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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

137 1p complex." The complex also includes the Q/t-SNARE proteins, Use1p, Sec20p, and Ufe1p, integral mem

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

163 SNAP-25 linker: First, linker motifs support t-SNARE interactions and accelerate ternary complex asse

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

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

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

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

168 NO1 can be rescued by increasing SYP41-SYP61 t-SNARE complex formation, implicating TNO1 as a tetheri

169 quired for correct localization of the SYP61 t-SNARE.

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

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

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

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

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

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

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

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

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

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

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

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

182 tethering factor that interacts with the TGN t-SNARE SYP41 and is required for correct localization o

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

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

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

186 The t-SNARE acceptor complex DeltaN49 was reconstituted into

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

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

205 fused with lipid-labeled PSMs containing the t-SNARE acceptor complex DeltaN49 prepared on gold-coate

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

274 -23 antibody that blocks the binding of this t-SNARE to the CFTR amino-terminal tail.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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