ライフサイエンスコーパス: Rab GTPase

1 ed transportation network linked together by Rab GTPases.

2 equires correct and specific localization of Rab GTPases.

3 the activation mechanisms of closely related Rab GTPases.

4 esis as an effector of melanosome-associated Rab GTPases.

5 king include myosin IIB, F-actin, ezrin, and Rab GTPases.

6 Rab31 is a member of the Rab5 subfamily of Rab GTPases.

7 tive, or dominant negative mutant of various Rab GTPases.

8 role in activation and membrane targeting of Rab GTPases.

9 everal host cell proteins, including Ras and Rab GTPases.

10 s detailed insight in the catalysis of human Rab GTPases.

11 d mediated by adaptor proteins, for example, Rab GTPases.

12 and increased phosphorylation of a subset of Rab GTPases.

13 RGGT), selectively preventing prenylation of Rab GTPases.

14 tion and activation of a series of different Rab GTPases.

15 tosis, presumably by inactivating the target Rab GTPases.

16 lcysteine residues of CaaX proteins and some RAB GTPases.

17 egulated, in part, by small molecular weight rab GTPases.

18 membranes for fusion under the regulation of RAB-GTPases.

19 GDP/GTP exchange factor (GEF) that activates Rab-GTPases.

20 d the interaction between NPC1L1 and Rab11a (Rab-GTPase-11a), whereas knockdown of CCK receptors or i

21 sion, and they are endowed with a variety of Rab GTPases (16 out of 43 tested).

22 omotypic fusion of yeast vacuoles requires a Rab GTPase, a large Rab effector complex, SNARE proteins

23 This process is mediated by Rab GTPases activated by their guanine exchange factors

24 ound form, Ryh1, an evolutionarily conserved Rab GTPase, activates TORC2 signaling to the AGC kinase

25 We demonstrate that AnkB binds to Rab GTPase Activating Protein 1-Like (RabGAP1L) and recr

26 that reactivates a cryptic transcript of the Rab GTPase activating protein TBC1D16 (TBC1D16-47 kDa; r

27 control of signaling downstream of the AS160 rab GTPase activating protein.

28 n increased steady state levels of Tbc1d1, a RAB-GTPase activating protein involved in Glucose 4 tran

29 rotein in signaling this process is AS160, a Rab GTPase-activating protein (GAP) whose activity appea

30 we demonstrate that TBC1D15, a mitochondrial Rab GTPase-activating protein (Rab-GAP), governs autopha

31 ranslocation, most likely by suppressing its Rab GTPase-activating protein activity.

32 TBC1 domain family member 1 (TBC1D1), a Rab GTPase-activating protein and paralogue of Akt subst

33 ugh its calcineurin-interacting site and Ras/Rab GTPase-activating protein domain, functions as an en

34 inding to Akt substrate of 160 kD (AS160), a Rab GTPase-activating protein that regulates the traffic

35 s have shown that Akt phosphorylation of the Rab GTPase-activating protein, AS160 (160-kDa Akt substr

36 assembly process by overexpressing 37 human Rab GTPase-activating proteins (GAPs) and assessing infe

37 The substrates for most Rab GTPase-activating proteins (GAPs) are unknown.

38 Overexpression of a specific subset of Rab GTPase-activating proteins (RabGAPs) inhibited hista

39 hydrolyze GTP very slowly unless assisted by Rab GTPase-activating proteins (RabGAPs).

40 ng of the orthologous Tre-2/Bub2/CDC16 (TBC) Rab GTPase-activating proteins TBC-7 and TBC1D15 in Caen

41 TBC1D8B is an uncharacterized Rab-GTPase-activating protein likely involved in endocyt

42 n between the Na(+),K(+)-ATPase and AS160, a Rab-GTPase-activating protein.

43 r, we describe the first screen for putative Rab-GTPase-activating proteins (GAPs) during collective

44 The Rab-GTPase-activating proteins TBC1D1 and TBC1D4 (AS160)

45 ion of active-site residues, the Ras-related Rab GTPase activation pathway differs from Ras and betwe

46 recludes interaction of the PI 3-kinase with Rab GTPase activators.

47 hese results demonstrate that stimulation of Rab-GTPase activity is a property of the S. pombe MOP es

48 overed that the order (and thus polarity) of Rab GTPases along the secretory and endocytic pathways a

49 achinery; Peter Novick, on the regulation of rab GTPases along the secretory pathway; Jim Spudich, on

50 uration requires a coordinated change in the Rab GTPase and phosphoinositide composition of the endos

51 ion of endosomes enriched in the multivalent Rab GTPase and phosphoinositide-binding protein Rabenosy

52 vacuolar environment by modulating both the Rab GTPase and the PI composition of the chlamydial incl

53 also illuminated, including a system of >40 Rab GTPases and associated regulatory proteins, where GP

54 1 is able to regulate the phosphorylation of Rab GTPases and indicate that monitoring phosphorylation

55 effects of C-terminal carboxylmethylation on RAB GTPases and provide a rationale for targeting ICMT i

56 A potential class of binding partners are Rab GTPases and Rab3A is known to associate with SVs and

57 interactors, TPCs were resolved to scaffold Rab GTPases and regulate endomembrane dynamics in an iso

58 This process depends on Ulk1, Rab GTPases and SNARE complexes implicated in secretory

59 These insertions are dependent on distinct Rab GTPases and SNARE complexes.

60 ation of the Golgi apparatus, recruitment of Rab GTPases and SNAREs, and translocation of cytoplasmic

61 ion at eukaryotic organelles is initiated by Rab GTPases and tethering factors.

62 at endomembranes requires cross-talk between Rab GTPases and tethers to drive SNARE-mediated lipid bi

63 Rab GTPases and their effectors mediate docking, the ini

64 is assays, demonstrating the druggability of Rab GTPases and their effectors.

65 through AS160/Tbc1D4 and Tbc1D1 to modulate Rab GTPases and through the Rho GTPase TC10alpha to act

66 this, we screened all Caenorhabditis elegans Rab GTPases and Tre2/Bub2/Cdc16 (TBC) domain containing

67 Rab GTPases and ubiquitination are critical regulators o

68 xtract monogeranylgeranylated membrane-bound Rab GTPases and, thus, is not merely a solubilization fa

69 oordination between phosphoinositide lipids, Rab GTPases, and microtubule-based motors to dynamically

70 kinetic proofreading of membrane surfaces by Rab GTPases, and permit accumulation of active Rabs only

71 al fusion events mediated by SNARE proteins, Rab-GTPases, and multisubunit tethering complexes.

72 Rab GTPases are a family of proteins that regulate and p

73 Recently, we demonstrated that several Rab GTPases are actively targeted to the inclusion.

74 Rab GTPases are central for autophagy but their regulati

75 Rab GTPases are considered master regulators of membrane

76 Rab GTPases are critical regulators of membrane traffick

77 Individual Rab GTPases are distributed to specific organelles and t

78 In their native form, most Rab GTPases are doubly geranylgeranylated at the C termi

79 Thus, we conclude that Rab GTPases are essential for membrane trafficking-depen

80 Rab GTPases are highly conserved components of vesicle t

81 Rab GTPases are highly conserved components of vesicle t

82 Rab GTPases are key cellular regulators of membrane traf

83 Rab GTPases are key regulators of membrane traffic pathw

84 regulators of the actin-based cytoskeleton; Rab GTPases are key regulators of membrane traffic.

85 Rab GTPases are known to play a crucial role in the endo

86 Rab GTPases are master regulators of membrane traffickin

87 Rab GTPases are molecular switches mobilizing intracellu

88 Rab GTPases are molecular switches that orchestrate vesi

89 Endocytic cargo and Rab GTPases are segregated to distinct domains of an end

90 The Rab GTPases are the largest family of proteins regulatin

91 Rab-GTPases are important molecular switches regulating

92 Because Rab-GTPases are important regulators of membrane traffic

93 regulators of intracellular trafficking, Ypt/Rab GTPases, are stimulated by specific upstream activat

94 de the first evidence for an early endosomal Rab GTPase as a positive regulator of NGF signal transdu

95 cology to unambiguously identify a subset of Rab GTPases as key LRRK2 substrates.

96 Global proteomic screens have revealed many Rab GTPases as phosphoproteins, but the effects of this

97 The dynamics by which host Rab GTPases associate with pathogen-occupied vacuoles pr

98 a demonstrate that different combinations of Rab GTPase association with Myo5B control distinct membr

99 how that MP colocalizes in vesicles with the Rab GTPase AtRAB-F2b, which is resident in prevacuolar l

100 A new study shows that Rab GTPase binding causes 'entropic collapse' of the coi

101 Rab-GTPase binding effector protein 2 (RABEP2) was ident

102 protein particle (TRAPP) complexes activate Rab GTPases by catalyzing GDP/GTP nucleotide exchange.

103 Activation and inactivation of Rab GTPases by GEFs and GAPs promotes or terminates vesi

104 f membrane traffic have come from studies of Rab GTPases by Marino Zerial and Peter Novick and their

105 ria and eukaryotic host organisms deactivate Rab GTPases by supplying catalytic arginine and glutamin

106 ir cargo to the trans-Golgi and suggest that Rab GTPases can regulate SNARE-tether interactions.

107 al proteins, Golgi resident enzymes, SNAREs, Rab GTPases, cargo, and cytoskeletal proteins.

108 Rab GTPases control membrane traffic and receptor-mediat

109 Rab GTPases control specific membrane compartments, from

110 Our results suggest that Rab GTPases coordinate with each other in the regulation

111 rs have shown that overexpression of certain Rab GTPases corrects defective membrane trafficking and

112 vacuole fusion to proteins that regulate the Rab GTPase cycle-Gdi1p (GDP-dissociation inhibitor [GDI]

113 Rab GTPases define the vesicle trafficking pathways unde

114 ntrifugation, and specific colocalization of Rab GTPases defined the subcellular distribution of Hyal

115 pneumophila as able to inhibit a SNARE- and Rab GTPase-dependent membrane fusion pathway in vitro, t

116 Regulation of endosomal trafficking by Rab GTPases depends on selective interactions with multi

117 ecifically, we show that eukaryotic Rho- and Rab-GTPase domains are found nearly exclusively in eukar

118 After whole-genome duplication, Rab GTPase duplicates are more highly retained than othe

119 tein-coupled receptors (GPCRs) interact with Rab GTPases during their intracellular trafficking.

120 uctural models suggests a possible conserved Rab GTPase effector function in tomosyn vertebrate homol

121 The Rab GTPase effector, Rab-coupling protein (RCP) is known

122 Many Rab GTPase effectors are membrane-tethering factors, tha

123 We identified two Rab GTPases, encoded by VPS21 and YPT72, required for tr

124 as a multicopy suppressor of loss of Ypt1, a Rab GTPase essential for COPII vesicle tethering at the

125 sport protein particle (TRAPP) complexes are Rab GTPase exchange factors that share a core set of sub

126 HE6 in early endosomal function, we examined Rab GTPase expression in early and late endosomes.

127 fications mediate the membrane attachment of Rab GTPases, facilitating their function in regulating i

128 ased motor protein that binds members of the Rab GTPase family (3A, 8A, 10, 11A, 27A) and is implicat

129 Members of the Rab GTPase family and their disparate effectors are recr

130 Members of the Rab GTPase family are master regulators of vesicle traff

131 The Rab GTPase family comprises approximately 70 GTP-binding

132 tion of these receptors is controlled by the Rab GTPase family of proteins.

133 In eukaryotes, members of the Rab GTPase family of small monomeric regulatory GTPases

134 ll GTPases, including Rac and members of the Rab GTPase family, and their effector proteins.

135 landscape of major members of the mammalian Rab GTPase family.

136 atic screen for interactions with the entire Rab GTPase family.

137 TBC1D1 is a member of the TBC1 Rab-GTPase family of proteins and is highly expressed in

138 Rab1b belongs to the Rab-GTPase family that regulates membrane trafficking an

139 ation inhibitor (GDI) solubilizes prenylated Rab GTPases from and shuttles them between membranes in

140 ectroscopy to directly observe extraction of Rab GTPases from model membranes by GDI.

141 Their finding that RAB GTPase function enables genomic amplification to con

142 il adaptor domain, a pair of EF-hands, and a Rab GTPase fused into a single polypeptide.

143 Simultaneous expression of an inactive Rab-GTPase (GAP) domain of TBC1D1 in the R125W mutant re

144 autophagosomes and identified 34 out of 186 Rab GTPase, GAP and GEF family members as potential auto

145 markers of functional diversification in the Rab GTPase gene family in three Paramecium aurelia speci

146 es the SNARE genes SYP124 and SYP125 and the Rab GTPase gene RABA4D.

147 myeloma because we have shown that targeting Rab GTPase geranylgeranylation impairs monoclonal protei

148 A subset of Rab GTPases have been implicated in cilium formation in

149 In Arabidopsis, most Rab GTPases have two C-terminal cysteines and potentiall

150 Applying this to 11 human Rab GTPases identified many known effectors and GAPs, as

151 squid giant axon showed a requirement for a Rab GTPase in Myo5a-dependent vesicle transport.

152 lization, suggesting a potential role of the Rab GTPase in the cup formation.

153 docytic structures, but the function of this Rab GTPase in the endocytic pathway remains poorly chara

154 stigation of the interaction between GDI and Rab GTPases in a membrane environment.

155 n, subcellular localization, and function of Rab GTPases in an organism with a brain.

156 Correct localization of Rab GTPases in cells is critical for proper function in

157 We investigated the role of the Rab GTPases in coordinating the assembly process by over

158 t well understood, and little is known about Rab GTPases in F. graminearum.

159 probed the potential involvement of several Rab GTPases in HSV-1 entry and suggest that endocytic en

160 her support for the collaboration of the two Rab GTPases in regulation of endosome dynamics.

161 ated, and no evidence for involvement of Ypt/Rab GTPases in such a regulation.

162 This is the first study to implicate Rab GTPases in the intracellular trafficking of an RGS p

163 dy was undertaken to investigate the role of Rab GTPases in the intracellular trafficking of EPCR and

164 Ts can not only prenylate a great variety of Rab GTPases in the presence of Rab escort protein but, u

165 usly reported to promiscuously bind multiple Rab GTPases in vitro.

166 e prenylome of P. falciparum is dominated by Rab GTPases, in addition to a small number of prenylated

167 s involved in pigmentation involves specific Rab GTPases, in this instance Rab32 and Rab38.

168 wn role(s) of ExoS-mediated apoptosis and/or Rab GTPase inactivation.

169 LRRK2 phosphorylates multiple RAB GTPases including RAB8A and RAB10.

170 and mammals, can also prenylate certain non-Rab GTPases independently of Rab escort protein.

171 l regulation consistent with statin-specific Rab-GTPase inhibition both in heterologous systems and c

172 bc)R trans-complex are both sensitive to the Rab-GTPase inhibitor, GDI, and to mutations in the vacuo

173 We identified evolutionarily conserved YPT/RAB GTPase Interacting Protein 4a (YIP4a) and YIP4b (for

174 d isoform, JM4, are distant relatives of the Rab GTPase-interacting factor PRA1, and share a topology

175 likely to act as a GEF during activation of Rab GTPases involved in ciliogenesis.

176 oteins and a panel of dominant negative (DN) Rab GTPases involved in TGN-endosome trafficking steps.

177 The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic ve

178 Rab GTPases, key regulators of vesicular transport, hydr

179 rylation of Rab10, a member of the family of Rab GTPases known to be important kinase substrates of L

180 intracellular trafficking, including several rab GTPases, known to modulate cellular localization of

181 ol (PI)-5-phosphatase that binds to multiple Rab GTPases, localizes to chlamydial inclusions.

182 the nodule primordium requires a functional Rab GTPase located in Golgi/trans-Golgi that also partic

183 Thus, Rab GTPases may be novel molecular targets for the selec

184 Our findings also suggest that disruption of Rab GTPase-mediated signalling may represent a major mec

185 APDC increased the activity of Rab4, a small Rab GTPase mediating fast recycling from early endosomes

186 ed by the combined action of coats, tethers, Rab GTPases, motors, and SNAREs in a mechanism that is j

187 Rab-GTPase mutants that restrain phagosome maturation in

188 ly observed three members of a sub-family of Rab GTPases namely Rab8A, 8B and 13 that are all phospho

189 hange factor that activates Sec4p, the final Rab GTPase of the yeast secretory pathway.

190 cargo-bound receptor, which is frequently a Rab GTPase on an organelle.

191 system depends on the initial recognition of Rab GTPase on transport vesicles by multisubunit tetheri

192 (PD) kinase LRRK2 phosphorylates a subset of Rab GTPases on a conserved residue in their switch-II do

193 ped for profiling expression and function of Rab GTPases on a genome-wide scale.

194 Rab GTPases play an essential role in vesicular transpor

195 a guanine nucleotide exchange factor for two RAB GTPases previously implicated in lysosome-related or

196 A novel Rab GTPase protein in Arabidopsis thaliana, CPRabA5e (CP

197 osing LRRK2 kinase phosphorylates a group of Rab GTPase proteins including Rab29, within the effector

198 the Arabidopsis thaliana RabA4 subfamily of Rab GTPase proteins.

199 Legionella Translocation assays for selected Rab-GTPase proteins revealed that they are indeed T4SS s

200 ering effects, can prevent isoprenylation of Rab-GTPase proteins, a protein family important for the

201 posttranslational isoprenyl modification of Rab GTPases, proteins that control vesicle formation, mo

202 utively active or dominant-negative forms of Rab GTPases provided additional insights into the distin

203 (TRAPPI) mediates nucleotide exchange on the RAB GTPase RAB1/Ypt1.

204 vesicle trafficking pathways mediated by the Rab GTPases Rab10 and Rab11 are redundantly required for

205 The small Rab GTPase, Rab10, is required for insulin-stimulated GL

206 e, dynamin2 (Dyn2), and the small regulatory Rab GTPase, Rab10, work independently at distinct steps

207 The ancestral Rab GTPase Rab18 and both subunits of the Rab3GAP comple

208 The Rab GTPase Rab27B and one of its effector proteins, Slac

209 Here, the authors identify the Rab GTPase Rab35 as an essential component of this contr

210 ffold protein VARP and the tissue-restricted Rab GTPase RAB38.

211 ed with 2 known WPB-associated proteins: the Rab GTPases Rab3b and Rab27a.

212 or that can interact with members of Rac and Rab GTPase (Rab4, Rab14 and Rab9) families at different

213 e data demonstrate for the first time that a Rab GTPase, Rab46, integrates G protein and Ca(2+) signa

214 Here we show that endosomal localization of Rab-GTPases (Rab5, Rab7 and Rab11) was inhibited in a st

215 1 (ARF1), bridging integrator 1 (BIN1), and Rab GTPases RAB7L1 and RAB8A are important regulators of

216 LRRK2 recruits the Rab GTPase Rab8A to damaged endolysosomes as well as the

217 SM, Sec17/alphaSNAP, and Sec18/NSF families; Rab-GTPases (Rabs); and Rab effectors.

218 Rab GTPases recruit effector proteins, via their GTP-dep

219 Rab GTPases recruit myosin motors to endocytic compartme

220 The Rab GTPases recruit peripheral membrane proteins to intr

221 The conserved Ypt/Rab GTPases regulate all membrane trafficking events in

222 Rab GTPases regulate all steps of membrane trafficking.

223 These results indicate that Rab GTPases regulate diverse endocytic trafficking pathw

224 Because Rab GTPases regulate specific trafficking pathways, we s

225 Overall our data show that Rab GTPases regulate the internalization and intracellul

226 isternal progression/maturation and that Ypt/Rab GTPases regulate this process.

227 These results show that Ypt/Rab GTPases regulate two separate steps of Golgi cistern

228 Rab GTPases regulate vesicle budding, motility, docking,

229 full understanding of the molecular basis of Rab GTPase-regulated membrane trafficking in eukaryotic

230 How these C(2)H(2) zinc fingers recognize Rab GTPases remains unknown.

231 Zerial was the first to discover that Rab GTPases represent identity markers for different mem

232 Rab GTPases represent the largest subfamily of Ras-relat

233 Thus, phosphocholination of Rab GTPases represents a mechanism by which bacterial FI

234 or post-translational geranylgeranylation of Rab GTPases represents one way to control the activity o

235 ding potential virus-specific differences in Rab GTPase requirements and glycosylphosphatidylinositol

236 ScSec2 acts as a GEF for the small Rab GTPase ScSec4, which regulates vesicle trafficking f

237 d Sro77 are thought to act downstream of the Rab GTPase Sec4 to promote soluble N-ethylmaleimide-sens

238 ort of secretory vesicles is mediated by the Rab GTPase Sec4, activated by its GEF Sec2.

239 y establishment of the exocytosis regulators Rab-GTPase Sec4 and its exchange factor Sec2, but it doe

240 A third Rab GTPase, Sec4, and the exocyst act in tethering and f

241 fashion that depends on the function of the Rab GTPase, Sec4.

242 In addition, the Rab GTPase Sec4p and its guanine nucleotide exchange fac

243 Using the Saccharomyces cerevisiae Rab GTPase Sec4p as a model, we have found that phosphor

244 ide exchange factor (GEF) that activates the Rab GTPase Sec4p on secretory vesicles.

245 tants, we determined that recruitment of the Rab GTPase Sec4p, as well as the exocyst components Sec3

246 p, the Guanine Exchange Factor (GEF) for the Rab GTPase Sec4p.

247 r that promotes exocytosis by activating the Rab GTPase Sec4p.

248 Rab GTPases serve as major control elements in the coord

249 Rab GTPases serve as molecular switches to regulate euka

250 nt increase in the activated levels of small Rab GTPases such as Rab5 and Rab7, both key regulators o

251 egulate membrane traffic in conjunction with Rab-GTPase switches, and we propose to name the gene and

252 Since MyoV binds several Rab GTPases, synchronized nucleator and motor targeting

253 this study we defined a stringent subset of Rab GTPases targeted by SidM and LidA during infection,

254 t, interaction between Dyn2 and a regulatory Rab GTPase that may play an important role in hepatocell

255 constitutively active and dominant-negative Rab GTPases that affect early and late endosome biogenes

256 y was not altered in cells expressing mutant Rab GTPases that affect recycling endosomes.

257 Enzymes called Rab GTPases that carry so-called "activating" mutations

258 lyzes the post-translational modification of RAB GTPases that contain C-terminal CXC motifs.

259 Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of th

260 These results provide the first examples of Rab GTPases that directly act as dynein adaptors and imp

261 nelles in the endomembrane system depends on Rab GTPases that interact with tethering factors before

262 P/GTP binding proteins of the Rab subfamily (Rab GTPases) that cycle between membranes and cytosol de

263 Moreover, although golgins bind to Rab GTPases, the functional significance of Rab binding

264 attachment of geranylgeranyl isoprenoids to Rab GTPases, the key organizers of intracellular vesicul

265 Some of the established players include the Rab GTPases, the SNARE complex proteins, and others, whi

266 Rab GTPases, their effectors, SNAREs of the R, Qa, Qb, a

267 to act as a downstream effector of the Sec4 Rab GTPase to promote soluble N-ethylmaleimide-sensitive

268 ed regulation of lipid phosphoinositides and Rab GTPases to define membrane compartment fates along d

269 ent that highlights the potential ability of Rab GTPases to reach binding partners at a significant d

270 aryotes and serves as an exchange factor for Rab-GTPases to regulate diverse cellular functions.

271 nto the Golgi surface, perhaps by binding to Rab GTPases, to mediate vesicle tethering.

272 apoptotic cells, through recruitment of the Rab GTPase UNC108.

273 the biological roles of inclusion localized Rab GTPases, we have begun to identify inclusion-localiz

274 ritically depends on the correctly localized Rab GTPase, which binds effectors and thus promotes memb

275 lular trafficking depends on the function of Rab GTPases, whose activation is regulated by guanine ex

276 umophila has been discovered to modify human Rab GTPases with ubiquitin.

277 Here we analyze the in vivo movement of 16 Rab GTPases within Drosophila larval axons and show that

278 LRRK2 phosphorylates a subset of Rab GTPases within their Switch-II motif controlling int

279 The Rab GTPase Ypt1 and its mammalian homolog Rab1 regulate

280 c guanine nucleotide exchange factor for the Rab GTPase Ypt1 that is recruited to the phagophore asse

281 de exchange factors (GEFs) that activate the Rab GTPase Ypt1, which is required for secretion.

282 Instead, we show here that the Rab GTPase Ypt1/Rab1 binds and activates Hrr25/CK1delta

283 nstrate that Sec7 is also an effector of two Rab GTPases, Ypt1 (Rab1) and Ypt31/32 (Rab11), signifyin

284 The Rab GTPase Ypt11 is a Myo2-binding protein implicated in

285 Two nonessential proteins, Mmr1 and the Rab GTPase Ypt11, bind Myo2 and have been implicated in

286 Trs31p) are minimally needed to activate the Rab GTPase Ypt1p in an event preceding membrane fusion.

287 eric guanine exchange factors (GEFs) for the Rab GTPase Ypt1p.

288 de exchange factors (GEFs) that activate the Rab GTPase Ypt1p.

289 In yeast, two Rab GTPases, Ypt31/32, are required for post-Golgi vesic

290 inking clathrin adaptor complex AP-1 and the Rab GTPase Ypt31p.

291 3) The Rab GTPase Ypt7 is essential in vivo but often dispensab

292 The Rab GTPase Ypt7 is essential on both membranes for prote

293 tethering complex, which is recruited by the Rab GTPase Ypt7, and vacuolar SNAREs to drive membrane f

294 anes through its affinities for the membrane Rab GTPase Ypt7.

295 ing pH-sensitive machinery downstream of the Rab-GTPase Ypt7 needed for SNARE-mediated lipid bilayer

296 This suggests that the vacuolar Rab-GTPase, Ypt7, and HOPS restrict cis-SNARE disassembl

297 imately 100 nm, only when the yeast vacuolar Rab GTPase Ypt7p is present in both tethered membranes.

298 Fusion of yeast vacuoles requires the Rab GTPase Ypt7p, four SNAREs (soluble N-ethylmaleimide-

299 r attachment protein receptors (SNAREs), the Rab GTPase Ypt7p, vacuolar lipids, Sec17p and Sec18p, an

300 otide exchange factor for the yeast vacuolar Rab GTPase Ypt7p.