ライフサイエンスコーパス: syntaxin 1

1 F4/80, choline acetyltransferase (ChAT), and syntaxin 1.

2 finger protein, Staring, that interacts with syntaxin 1.

3 tion and proteasome-dependent degradation of syntaxin 1.

4 II-mediated phosphorylation on serine-14 of syntaxin 1.

5 he Mint.Munc18-1 complex in conjunction with syntaxin 1.

6 re greatly enriched, instead, in SNAP-25 and syntaxin 1.

7 l 69 residues are crucial for the binding to syntaxin-1.

8 unc18-1 binding to the N-terminal peptide of syntaxin-1.

9 corresponding C-terminal region can bind to syntaxin-1.

10 binds to the first 80 N-terminal residues of syntaxin-1.

11 brevin and the target (t)-SNAREs Snap-25 and syntaxin-1.

12 s a more than 10-fold excess of SNAP-25 over syntaxin-1.

13 ve the same cavity of Munc18-1 that binds to syntaxin-1.

14 roteins can co-reside on membrane-integrated syntaxin-1.

15 1 binding to SNARE complexes containing open syntaxin-1.

16 ation and to SNARE complexes containing open syntaxin-1.

17 eptin 5 by Cdk5/p35 decreases its binding to syntaxin-1.

18 attachment protein receptor (SNARE) protein Syntaxin-1.

19 htly to assembled SNARE complexes containing syntaxin-1.

20 e kinesin family member 5B (KIF5B) motor and syntaxin-1.

21 ts SNARE complex formation by absorbing free syntaxin-1.

22 synapses via lateral diffusion together with syntaxin-1.

23 Syntaxin 1, 3, and 5 could not be detected.

24 Syntaxins 1-4 are localized to the plasma membrane, and

25 and 18c) bind to the closed conformation of syntaxins 1-4, which requires the N-terminal H(abc) doma

26 Most taste cells expressing syntaxin-1 (82%) also expressed the A blood group antige

27 GSIS, and we have identified SUMOylation of syntaxin 1 A as a potential component of this brake.

28 of a core synaptic fusion complex containing syntaxin-1 A, synaptobrevin-II and SNAP-25B.

29 on the membrane of a vesicular carrier, and syntaxin 1, a SNARE on the target membrane, as well as t

30 Recently, it was shown that PI(4,5)P2and syntaxin 1, a SNARE protein that catalyzes regulated exo

31 Syntaxin-1, a core protein of the soluble N-ethylmaleimi

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

33 amino terminus of Abi-1 that interacts with Syntaxin-1, a SNARE family member.

34 We observed that endogenous syntaxin-1 accumulates at the Golgi of Munc18-1 KO neuro

35 c-18 mutants, UNC-64 (Caenorhabditis elegans Syntaxin-1) accumulates in neuronal cell bodies.

36 ontaneous release, whereas other SNAP-25 and syntaxin-1 acidic residues at the other face mediate pri

37 attachment protein receptor (SNARE) protein syntaxin-1 adopts a closed conformation when bound to Mu

38 lates fusion both as a fusion restraint that syntaxin-1 alleviates and as an essential cofactor that

39 We conclude that clustering of syntaxin-1 allows the cell to maintain a high syntaxin-1

40 s in two distinct modes (i.e., with isolated syntaxin-1 alone in a "closed" conformation and with ass

41 syntaxin-1 opens and reveal how part of the syntaxin-1 amino-terminal region can help nucleate inter

42 Syntaxin 1, an essential protein in synaptic membrane fu

43 to form template complexes with Munc18-1 and syntaxin-1, an essential intermediate for SNARE assembly

44 om brain extracts that predominantly contain syntaxin 1 and 2.

45 the inner plexiform layer strata displaying syntaxin 1 and ChAT.

46 hed E2 ubiquitin-conjugating enzyme UbcH8 to syntaxin 1 and facilitates the ubiquitination and protea

47 -1 is a neuronal protein that interacts with syntaxin 1 and is required for synaptic vesicle exocytos

48 brane protein 2) on the synaptic vesicle and syntaxin 1 and SNAP-25 (synaptosome-associated protein o

49 We demonstrate that syntaxin 1 and SNAP-25 cooperate as SNARE proteins to su

50 lso contained the synaptic t-SNARE proteins, syntaxin 1 and SNAP-25, suggesting that SV2B may partici

51 Focusing on syntaxin 1 and SNAP-25, we implemented direct stochastic

52 -embedded t-SNAREs consisting of full-length syntaxin 1 and SNAP-25B at the membrane, as measured by

53 The expression of syntaxin 1 and synaptosome-associated protein of 25 kDa

54 shes the ability of SNAP-25 to interact with syntaxin 1 and VAMP2 and prevents the assembly of the SN

55 ate containing Munc18-1 and 2 SNARE proteins-syntaxin 1 and VAMP2.

56 d protein of 25 kDa (SNAP-25) interacts with syntaxin 1 and vesicle-associated membrane protein 2 (VA

57 fied as a molecular clamp that controls free syntaxin-1 and dynamin-1 availability and thereby regula

58 3a of Munc18-1 abolishes its ability to bind syntaxin-1 and fails to rescue the level and trafficking

59 aphilin competes with SNAP-25 for binding to syntaxin-1 and inhibits SNARE complex formation by absor

60 quires the polybasic juxtamembrane region of syntaxin-1 and is not affected by the superclamp mutatio

61 thereby increasing the immunoavailability of syntaxin-1 and leading indirectly to Ca(2+) current inhi

62 rprisingly, we find that both lipid-anchored syntaxin-1 and lipid-anchored synaptobrevin-2 lacking TM

63 Although SNARE complexes containing open syntaxin-1 and Munc18-1 are essential for exocytosis, th

64 Syntaxin-1 and Munc18-1 depend on each other for normal

65 mptothecin uncovered striking differences to syntaxin-1 and MUNC18-1 depleted neurons.

66 H+-ATPase binds directly to the H3 domain of syntaxin-1 and not through VAMP-2 or SNAP-23.

67 mutant of P335A reduces the ability to bind syntaxin-1 and rescue syntaxin-1 levels.

68 ronal SM protein Munc18-1 and SNARE proteins syntaxin-1 and SNAP-25 (25 kDa synaptosome-associated pr

69 that CAPS exhibits high affinity binding to syntaxin-1 and SNAP-25 and moderate affinity binding to

70 synaptobrevin and the plasma membrane SNAREs syntaxin-1 and SNAP-25 assemble into a tight SNARE compl

71 ibody targeting otoferlin immunoprecipitated syntaxin-1 and SNAP-25 but not synaptobrevin-1.

72 ctor (NSF) and alpha-SNAP, which disassemble syntaxin-1 and SNAP-25 heterodimers.

73 ype SNAP-25, indicating that pairing between syntaxin-1 and SNAP-25 is required for parietal cell act

74 ngle molecules, and the numbers of unlabeled syntaxin-1 and SNAP-25 molecules per cell.

75 Fifty to seventy copies each of syntaxin-1 and SNAP-25 molecules were associated with a

76 we observed nanoscale clusters consisting of syntaxin-1 and SNAP-25 that contained associated Munc18-

77 ly, VAMP4 forms a stable complex with SNAREs syntaxin-1 and SNAP-25 that does not interact with compl

78 gth amisyn forms a stable SNARE complex with syntaxin-1 and SNAP-25 through its C-terminal SNARE moti

79 tic vesicles (SVs), forms helix bundles with syntaxin-1 and SNAP25 for the SNARE assembly.

80 Its components, syntaxin-1 and SNAP25, are largely present in individual

81 ible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly.

82 tially containing the plasma membrane SNAREs syntaxin-1 and soluble NSF attachment protein (SNAP)-25.

83 nteractions between the amino termini of the syntaxin-1 and synaptobrevin SNARE motifs, while their c

84 tion of the synaptic SNARE proteins SNAP-25, syntaxin-1 and synaptobrevin-2, as well as by an age-dep

85 structures of Munc18-1 bound to cross-linked syntaxin-1 and synaptobrevin.

86 o exocytosis, they must recruit the proteins syntaxin-1 and synaptosomal associated protein 25 (SNAP-

87 unc18-1 with the N-terminal H(abc) domain of syntaxin-1 and the four-helical bundle of the assembled

88 bility of the Munc18-1 variants to chaperone syntaxin-1 and to rescue exocytosis is strongly impaired

89 The neuronal SM protein Munc18-1 binds to syntaxin-1 and to the SNARE complex through interactions

90 ays a significant role in the chaperoning of syntaxin-1 and, if so, how these dual functions of domai

91 racts from brain regions shows that SNAP-25, syntaxin 1, and 4 are broadly distributed, while SNAP-23

92 CAPS bound syntaxin-1, and CAPS truncations that competitively inhi

93 N-peptide is not spatially constrained along syntaxin-1, and it is functional when translocated to an

94 quires Munc18-1, which binds to the released syntaxin-1, and Munc13-1, which, together with Munc18-1,

95 rans complexes of the SNARE proteins VAMP-2, syntaxin-1, and SNAP-25 that bridge vesicle and plasma m

96 The presynaptic proteins MUNC18-1, syntaxin-1, and SNAP25 drive SNARE-mediated synaptic ves

97 The presence of complexin I/II, syntaxin-1, and synapsin I in rabbit horizontal cell pro

98 subcellular distribution of complexin I/II, syntaxin-1, and synapsin I in rabbit retina.

99 ly of the SNARE complex composed of SNAP-25, syntaxin-1, and synaptobrevin-2 (sybII) proteins.

100 ermolecular interactions among the receptor, syntaxin-1, and the Ca(V)2.2 channel.

101 Syntaxin-1 appeared only in taste cells, but SNAP-25, sy

102 fails to rescue the level and trafficking of syntaxin-1 as well as to restore exocytosis in Munc18-1/

103 that DAP kinase binds to and phosphorylates syntaxin-1 at serine 188.

104 tion as a molecular clamp that controls free syntaxin-1 availability for the assembly of the SNARE co

105 Pre-docked syntaxin 1-based SNARE complexes bound by Munc18-1 were

106 is trafficking defect is specific for UNC-64 Syntaxin-1, because 14 other SNARE proteins and two acti

107 APS truncations that competitively inhibited syntaxin-1 binding also inhibited CAPS-dependent fusion.

108 he Sly1 N-terminal domain is opposite to the syntaxin 1-binding surface of the Munc18-1 N-terminal do

109 AMP-2 and SNAP-23, but only non-H3-truncated syntaxin-1 bound H+-ATPase, and synt-1ADeltaC expression

110 formation of syntaxin-1 not only in the free syntaxin-1 but also in the t-SNARE (syntaxin-1/SNAP-25)

111 nt liposome fusion with N-terminal truncated syntaxin-1 but exhibits impaired activity with C-termina

112 nc18-1 that preserve tight binding to closed syntaxin-1 but markedly disrupt Munc18-1 binding to SNAR

113 s known to bind tightly to the SNARE protein syntaxin-1, but only when syntaxin-1 is in a closed conf

114 Munc18-1 reclustering was independent of syntaxin-1, but required calcium influx and protein kina

115 Here we report that cleavage of syntaxin 1 by BoNT/C, and cleavage of SNAP-25 by BoNT/E

116 and its binding partner, the t-SNARE-protein Syntaxin-1, by approximately 30% and decrease spontaneou

117 at the preferential binding of CAPS1 to open syntaxin-1 can contribute to the stabilization of the op

118 As expected for a C-terminal binding site on syntaxin-1, CAPS stimulates SNARE-dependent liposome fus

119 alpha-helix containing Pro-335 promotes the syntaxin-1 chaperoning function, whereas the P335A mutat

120 ion could not be explained by differences in syntaxin-1 chaperoning/localization or vesicle docking,

121 l cholesterol depletion, leading directly to syntaxin-1 cluster dispersal and Ca(2+) current inhibiti

122 Also, calcium was shown to promote syntaxin 1 clustering in the plasma membrane, but the mo

123 te Ca(2+) influx by expanding or contracting syntaxin-1 clusters.

124 ex is biased toward the open conformation of syntaxin-1 compared with the binary complex.

125 1-226 bound poorly in vitro with recombinant syntaxin-1 compared with wild type SNAP-25, indicating t

126 Correspondingly, the N-terminal region of syntaxin-1 competes with the SNARE four-helix bundle and

127 1 catalyzes the transition from the Munc18-1/syntaxin-1 complex to the SNARE complex, the molecular m

128 s this fusion, in part by forming the closed syntaxin-1 conformation.

129 The synaptic target membrane SNARE syntaxin 1 contains a highly conserved H(abc) domain, wh

130 densities and liposomes containing very low syntaxin-1 densities.

131 , and late CC-3 activation were conserved in syntaxin-1 depleted human neurons.

132 current study demonstrates that MUNC18-1 or syntaxin-1 depleted neurons show a new, atypical, staged

133 ction hours before cell death in MUNC18-1 or syntaxin-1 depleted neurons, whereas all neurites retrac

134 expected, but not cell death in MUNC18-1 or syntaxin-1 depleted neurons.

135 et of Munc18-1 rescues impaired secretion in syntaxin-1-depleted PC12 cells and the lethality and let

136 Cell death on MUNC18-1 or syntaxin-1 depletion is characterized by consecutive neu

137 The C-terminal site for CAPS binding on syntaxin-1 does not overlap the Munc18-1 binding site an

138 Thus, the N-terminal syntaxin-1 domains mediate different functions in synapt

139 ailable about the in vivo functions of these syntaxin-1 domains.

140 te to the stabilization of the open state of syntaxin-1 during its transition from "closed" state to

141 -attachment protein receptor (SNARE) protein syntaxin-1 exhibits two conformations that both bind to

142 smitter release machinery, and regulation of syntaxin 1 expression levels is thought to contribute to

143 yntaxin-1 allows the cell to maintain a high syntaxin-1 expression level without compromising Ca(2+)

144 Munc18-1 binds to the SNARE syntaxin-1 folded into a closed conformation and to SNAR

145 8-1, which binds to the SNARE complex and to syntaxin-1 folded into a closed conformation.

146 Exocytosis likely starts with Syntaxin-1 folded into a self-inhibited closed conformat

147 vel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation by the ubiquitin-proteasome p

148 napses use classical SNARE machinery such as syntaxin-1 for neurotransmitter release in rat circumval

149 l transmembrane regions of synaptobrevin and syntaxin-1 form continuous helices that act mechanically

150 mpromising Ca(2+) influx, and recruitment of syntaxin-1 from clusters by SNAP-25 expression makes it

151 ous or exogenous SNAP-25 expression recruits syntaxin-1 from clusters on the plasma membrane, thereby

152 Thus, the closed conformation of syntaxin-1 gates the initiation of the synaptic vesicle

153 ptide is functionally important, whereas the syntaxin-1 H(abc)-domain is not, but limited information

154 ntly inhibits liposome fusion by: binding to syntaxin-1, hindering Munc18-1 binding; binding to synta

155 Lim-syn isoforms showed great identity with syntaxin 1-homologs (syntaxin 1A/1B) from various other

156 g and trafficking the central SNARE protein, syntaxin-1 (i.e. chaperoning function), by its domain-1;

157 inding protein Doc2B or ubMunc13-2 increases syntaxin-1 immunoavailability and concomitantly down-reg

158 racted with ER and Golgi syntaxin 5 and with syntaxin 1 in the absence of Munc18a, when syntaxin 1 is

159 rnary SNARE complex formation by locking the syntaxin-1 in a cleft of Munc18-1.

160 its biochemical interaction with the t-SNARE syntaxin-1 in a closed conformation caused premature ter

161 However, whether CAPS1 interacts with syntaxin-1 in a similar mode to Munc13-1 remains unclear

162 nd with assembled SNARE complexes containing syntaxin-1 in an "open" conformation).

163 protein Munc18-1 traps the Qa-SNARE protein syntaxin-1 in an autoinhibited closed conformation.

164 yntaphilin and inhibits its interaction with syntaxin-1 in neurons.

165 g/closing transition reveals that the closed syntaxin-1 in the syntaxin-1/SNAP-25/Munc18-1 complex is

166 vestigated the presynaptic membrane protein, syntaxin-1, in circumvallate taste buds of the rat.

167 basic residues in the plasma membrane SNARE syntaxin-1 increase inhibition by PI 4,5-P(2), suggestin

168 In contrast, syntaxin-1 inhibits Ca(2+) currents independently of SNA

169 For instance, the protein syntaxin-1 involved in neuronal SNAREs, has a single tra

170 Syntaxin 1 is a SNARE protein that plays a central role

171 Syntaxin 1 is an essential component of the neurotransmi

172 h syntaxin 1 in the absence of Munc18a, when syntaxin 1 is retained in the ER.

173 tory interaction between Munc18-1 and closed syntaxin 1 is well described, the mechanism of how Munc1

174 Syntaxin-1 is a key component of the synaptic vesicle do

175 Syntaxin-1 is a key component of the synaptic vesicle do

176 s suggest that binding of Munc18-1 to closed syntaxin-1 is a specialization that evolved to meet the

177 Because the main role of syntaxin-1 is as a target-SNARE for vesicle fusion, appe

178 more potent than the A-isoform, but not when syntaxin-1 is cleaved by botulinum neurotoxin C.

179 Importantly, the binding mode of CAPS1 to syntaxin-1 is distinct from that of Munc13-1; CAPS1 bind

180 the SNARE protein syntaxin-1, but only when syntaxin-1 is in a closed conformation that is incompati

181 yx-of-Held synapse from mutant mice in which syntaxin-1 is rendered constitutively open and SNARE-com

182 Syntaxin-1 is the central SNARE protein for neuronal exo

183 ntial for exocytosis, the function of closed syntaxin-1 is unknown.

184 is avoided only when Munc18-1 binds first to syntaxin-1, leading to Munc18-1-Munc13-1-dependent lipos

185 es the ability to bind syntaxin-1 and rescue syntaxin-1 levels.

186 d two conserved residues (R151, I155) in the syntaxin-1 linker region as key sites for the MUN domain

187 ation tightly bound to Munc18-1, whereas the syntaxin-1 linker region changes its conformation, simil

188 uggest that the conformational change of the syntaxin-1 linker region induced by Munc13-1 initiates t

189 We also show that anchoring SNAP-25 on the syntaxin-1 liposomes dramatically enhances fusion.

190 dicate that diffuse cytoplasmic and punctate syntaxin-1-LIR are present in different subsets of taste

191 The punctate syntaxin-1-LIR is believed to be associated with Golgi b

192 is present in type III cells while punctate syntaxin-1-LIR is present in type II cells.

193 Diffuse, cytoplasmic syntaxin-1-LIR is present in type III cells while puncta

194 All of the synapses associated with syntaxin-1-LIR taste cells are from type III cells onto

195 Cell death was too rapid after syntaxin-1 loss to study Golgi abnormalities.

196 yrosine (Y337A), which interacts with closed syntaxin-1, mildly increased secretory amplitude.

197 ction is important for a tripartite Munc18-1/syntaxin-1/MUN complex, in which syntaxin-1 still adopts

198 th occurs in cultured neurons upon depleting syntaxin-1, Munc18-1, and/or SNAP-25, well before synaps

199 As proteins, such as syntaxin-1, Munc18-1, or SNAP-25, modulate alpha-synucle

200 proteins involved in synaptic transmission (syntaxin-1, Munc18-1, SNAP-25), whereas other proteins i

201 n-neuronal Munc18 isoform that does not bind syntaxin-1, Munc18-3, in Munc18-1 KO neurons prevented c

202 mplex is less stable than that in the closed syntaxin-1/Munc18-1 complex, which is manifested by the

203 Rescue experiments with syntaxin-1 mutants revealed that Munc18-1 recruitment to

204 t exhibits impaired activity with C-terminal syntaxin-1 mutants.

205 the same low-affinity binding of the extreme syntaxin-1 N terminus to Munc18-1, suggesting that this

206 ults reveal a striking interplay between the syntaxin-1 N-peptide and the conformational state of the

207 Previous in vitro studies suggested that the syntaxin-1 N-peptide is functionally important, whereas

208 hydrophobic pocket, which interacts with the syntaxin-1 N-terminal peptide, has been highly controver

209 SNARE complex through interactions with the syntaxin-1 N-terminal region that are critical for neuro

210 1 proteins induce the closed conformation of syntaxin-1 not only in the free syntaxin-1 but also in t

211 lethargy of unc-64 (C. elegans orthologue of syntaxin-1)-null mutants.

212 presynaptic, GB(1a)-containing receptors on syntaxin-1 opening and calcium entry to enhance probabil

213 The structures allow visualization of how syntaxin-1 opens and reveal how part of the syntaxin-1 a

214 , which activates SNARE complexes containing syntaxin-1 or -3, but not complexes containing syntaxin-

215 The loss of presynaptic proteins Munc18-1, syntaxin-1, or SNAP-25 is known to produce cell death, b

216 a demonstrate that cell death upon Munc18-1, syntaxin-1, or SNAP-25 loss occurs via a degenerative pa

217 Munc13s open Syntaxin-1, orchestrating SNARE complex assembly in an N

218 that the N-peptide and the H(abc)-domain of syntaxin-1 perform distinct and independent roles in syn

219 pecifically and reversibly connects multiple syntaxin 1/PI(4,5)P2complexes into larger mesoscale doma

220 ic vesicle priming and were proposed to open syntaxin-1, promoting SNARE complex assembly.

221 gans genetics, we show that the N-peptide of syntaxin-1 recruits the SM protein Munc18-1/nSec1 to the

222 cular events that control the degradation of syntaxin 1 remain undefined.

223 Modeling based on the known structure of syntaxin 1 revealed that these residues are exposed on t

224 e neuronal proteins synaptobrevin 1 (VAMP1), syntaxin 1, SNAP-25, and soluble N-ethylmaleimide-sensit

225 exocytosis of MSGs in neuroendocrine cells, syntaxin 1, SNAP-25, and VAMP2, were not involved in hom

226 rate assembly of the SNARE complex formed by syntaxin-1, SNAP-25 and synaptobrevin, allowing exquisit

227 nsmitter release includes the SNARE proteins syntaxin-1, SNAP-25 and synaptobrevin, which form a tigh

228 nesis, within 1-4 DIV upon loss of t-SNAREs (syntaxin-1, SNAP-25) or Munc18-1, but not v-SNAREs (syna

229 euron, SNARE/SM protein complexes containing syntaxin-1, SNAP-25, and Munc18-1 are preassembled in mi

230 The SNAP receptor (SNARE) proteins syntaxin-1, SNAP-25, and synaptobrevin mediate neurotran

231 ent protein (SNAP) receptor (SNARE) proteins syntaxin-1, SNAP-25, and synaptobrevin/VAMP (vesicle-ass

232 cts, double-labeling experiments showed that syntaxin-1, SNAP-25, synaptobrevin, and synaptophysin co

233 SNARE- and SM-protein complexes composed of syntaxin-1, SNAP-25, synaptobrevin-2/VAMP2, and Munc18-1

234 in-1, hindering Munc18-1 binding; binding to syntaxin-1-SNAP-25 heterodimers, precluding SNARE comple

235 e fusion between synaptobrevin liposomes and syntaxin-1-SNAP-25 liposomes, but high fusion efficiency

236 ution assays with the neuronal SNAREs, using syntaxin-1-SNAP-25-containing liposomes and liposomes co

237 es containing preassembled t-SNARE proteins (syntaxin 1.SNAP-25), we determined how Munc18-1 controls

238 t to BoNT/C and E in neurons, can substitute syntaxin 1/SNAP-25 and prevent toxin-induced neuron deat

239 h neuronal cytotoxicity for BoNTs and reveal syntaxin 1/SNAP-25 as the ubiquitous and essential SNARE

240 ma membrane recycling processes that utilize syntaxin 1/SNAP-25, independent of synaptic vesicle exoc

241 so uncover interactions of membrane-anchored syntaxin-1/SNAP-25 heterodimers with the MUN domain, Mun

242 3/Munc13s may provide a template to assemble syntaxin-1/SNAP-25 heterodimers, leading to an acceptor

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

244 usion assay using VAMP2-containing donor and syntaxin-1/SNAP-25-containing acceptor liposomes.

245 on reveals that the closed syntaxin-1 in the syntaxin-1/SNAP-25/Munc18-1 complex is less stable than

246 t protein receptor (SNARE) complex formed by syntaxin-1, SNAP25, and synaptobrevin.

247 e on depletion of presynaptic SNARE proteins syntaxin-1, SNAP25, or MUNC18-1.

248 te Munc18-1/syntaxin-1/MUN complex, in which syntaxin-1 still adopts a closed conformation tightly bo

249 Syntaxin 1 (Stx1) is a SNARE protein that is phosphoryla

250 Syntaxin-1 (STX1) and Munc18-1 are two requisite compone

251 Syntaxin-1 (Stx1) is a component of the synaptic vesicle

252 receptor (SNARE) complexes by SNARE proteins syntaxin-1 (Stx1), synaptosomal-associated protein 25 (S

253 chanisms: First, neuronal silencing promotes syntaxin-1 switch from a closed to an open conformation

254 e and requires that the target-SNARE protein syntaxin-1 switches from a closed to an open conformatio

255 lease depends on the SNARE complex formed by syntaxin-1, synaptobrevin and SNAP-25, as well as on com

256 The SNAREs Syntaxin-1, Synaptobrevin, and SNAP-25 play a central ro

257 ins among other factors: the neuronal SNAREs syntaxin-1, synaptobrevin, and SNAP-25, which form a tig

258 ated proteins, such as VAMP (synaptobrevin), syntaxin-1, synaptophysin, synapsin Ia/b and IIa, munc-1

259 nock-down of syntabulin or disruption of the syntaxin-1-syntabulin-KIF5B complex impairs the anterogr

260 We now report that the complex of syntaxin-1-syntabulin-KIF5B mediates axonal transport of

261 C2D-F domains interact with the syntaxin-1 t-SNARE motif with maximum binding within the

262 veral other phenotypes as causal (defects in syntaxin-1 targeting and synaptic transmission).

263 The mutants rescued vesicle docking and syntaxin-1 targeting to the plasma membrane, with the ex

264 morphology, but not synaptic transmission or syntaxin-1 targeting.

265 ception of P335A that only supported partial syntaxin-1 targeting.

266 Munc18 binds to the closed conformation" of syntaxin 1, the ER-Golgi SM protein Sly1 interacts only

267 f the six different SNARE proteins examined [syntaxins 1 through 4 of 25-kDa synaptosome-associated p

268 epletion of presynaptic proteins MUNC18-1 or syntaxin-1 triggers an atypical, staged cell death pathw

269 proteins mediating synaptic vesicle fusion, syntaxin-1 uniquely includes an N-terminal peptide ('N-p

270 transition depends upon the linker region of syntaxin-1 upstream of its helical bundle-forming SNARE

271 nformational states ("closed" vs. "open") of syntaxin-1 using PC12 cells and Caenorhabditis elegans.

272 o form ternary template complexes - Munc18-1:Syntaxin-1:VAMP2 for synaptic vesicle fusion and Munc18-

273 The interaction of SNAP-29 with syntaxin-1 was further confirmed with immunoprecipitatio

274 Binding of Munc18-1 to syntaxin-1 was impaired in syntaxin-1B(Open) synapses, a

275 ensitive factor attachment protein receptor) syntaxin-1 was shown previously to be present on putativ

276 rmation, similar to that of the LE mutant of syntaxin-1 when bound to Munc18-1.

277 e, binding first to a closed conformation of syntaxin-1 where its amino-terminal region interacts wit

278 ritical role in intracellular trafficking of syntaxin-1, which is dependent on the conformational sta

279 al a novel mode of binding between CAPS1 and syntaxin-1, which play a crucial role in neurosecretion.

280 APS1 binds to the full-length of cytoplasmic syntaxin-1 with preference to its "open" conformation, w

281 Expression of Munc18-1, which recruits syntaxin-1 within the exocytotic pathway, does not modul