ライフサイエンスコーパス: t-SNARE

1 C2D-F domains interact with the syntaxin-1 t-SNARE motif with maximum binding within the range of 2

2 mmunoprecipitation studies showed that the 2 t-SNAREs syntaxin 2 and SNAP-23 do form a complex in viv

3 to bind membrane-embedded syntaxin-SNAP-25 (t-SNARE) complexes.

4 sma membrane SNAREs syntaxin 1A and SNAP-25 (t-SNAREs) and the delivery-vesicle SNARE VAMP2 (or v-SNA

5 s with native UT-A1, SNAP23, and syntaxin-4 (t-SNARE partners), indicating that UT-A1 participates wi

6 Although VAMP-8 (v-SNARE) and SNAP-23 (a t-SNARE class) are important for platelet secretion, the

7 ntaining vesicles and binds to syntaxin 4, a t-SNARE protein that regulates fusion of transport vesic

8 sion, consistent with Gos28 functioning as a t-SNARE for Rh1 transport.

9 ified SYNTAXIN OF PLANTS 13II (SYP13II) as a t-SNARE that is essential for the formation of a stable

10 nstrating that syntaxin 3B can function as a t-SNARE.

11 nclude that CFTR channels are regulated by a t-SNARE complex that may tune CFTR activity to rates of

12 ecificity in the choice of light chains by a t-SNARE, we undertook a comprehensive examination of the

13 netic interaction with SLY1, which encodes a t-SNARE-interacting protein that functions in endoplasmi

14 was one of three regions predicted to form a t-SNARE binding site in VPS33B.

15 Syntaxin-1A is a t-SNARE that is involved in vesicle docking and vesicle

16 function either as a v-SNARE or as part of a t-SNARE complex.

17 licing of SYP13II allows plants to replace a t-SNARE involved in traffic to the plasma membrane with

18 ddition of purified recombinant v-SNARE to a t-SNARE-reconstituted lipid membrane increased only the

19 ved in traffic to the plasma membrane with a t-SNARE that is more stringent in its localization to fu

20 P-2)-containing proteoliposomes and acceptor t-SNARE complex-containing planar supported bilayers was

21 ative, and binding to the prefusion acceptor t-SNARE complex is stronger than to the postfusion core

22 ect of complexin beginning with the acceptor t-SNARE complex and the subsequent activation of the cla

23 er two helices are contributed by additional t-SNARE light chains.

24 dly reduced the attachment between syt-1 and t-SNARE-carrying vesicles in the absence of phosphatidyl

25 We also found that overexpression of Lgl and t-SNARE proteins not only improves exocytosis but also r

26 ing and membrane fusion by regulating v- and t-SNARE interactions.

27 quent Ca(2+)-triggered fusion between v- and t-SNARE liposomes.

28 These data show that elevated v- and t-SNARE protein levels are associated with insulin resis

29 TMD modifications designed to disrupt v- and t-SNARE TMD zippering prolonged pore lifetimes dramatica

30 We found that interactions between v- and t-SNARE transmembrane domains (TMDs) promote, but are no

31 Ba2+, we found that binding of syt to PS and t-SNAREs can be dissociated from activation of fusion, u

32 ind 1,2-dioleoyl phosphatidylserine (PS) and t-SNAREs in a Ca(2+)-promoted manner with their abilitie

33 ane prior to the interaction of v-SNAREs and t-SNAREs across the membrane junction.

34 aracteristic of pairing between v-SNAREs and t-SNAREs extends to the formation of homo-oligomeric t-S

35 cles at an active zone to bring v-SNAREs and t-SNAREs, the proteins that mediate vesicle fusion, with

36 ry to maintain a supply of uncombined v- and t-SNAREs for fusion in cells.

37 expressing the interacting domains of v- and t-SNAREs on the cell surface were found to fuse spontane

38 distinct requirements for anchors of v- and t-SNAREs to function: v-SNAREs require anchors capable o

39 ce spectrum was observed when cognate v- and t-SNAREs were present in the opposite bilayers.

40 -SNAREs Gos1p or Ykt6p, but not other v- and t-SNAREs, partially suppressed phenotypes of ric1Delta a

41 with the interaction between opposing v- and t-SNAREs, prevented such facilitation.

42 ith the vesicle and target membranes (v- and t-SNAREs, respectively).

43 identity of the functional syntaxin (another t-SNARE class) has been controversial.

44 xin1a NRD and H3 domain within the assembled t-SNARE complex, positioning them for productive VAMP2 b

45 or) liposomes and target-membrane-associated t-SNARE-reconstituted planar, supported bilayers (t-SBLs

46 "SNAREpins") with target membrane-associated t-SNAREs, a zippering-like process releasing approximate

47 ein machinery composed of membrane-attached (t-SNARE) and vesicle-attached (v-SNARE) proteins that zi

48 ly by competing for binding on the available t-SNAREs, blocks recovery from the acyl-CoA inhibition.

49 ination of the capacity of all 21 Sed5-based t-SNAREs that theoretically could assemble in the yeast

50 the Sed5/Bos1/Sec22 t-SNARE complex because t-SNARE assembly removes autoinhibitory contacts to expo

51 ion assays that monitor lipid mixing between t-SNARE and v-SNARE vesicles in bulk solution exhibit re

52 The subtle bidirectional t-SNARE conformational switch was mediated by the ionic

53 ATG14 directly binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP

54 main, and stabilizes the STX17-SNAP29 binary t-SNARE complex on autophagosomes.

55 ex, with no detectable binding to the binary t-SNARE complex or any of the three individual SNAREs in

56 into planar lipid bilayers containing binary t-SNAREs (anchored syntaxin associated with SNAP25) was

57 motes the formation of an Sso2-Sec9 'binary' t-SNARE complex, the early rate-limiting step in SNARE c

58 ber of the Sec1 family of proteins that bind t-SNAREs.

59 amate, but not phenylalanine, activates both t-SNARE binding and exocytosis.

60 is independent of the t-SNAREs, whereas both t-SNAREs will localize to vertices when trans-pairing of

61 Ca2+/membrane-binding loops, decreases C2AB t-SNARE binding and Ca2+-triggered fusion in vitro witho

62 precludes GOS-28 from binding to its cognate t-SNARE, syntaxin-5.

63 ls are coordinately regulated by two cognate t-SNAREs, SNAP-23 (synaptosome-associated protein of 23

64 gamma binds to both ternary SNARE complexes, t-SNARE heterodimers, and monomeric SNAREs, competing wi

65 events on a planar lipid bilayer containing t-SNAREs.

66 AFM, and immunochemical studies demonstrated t-SNAREs to localize at the base of the fusion pore.

67 cium-mediated stabilization of the C2 domain.t-SNARE complex.

68 ere, we show that Gtaxin (GTX), a Drosophila t-SNARE (target-soluble N-ethylmaleimide-sensitive facto

69 ggest that the NRD is required for efficient t-SNARE complex formation and does not recruit necessary

70 a interacts specifically with lipid-embedded t-SNAREs consisting of full-length syntaxin 1 and SNAP-2

71 in, which interacts with the early endosomal t-SNARE syntaxin-13.

72 raffic, are ER-localized, and bind to the ER t-SNARE Ufe1p.

73 In all cases examined, t-SNARE function is provided as a three-helix bundle com

74 ls ectopically expressing cognate, "flipped" t-SNAREs.

75 ls ectopically expressing cognate, 'flipped' t-SNAREs.

76 hains, Tlg1p and Vti1p, to form a functional t-SNARE that mediates fusion, specifically with the v-SN

77 other membrane where they form a functional t-SNARE.

78 rane increased only the size of the globular t-SNARE oligomer without influencing the electrical prop

79 vesicle tethering protein Uso1 and the Golgi t-SNARE Sed5.

80 re we report the identification of the Golgi t-SNARE syntaxin 5 (Syn5) as the ubiquitinated substrate

81 lipoprotein structure, the base of which has t-SNAREs and allows for docking and release of secretory

82 SNAP-23 appear to make up the heterodimeric t-SNAREs required for lysosome exocytosis.

83 gether with protein localization to identify t-SNAREs that are present on the host-microbe interface

84 What replaces SNAP-25 in t-SNAREs of intracellular membranes?

85 Individual t-SNAREs (e.g., syntaxin 1A) also regulate synaptic calc

86 the regulation of ion channels by individual t-SNAREs is related to SNARE complex assembly and membra

87 Here we show that an intracellular t-SNARE is built from a 'heavy chain' homologous to synt

88 Complexes between Nyv1p and its t-SNARE partner Vam3p were also isolated, but these comp

89 o Munc13-1, CAPS1 binds to syntaxin-1, a key t-SNARE protein in neurosecretion.

90 syntaxin 6, a Golgi- and endosome-localized t-SNARE, and that it does so by regulating the post-Golg

91 Locking t-SNAREs creates the potential for spatial and temporal

92 On low t-SNARE-density bilayers at 37 degrees C, docking is eff

93 ells contain two homologues of the mammalian t-SNARE protein SNAP-25, encoded by the SEC9 and SPO20 g

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

95 w complexin binds to the 1:1 plasma membrane t-SNARE complex of syntaxin-1a and SNAP-25 while simulta

96 dimer of Sec6p binds to the plasma membrane t-SNARE Sec9p and inhibits the interaction between Sec9p

97 microdomains enriched in the plasma membrane t-SNARE syntaxin 4 (Stx4), and disruption of Stx4 impair

98 novel apical and basolateral plasma membrane t-SNARE.

99 in cell lysates between the plasma membrane t-SNAREs SNAP-23 and syntaxin 4 and the lysosomal v-SNAR

100 eptor (v-SNARE) Sncp and the plasma membrane t-SNAREs Ssop and Sec9p into a SNARE complex.

101 ARE complex, composed of the plasma membrane t-SNAREs syntaxin 1A and SNAP-25 and the vesicle v-SNARE

102 ment protein receptors) with target membrane t-SNAREs has a central role in intracellular membrane fu

103 icle-associated v-SNAREs and target membrane t-SNAREs, but the mechanisms governing the subsequent po

104 f exocytic vesicle (v)- and target membrane (t)-SNAREs (soluble N-ethylmaleimide-sensitive fusion pro

105 logy of the TMD of Sso1p, a target membrane (t-) SNARE involved in the trafficking from Golgi to plas

106 cle membrane (-v) SNARE and target membrane (t-) SNARE proteins into separate liposome populations.

107 e-associated (v-) SNARE and target membrane (t-) SNARE results in the coiled coil core that bridges t

108 (v-) SNARE intertwines with target membrane (t-) SNARE to form a coiled coil that bridges two membran

109 v-) SNARE associates with a target membrane (t-) SNARE to form a SNARE complex bridging two membranes

110 as vesicle (v-) SNAREs and target membrane (t-) SNAREs interact specifically to control and mediate

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

112 tor of accessibility of the target membrane (t-SNARE) protein syntaxin 4 to participate in SNARE core

113 e vesicle (v-SNARE) and the target membrane (t-SNARE).

114 membrane (v-SNAREs) and the target membrane (t-SNAREs).

115 membrane [v-SNARE] and the target membrane [t-SNARE]).

116 ated SNAREs with SNAREs on target membranes (t-SNAREs).

117 gnificantly reduced affinity of this mutated t-SNARE for Gbetagamma, but it still interacted with syn

118 dominant activator of the cis-Golgi network t-SNARE Sed5p, also functioned as a multicopy suppressor

119 Here we show that the neural t-SNARE (target-membrane-associated-soluble N-ethylmalei

120 N-terminal conserved domain of the neuronal t-SNARE syntaxin-1A was determined to a resolution of 1.

121 inherent to the coil domains of the neuronal t-SNARE that pairs with the cognate v-SNARE.

122 that Kin1 and Kin2 induce phosphorylation of t-SNARE Sec9 in vivo and stimulate its release from the

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

124 orms the initial vertex ring, independent of t-SNAREs or actin; (b) F-actin disassembly and GTP-bound

125 synaptogenesis, within 1-4 DIV upon loss of t-SNAREs (syntaxin-1, SNAP-25) or Munc18-1, but not v-SN

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

127 extends to the formation of homo-oligomeric t-SNARE complexes as well.

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

129 receptors (SNAREs), but despite consensus on t-SNAREs usage, it is unclear which Vesicle Associated M

130 Sed5 could potentially combine to form other t-SNAREs.

131 he interaction between Sec9p and its partner t-SNARE Sso1p.

132 -associated v-SNARE engages with its partner t-SNAREs on the target membrane to form a coiled coil th

133 mbers of the endosomal SNARE complex, PEP12 (t-SNARE) and PEP7 (homologue of mammalian EEA1); Pep3p a

134 different color, dock and fuse with a planar t-SNARE bilayer supported on glass.

135 of syntaxin 4 with SNAP-23, another platelet t-SNARE.

136 characterize one candidate, the postsynaptic t-SNARE Syntaxin 4 (Syx4).

137 unilamellar vesicles containing preassembled t-SNARE proteins (syntaxin 1.SNAP-25), we determined how

138 ectly and functionally with the preassembled t-SNARE complex.

139 ct with, or colocalize with, the prevacuolar t-SNARE AtPEP12.

140 mplement of SNAREs required in this process, t-SNAREs BNIP1 and USE1, and v-SNARE YKT6.

141 uolar compartment (PVC) and requires the PVC t-SNARE Pep12p.

142 Additionally, we found that the endosomal Q/t-SNARE Tlg2 and the R/v-SNAREs Sec22 and Ykt6 interact

143 1p complex." The complex also includes the Q/t-SNARE proteins, Use1p, Sec20p, and Ufe1p, integral mem

144 e evidence for the involvement of exocytic Q/t-SNAREs in autophagosome formation, acting in the recru

145 ensitive factor attachment protein receptor (t-SNARE) complex in mammals and the first mammalian muta

146 -ethylmaleimide attachment protein receptor (t-SNARE) involved in membrane fusion events along the se

147 ane soluble NSF attachment protein receptor (t-SNARE) isoforms.

148 -ethylmaleimide attachment protein receptor (t-SNARE) protein, interferes with VEGFR2 trafficking to

149 h the general target membrane SNAP receptor (t-SNARE) protein SNAP-23 appear to make up the heterodim

150 nsitive factor-attachment protein receptors (t-SNAREs) that are dedicated to symbiosis and used cell-

151 f the SNARE complex assembled by recombinant t-SNARE Sso1p/Sec9 and v-SNARE Snc2p, which are involved

152 A large fraction (~75%) of the reconstituted t-SNARE was laterally mobile with a lateral diffusion co

153 Reconstituted t-SNAREs in supported bilayers bound soluble green fluor

154 in (GFP-VAMP) was bound to the reconstituted t-SNAREs.

155 that there was insufficient time to recruit t-SNAREs to the fusion site, consistent with t-SNAREs be

156 COPII favors Sed5 within the Sed5/Bos1/Sec22 t-SNARE complex because t-SNARE assembly removes autoinh

157 ing an upright orientation of the rod-shaped t-SNARE/v-SNARE complex from the membrane surface.

158 rd this goal, recombinant syntaxin1A/SNAP25 (t-SNARE) was reconstituted into polymer-supported planar

159 integral membrane protein syntaxin1A/SNAP25 (t-SNARE) was reconstituted into tethered polymer-support

160 fusion by binding the target membrane SNARE (t-SNARE) complex and preventing the initiation of ternar

161 ing of otoferlin C2 domains to target SNARE (t-SNARE) proteins and phospholipids.

162 s that selectively inhibit syt.target-SNARE (t-SNARE) interactions reduced syt stimulation of fusion.

163 The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, of

164 ely 100 nm) carrying target membrane SNAREs (t-SNAREs) both adhere to and freely move on the surface

165 Target plasma membrane SNAREs (t-SNAREs) syntaxin 1A and SNAP-25 form the t-SNARE compl

166 NAREs [v-SNAREs] and target membrane SNAREs [t-SNAREs] combine in the same membrane) are disrupted by

167 raction between the H+-ATPase and a specific t-SNARE.

168 a clearly show that SNAPs, NSF, and specific t-SNAREs are used for dense core granule release; these

169 on involving exocyst components and the Sso1 t-SNARE.

170 force spectroscopy, we modeled the synaptic t-SNARE complex as a parallel three-helix bundle with a

171 tagmin 1 complex also contained the synaptic t-SNARE proteins, syntaxin 1 and SNAP-25, suggesting tha

172 Uniquely, 2 syntaxin t-SNAREs, syntaxin 2 and 4, which localize to granules a

173 These proteins chaperone syntaxin t-SNAREs and are required for exocytosis.

174 n, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of

175 as acceptor membranes, which suggests that t-t-SNARE interactions, either direct or indirect, may be

176 We determined the organization of target (t) SNARE proteins on the basolateral endothelial plasma

177 Vesicular (v)- and target (t)-SNARE proteins assemble in SNARE complex to mediate m

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

179 ARE complexes containing yeast Golgi target (t)-SNARE Sed5p.

180 e could not find evidence that these target (t)-SNARE molecules are involved in homotypic ISG fusion.

181 Vesicular (v)- and target (t)-SNAREs play essential roles in intracellular membrane

182 s, three (Q(a), Q(b), and Q(c)) from target (t)-SNAREs and one (R) from the vesicular (v)-SNARE.

183 oteoliposomes reconstituted with the target (t)-SNAREs (soluble N-ethylmaleimide-sensitive factor att

184 In yeast, the assembly of the target (t)-SNAREs [Tlg2p/Tlg1p,Vti1p] and [Pep12p/Tlg1p,Vti1p] w

185 These findings demonstrate that t-SNARE clusters in the endothelial target PM serve as t

186 Immunochemical studies demonstrated that t-SNAREs, NSF, actin, vimentin, alpha-fodrin and the cal

187 The t-SNARE complex consists of Syntaxin4 and SNAP23, and wh

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

189 The t-SNARE in a late Golgi compartment (Tlg2p) syntaxin is

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

191 Although the t-SNARE syntaxin 4 has been localized to the basolateral

192 Both the v-SNARE and the t-SNARE are necessary for efficient docking and fast fus

193 Membrane topologies of syntaxin 1A and the t-SNARE complex were investigated using site-directed sp

194 eraction between the exocyst complex and the t-SNARE implicates the exocyst in SNARE complex regulati

195 ternary complex of Sec4-GTP, Sro7p, and the t-SNARE Sec9p.

196 the interaction between Vps52/53/54 and the t-SNARE Tlg1p.

197 n intermediate between the chaperone and the t-SNARE.

198 They are the t-SNARE SNAP-25 and the GTPase dynamin 1, which are nece

199 ed the respective interaction domains as the t-SNARE region of Stx5 and amino acids 5 to 72 of PC2.

200 membrane insertion leaves no gap between the t-SNARE core and the membrane.

201 The C2F domain directly binds the t-SNARE SNAP-25 maximally at 100 muM and with reduction

202 t occupancy of the N terminus of Sro7 by the t-SNARE Sec9, which results in the open conformation of

203 ed by the v-SNARE and the other three by the t-SNARE.

204 Ypt7p, its HOPS/Vps-C effector complex, the t-SNARE Vam3p, and protein phosphatase 1) accumulate at

205 on synapses in the retina do not contain the t-SNARE (target-soluble N-ethylmaleimide-sensitive facto

206 of endogenous Golgi SNAREpins containing the t-SNARE, syntaxin 5.

207 In contrast, the t-SNARE Vam3p was a necessary vacuolar component.

208 ed that increasing cholesterol in either the t-SNARE or the v-SNARE membrane favors a mechanism of di

209 ld provide the flexibility necessary for the t-SNARE core.

210 vious reports have implicated a role for the t-SNARE protein, syntaxin 1A (S1A), in the regulation of

211 3B had a much lower binding affinity for the t-SNARE SNAP25 compared with syntaxin 1A.

212 (t-SNAREs) syntaxin 1A and SNAP-25 form the t-SNARE complex that serves as an intermediate toward fi

213 wo light chains (Bos1 and Sec22) to form the t-SNARE needed to receive vesicles from the endoplasmic

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

215 However, the t-SNARE complex readily misfolds, and its structure, sta

216 lin secretory dysfunction, we identified the t-SNARE protein Syntaxin 4 as a target of modification b

217 nt, which has a single-point mutation in the t-SNARE and displays enhanced spontaneous release.

218 le with either 0 or 20% DOPE included in the t-SNARE bilayer gives rise to hemifusion events.

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

220 ts with helix C of the Syntaxin1a NRD in the t-SNARE complex.

221 is provided by a syntaxin family member (the t-SNARE heavy chain), and the other two helices are cont

222 In neurons, the t-SNARE SNAP-25 is essential for synaptic vesicle fusion

223 coil in the membrane-proximal domain of the t-SNARE and accelerates fusion, implying that the intrin

224 ated in the membrane-proximal portion of the t-SNARE and controls the rate at which the helical bundl

225 ed lipids reduced the mobile fraction of the t-SNARE and the lipids themselves.

226 The structure of the t-SNARE complex appears to be virtually identical to tha

227 In addition, the specific activity of the t-SNARE complex is significantly influenced by expressio

228 The newly refined structure of the t-SNARE complex provides a basis for the better understa

229 ex locks the C-terminal (CTD) portion of the t-SNARE into the same structure as in the postfusion 4-h

230 in activity-dependent redistribution of the t-SNARE proteins, SYNTAXIN and SNAP-25, away from neurot

231 Replacement of the t-SNARE SNAP25b with yeast Sec9c had little effect, sugg

232 Mutation of the central glutamine of the t-SNARE Sso1 impaired sporulation, but does not affect v

233 , fusion is dependent on SNAP-25, one of the t-SNARE subunits that is required for fusion in vivo.

234 n this study we identified expression of the t-SNARE syntaxin 8 (STX8) (Qc SNARE) in mouse and human

235 c18-binding residue on the N terminus of the t-SNARE syntaxin uncouples Munc18-stimulated vesicle adh

236 in to the conserved N-terminal domain of the t-SNARE therefore provides a crucial link between compon

237 switch is "off" (the intrinsic state of the t-SNARE), zippering of the helices from their membrane-d

238 inds reversibly to the cognate region of the t-SNARE.

239 ect fusion, although it has an effect on the t-SNARE complex, depending on the presence of other fact

240 on the v-SNARE side than when it was on the t-SNARE side.

241 unc18-1 protein and its binding partner, the t-SNARE-protein Syntaxin-1, by approximately 30% and dec

242 Tomosyn recognizes the t-SNARE complex and prevents its pairing with the v-SNAR

243 erature-, and ATP-dependent and requires the t-SNARE Pep12p.

244 to the previous reports, suggesting that the t-SNARE complex has the disordered midsection and the un

245 ted and biochemical findings showed that the t-SNARE proteins present in endothelial cells (SNAP-23 a

246 Thus, the t-SNARE complex acted as a switch to enable fast and con

247 Recombinant Sec1p binds strongly to the t-SNARE complex (Sso1p/Sec9c) as well as to the fully as

248 function is known to involve binding to the t-SNARE Syntaxin 4, a paucity of Munc18c-binding protein

249 a membrane by permitting their access to the t-SNARE syntaxin 4.

250 yeast and mammalian cells by binding to the t-SNARE Syntaxin5a/Sed5p and enhancing the stability of

251 nal domain (NTD) of the v-SNARE docks to the t-SNARE, which leads to a conformational rearrangement i

252 e only observe optimal lipid mixing when the t-SNARE proteins are coexpressed before purification.

253 M, 50% of the caveolae co-localized with the t-SNARE clusters, indicating that these caveolae were at

254 ring exocytosis, directly interacts with the t-SNARE protein Sso2.

255 t Kin1 and Kin2 physically interact with the t-SNARE Sec9 and the Lgl homologue Sro7, proteins acting

256 n in exocytosis through interaction with the t-SNARE Sec9.

257 interactions of the Syt1-C2B domain with the t-SNARE SNAP25/Syntaxin1 complex and/or plasma membrane

258 Along with the t-SNARE Syntaxin 18, we now reveal the complete compleme

259 nhibits its biochemical interaction with the t-SNARE syntaxin-1 in a closed conformation caused prema

260 herin-containing transport vesicles with the t-SNARE targeting complex.

261 thrin-coated vesicles and interacts with the t-SNARE, Syntaxin3.

262 has minimal contact with SNAP25b within the t-SNARE complex.

263 roximately 50% when the vesicles bearing the t-SNAREs syntaxin-1A and SNAP-25 were preincubated with

264 ocalization of other fusion factors; (c) The t-SNAREs Vam3p and Vam7p regulate each other's vertex en

265 red for SNARE vertex enrichment; and (d) The t-SNAREs regulate the vertex enrichment of both G-actin

266 of the plasma membrane fusion machinery, the t-SNAREs syntaxin 2, 3, and 4 and SNAP-23, are different

267 distinct pathway that is independent of the t-SNAREs, whereas both t-SNAREs will localize to vertice

268 r sialyl transferase (ST)-mRFP, nor with the t-SNAREs Memb11, SYP31 and BS14a.

269 We investigated the role of these t-SNAREs during the formation of a host-microbe interfac

270 been able to assign roles for some of these t-SNAREs in dense core granule release.

271 Surprisingly, all of these t-SNAREs redistribute to intracellular locations when Ma

272 mation and Ca(2+) channel regulation by this t-SNARE.

273 -23 antibody that blocks the binding of this t-SNARE to the CFTR amino-terminal tail.

274 In vitro, this t-SNARE is inert, locked in a nonfunctional state, unles

275 resented by the combined effect of the three t-SNARE N-terminal regions and the second is located wit

276 (STX7), STX8, and vesicle transport through t-SNARE homolog 1B (Vti1b)], leading to the assembly of

277 ptobrevin2 and Syt1-R398/399Q also docked to t-SNARE-containing giant vesicles (GUVs), similar to Syt

278 aining VAMP 2) and only occurred in trans to t-SNARE vesicles (containing syntaxin 1A and SNAP-25).

279 Many SNARE complexes contain two t-SNAREs that form a heterodimer, a putative intermediat

280 hereby revealed a previously uncharacterized t-SNARE in which Sed5 is the heavy chain and Gos1 and Yk

281 struction of a cognate GOS-28-syntaxin-5 (v-/t-SNARE) complex by first linking the SNAREs to promote

282 questered in the four-helix bundle of the v-/t-SNARE complex.

283 uoles; and fusion, mediated by calmodulin/V0/t-SNARE interactions.

284 The Vam7p t-SNARE is an essential component of the vacuole fusion

285 ne syntaxin, Sso1p, can be circumvented when t-SNARE complex formation is made intramolecular.

286 However when t-SNARE vesicles were added to a v-SNARE membrane, SNARE

287 However, when t-SNAREs were reconstituted into the proteoliposome and

288 s capable of spanning both leaflets, whereas t-SNAREs do not, so long as the anchor is sufficiently h

289 ting the interaction of synaptotagmin 1 with t-SNARE proteins.

290 x was decreased when UT-A1 was combined with t-SNARE components syntaxin-4 and SNAP23.

291 t-SNAREs to the fusion site, consistent with t-SNAREs being preclustered by cholesterol into function

292 le fusion reactions through interaction with t-SNAREs (target soluble N-ethylmaleimide-sensitive fact

293 n via their Ca2+-regulated interactions with t-SNAREs and PIP2, target molecules known to play critic

294 C2A and C2B interactions with t-SNAREs were insensitive to calcium.

295 as well as active zones, and interacts with t-SNAREs.

296 apacity to trigger fusion by partnering with t-SNAREs that mark the Golgi, the vacuole and the plasma

297 patitis C virus NS5B polymerase or the yeast t-SNARE Ufe1p.

298 with the ability to interact with the yeast t-SNARE.

299 Finally, we also show that none of the yeast t-SNAREs are located at the preautophagosomal structure,

300 t a role for NSF in replenishing active zone t-SNAREs for subsequent vesicle priming, and provide new