neuronal v-SNAREs fused with planar bilayers reconstituted with c

102 (c) Vacuoles with t-SNARE but no v-SNARE still require Sec17p/Sec18p priming, whereas the

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

104 A cDNA encoding a novel v-SNARE was isolated from a human megakaryocyte cDNA lib

105 TP binding protein), Vam3p (t-SNARE), Nyv1p (v-SNARE), and LMA1 (low Mr activity 1, a heterodimer of

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

107 ssociated with the t-SNARE in the absence of v-SNARE, but is not bound to the v-SNARE without t-SNARE

108 Exocyst disruption induces accumulation of v-SNARE-containing vesicles at the midbody ring.

109 Assembly of v-SNARE-t-SNARE targeting complexes is modulated by memb

110 gene are more defective for the packaging of v-SNARE molecules and Emp24p than they are for the packa

111 These data imply a ranked redundancy of v-SNARE usage in platelets and suggest that VAMP-8-/- mi

112 The Arabidopsis genome contains a family of v-SNAREs: VTI11, VTI12, and VTI13.

113 target membrane prior to the interaction of v-SNAREs and t-SNAREs across the membrane junction.

114 Likewise, a number of v-SNAREs (Ykt6p, Nyv1p, Vti1p) and homotypic fusion vacu

115 transmission, exploiting the large number of v-SNAREs available in synaptic vesicles.

116 e microsomes leads to increased packaging of v-SNAREs and Emp24p with no increase in the packaging of

117 or deleted and suggests that two species of v-SNAREs (VAMP and synaptotagmin) and two species of t-S

118 Es) and the delivery-vesicle SNARE VAMP2 (or v-SNARE) contain the "SNARE regions" that essentially me

119 Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly w

120 gests that the mere presence of a particular v-SNARE may not be sufficient to determine the preferred

121 t Golgi to fuse with each of the 7 potential v-SNAREs also present in this organelle.

122 We have tested all of the potential v-SNAREs encoded in the yeast genome for their capacity

123 protein/vesicle-associated membrane protein (v-SNARE), and the SNARE complexes could be specifically

124 SNAREs are integral membrane proteins (v-SNAREs on vesicles, t-SNAREs on the target organelles)

125 sicles that bear integral membrane proteins (v-SNAREs) which selectively interact with similar protei

126 We report the identification of a putative v-SNARE (GOS-28), localized primarily to transport vesic

127 that constitute the trimeric acceptor for R/v-SNAREs on Golgi-derived vesicles at the ER.

128 that the endosomal Q/t-SNARE Tlg2 and the R/v-SNAREs Sec22 and Ykt6 interact with Sso1-Sec9, and are

129 ensitive fusion protein attachment receptor (v-SNARE) Vesicle associated membrane protein (VAMP), but

130 fusion protein attachment protein receptor (v-SNARE) and target membrane SNARE to each of the three

131 aleimide factor attachment protein receptor (v-SNARE) called cellubrevin/vesicle-associated membrane

132 ted soluble NSF attachment protein receptor (v-SNARE) on transport vesicles with a SNARE on the targe

133 ensitive factor attachment protein receptor (v-SNARE) Sncp and the plasma membrane t-SNAREs Ssop and

134 SNARE) and vesicle-associated SNAP receptor (v-SNARE) proteins is a critical step for the docking of

135 Among the membrane-bound v-SNAP receptor (v-SNARE) proteins, Bos1p is required only for forward tr

136 Addition of purified recombinant v-SNARE to a t-SNARE-reconstituted lipid membrane increa

137 kt6p and perhaps Sft1p, acts as a retrograde v-SNARE capable of interacting with the cis-Golgi t-SNAR

138 riments showed that Mnn9p and the retrograde v-SNARE, Sec22p, were incorporated into COPI-coated vesi

139 lgi coat complex), Sec18p (NSF), and Sec22p (v-SNARE) for ER to Golgi transport.

140 ion events, we identify VAMP2 as a selective v-SNARE for GPCR delivery.

141 results identify VAMP2 as a cargo-selective v-SNARE and suggest that surface delivery of specific GP

142 Several v-SNAREs have a Longin N-terminal extension that, by pro

143 They also show that a single v-SNARE can be involved in both anterograde and retrogra

144 Therefore, a single v-SNARE can interact functionally with two different t-S

145 croscopy of labeled lipids to monitor single v-SNARE vesicle docking and fusion events on a planar li

146 e zippering of the vesicle-associated SNARE (v-SNARE) onto a binary SNARE complex on the target plasm

147 NARE assembly with vesicle-associated SNARE (v-SNARE).

148 logical function of the VAMP3 vesicle SNARE (v-SNARE) isoform in the regulation of GLUT4 vesicle traf

149 Vesicle SNARE (v-SNARE) proteins reconstituted into giant vesicles ( ap

150 obrevin/VAMP-8 is the primary vesicle-SNARE (v-SNARE) responsible for efficient release of dense and

151 pright orientation of the rod-shaped t-SNARE/v-SNARE complex from the membrane surface.

152 SNARE complexes (formed when vesicle SNAREs [v-SNAREs] and target membrane SNAREs [t-SNAREs] combine

153 The pairing of a stage-specific v-SNARE with its cognate t-SNARE may mediate the specifi

154 ne fusion through interactions with specific v-SNARE molecules on vesicle membranes, providing the in

155 c in eukaryotic cells requires that specific v-SNAREs on transport vesicles interact with specific t-

156 The neuron-specific synaptic v-SNARE n-syb (neuronal Synaptobrevin) plays a key role

157 , we generated four variants of the synaptic v-SNARE synaptobrevin-2 (syb2) anchored to the membrane

158 in opposing bilayers to allow appropriate t-/v-SNARE interactions leading to membrane fusion.

159 Approximately 11% smaller t-/v-SNARE ring complexes are generated using 50 nm cholest

160 not the alpha-helical contents within the t-/v-SNARE complex.

161 icles of secretory and of vesicle targeting (v-SNARE) proteins.

162 sed this assay to investigate how targeting [v-SNARE, vesicle-soluble NSF (N-ethylmaleimide-sensitive

163 the interaction of vesicle proteins, termed v-SNAREs, with target membrane proteins, termed t-SNAREs

164 on MOR-containing endosomes, suggesting that v-SNAREs are copackaged with specific cargo into separat

165 The v-SNARE Nyv1p forms a SNARE complex with Vam3p in homoty

166 The v-SNARE proteins Snc1p and Snc2p are required for fusion

167 The v-SNARE vesicles, labeled with lipid and content markers

168 The v-SNARE Vti1p is enriched at vertices by a distinct path

169 cluding the t-SNAREs Vam3p and Vam7p and the v-SNARE Nyv1p, are found in a multisubunit "cis" complex

170 in which the interaction between Cpx and the v-SNARE serves as a spring to prevent premature zipperin

171 reviously identified Syp1 cargo Mid2 and the v-SNARE Snc1.

172 nic Drosophila with mutations in Cpx and the v-SNARE that disrupted a salt bridge between these two p

173 tion between the Cpx accessory helix and the v-SNARE would enhance Cpx flexibility and thus promote s

174 Using a proteomics approach, the v-SNARE Vti1a (vps10p tail interacting 1a) was identifie

175 ns each functional aspect of priming, as the v-SNARE regulates the rate of Sec17p release and, in tur

176 d whereas many studies identify VAMP2 as the v-SNARE, others suggest that either VAMP3 or VAMP8 may a

177 n require regulated interactions between the v-SNARE, VAMP2, and the t-SNARE, syntaxin 4.

178 Both the v-SNARE and the t-SNARE are necessary for efficient dock

179 our helices, of which one is supplied by the v-SNARE and the other three by the t-SNARE.

180 omplex formation is tightly regulated by the v-SNARE-membrane interactions.

181 lar lipid vesicles (SUVs) that contained the v-SNARE Synaptobrevin2 and Syt1-R398/399Q also docked to

182 to large unilamellar vesicles containing the v-SNARE synaptobrevin 2, which were docked and fused wit

183 of small unilamellar vesicles containing the v-SNARE VAMP2 and the Ca(2+) sensor synaptotagmin 1.

184 exocyst that exposes a binding site for the v-SNARE.

185 Removal of phosphatidylserine from the v-SNARE vesicle has no effect on docking or fusion.

186 an be mediated by a peptide derived from the v-SNARE, which likely bypasses additional regulatory pro

187 nctional clues to the membrane fusion in the v-SNARE deleted fusion models.

188 e synthetically lethal with mutations in the v-SNARE genes SEC22 and BET1.

189 lamine (DOPE) for phosphatidylcholine in the v-SNARE vesicle with either 0 or 20% DOPE included in th

190 e element of this recognition process is the v-SNARE, VAMP-2, because tetanus toxin, which cleaves VA

191 moeboid-like invasive tumour cell lines, the v-SNARE, VAMP3, regulates delivery of microvesicle cargo

192 n localized to the basolateral membrane, the v-SNARE operative in the AP-1B pathway remained unknown.

193 (a) Antibodies to the t-SNARE, but not the v-SNARE, block Sec17p release.

194 creating the binding site for the CTD of the v-SNARE and enabling fusion.

195 Interestingly, the level of the v-SNARE Bet1L is also drastically reduced in both of the

196 First, the N-terminal domain (NTD) of the v-SNARE docks to the t-SNARE, which leads to a conformat

197 ere to and freely move on the surface of the v-SNARE giant vesicle.

198 and that no particular specialization of the v-SNARE is required to differentiate synaptic exocytosis

199 with the v-SNARE promotes unraveling of the v-SNARE off the core SNARE bundle.

200 suggests that the cytoplasmic domain of the v-SNARE protein Sec22p is required for its packaging int

201 f Apm1, increases cell surface levels of the v-SNARE Snc1.

202 on in the membrane insertion sequence of the v-SNARE synaptobrevin/vesicle-associated membrane protei

203 terol induces a conformational change of the v-SNARE transmembrane domain (TMD) from an open scissors

204 s from both bilayers, and in the case of the v-SNARE, from both leaflets.

205 can be rescued by the overexpression of the v-SNARE, Ykt6p, which physically interacts with Vti1p.

206 Sly1p, allowing subsequent formation of the v-SNARE-t-SNARE targeting complex.

207 like Ypt1p, is required for assembly of the v-SNARE/t-SNARE complex.

208 more pronounced when cholesterol was on the v-SNARE side than when it was on the t-SNARE side.

209 rmally present, vacuoles containing only the v-SNARE can fuse with those containing only the t-SNARE.

210 ing cholesterol in either the t-SNARE or the v-SNARE membrane favors a mechanism of direct fusion por

211 inception of Golgi reassembly to protect the v-SNARE and regulate SNARE function.

212 ntified a site on Sec24p that recognizes the v-SNARE Bet1p and show that packaging of a number of car

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

214 We now find that the v-SNARE tetanus toxin-insensitive vesicle-associated mem

215 Here, we show that the v-SNARE VAMP7 mediates fusion of melanosomes with tubula

216 ken together, these results suggest that the v-SNARE Vti1a may regulate a step common to both GLUT4 a

217 These data show that the v-SNARE, cellubrevin/VAMP-3 is not a requirement for the

218 Thus, the v-SNARE-membrane interaction may be a major molecular de

219 absence of v-SNARE, but is not bound to the v-SNARE without t-SNARE.

220 Fusion only occurs when the v-SNARE Bet1 is on one membrane and the syntaxin heavy c

221 similar set of genetic interactions with the v-SNARE genes, they exhibit a synthetic lethal interacti

222 demonstrated that Cpx's interaction with the v-SNARE promotes unraveling of the v-SNARE off the core

223 MoSso1, inhibiting its interaction with the v-SNARE protein MoSnc1.

224 d, once bound to Sso1p, can complex with the v-SNARE Snc2p.

225 le large unilamellar vesicles doped with the v-SNARE synaptobrevin 2 by means of spinning-disc confoc

226 They co-precipitate with the v-SNARE Vti1p, which is implicated in Golgi-endosome tra

227 E complex to initiate NTD zippering with the v-SNARE, a mechanism likely shared by the mammalian unco

228 y of two t-SNAREs, Sso1/2 and Sec9, with the v-SNARE, Snc1/2, on secretory vesicles.

229 RE complex and prevents its pairing with the v-SNARE, therefore arresting the fusion reaction at a pr

230 SNAREs, the t-SNAREs Vam3p and Vam7p and the v-SNAREs Nyv1p, Vti1p, and Ykt6p.

231 nstrate that double mutants lacking both the v-SNAREs synaptotagmin and snb-1 are phenotypically simi

232 We now identify the v-SNAREs Vti1p and Ykt6p by mass spectrometry as additio

233 containing bound cytoplasmic domains of the v-SNAREs, Sec22p or Bos1p, or of the ER resident protein

234 the addition of exogenous Sar1p, whereas the v-SNAREs and Emp24p are not efficiently packaged under t

235 that mediates fusion, specifically with the v-SNAREs Snc1p and Snc2p.

236 In control cells, these v-SNARE vesicles colocalize with a GFP-tagged secreted p

237 In cultured neurons, these v-SNARE mutations strongly inhibit spontaneous as well a

238 owing scorpion envenomation as both of these v-SNARE proteins are associated with zymogen granule mem

239 2, or rat cellubrevin failed to detect these v-SNAREs in human platelets, although membrane proteins

240 erentially with syntaxin 4, implicating this v-SNARE in basolateral fusion events.

241 Thus, v-SNARE TMDs and phospholipids cooperate in supporting m

242 een suggested that Sec17p and Sec18p bind to v-SNARE/t-SNARE complexes and mediate the membrane fusio

243 atory effect was topologically restricted to v-SNARE vesicles (containing VAMP 2) and only occurred i

244 smic reticulum and Golgi complex employs two v-SNAREs, Bos1p and Sec22p, each containing a domain tha

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

246 for vesicle-associated membrane protein type v-SNARE proteins (or synaptobrevins) reveals characteris

247 ed the dilation of single fusion pores using v-SNARE-reconstituted 23-nm-diameter discoidal nanolipop

248 ial negative regulators of Pmc1p, a vacuolar v-SNARE protein, Nyv1p, was recovered.

249 Even in the absence of the vacuolar v-SNARE Nyv1p, a subcomplex which includes Vam7p and the

250 erlapped with vesicles visualized by VAMP721 v-SNARE, but the majority of the foci represent sites wi

251 plasma membrane t-SNARE) and VAMP (a vesicle v-SNARE) to form a core protein complex thought to be an

252 ein to replace Sncp as the secretory vesicle v-SNARE.

253 sma membrane t-SNARE complex and the vesicle v-SNARE or VAMP.

254 AREs syntaxin 1A and SNAP-25 and the vesicle v-SNARE synaptobrevin, mediates the fusion of 2 membrane

255 The pairing of vesicle v-SNAREs (soluble N-ethylmaleimide-sensitive factor atta

256 mbrane, which then zippers with the vesicle (v)-SNARE on the vesicle to drive membrane fusion.

257 uld we find any involvement for the vesicle (v)-SNARE VAMP4, which is known to be associated with syn

258 axin 17 (STX17) and SNAP29, and the vesicle (v)-SNARE VAMP8 (vesicle-associated membrane protein 8).

259 sts that pairs of proteins known as vesicle (v-) SNAREs and target membrane (t-) SNAREs interact spec

260 complex must be located on both the vesicle (v-SNARE) and the target membrane (t-SNARE).

261 family of membrane proteins in the vesicle (v-SNAREs) and a heterodimeric complex of syntaxin and SN

262 ) that reside on the surface of the vesicle (v-SNAREs) and target membrane (t-SNAREs).

263 fic interaction and fusion between vesicles (v-SNAREs) and their target membranes (t-SNAREs).

264 ral membrane proteins on transport vesicles (v-SNAREs) and target organelles (t-SNAREs) that bind to

265 and [Pep12p/Tlg1p,Vti1p] with the vesicular (v)-SNARE Snc2p promotes endocytic fusion.

266 f SNARE complexes composed of the vesicular (v)-SNARE synaptobrevin and the target (t)-SNAREs Snap-25

267 t (t)-SNAREs and one (R) from the vesicular (v)-SNARE.

268 ructures, where it physically interacts with v-SNARE GS15.

269 s are comparable in the two assays (one with v-SNARE vesicles tethered to a surface and the other wit

270 les tethered to a surface and the other with v-SNARE vesicles free in solution).

271 priming, whereas their fusion partners with v-SNARE but no t-SNARE do not.

272 The budding yeast v-SNARE, Snc1, mediates fusion of exocytic vesicles to t

273 at none of the coiled-coil residues of yeast v-SNARE is buried in the hydrophobic layer of the membra

274 I1b, two Arabidopsis homologues of the yeast v-SNARE Vti1p, which is required for multiple transport