ライフサイエンスコーパス: Rab GTPase

1 equires correct and specific localization of Rab GTPases.

2 the activation mechanisms of closely related Rab GTPases.

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

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

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

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

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

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

9 tosis, presumably by inactivating the target Rab GTPases.

10 RGGT), selectively preventing prenylation of Rab GTPases.

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

12 brane protein (Inc), interacts with multiple Rab GTPases.

13 gulate vesicle traffic via interactions with Rab GTPases.

14 lcysteine residues of CaaX proteins and some RAB GTPases.

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

16 ed transportation network linked together by Rab GTPases.

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

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

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

20 al binding sites for as many as 14 different Rab GTPases across its entire length.

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

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

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

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

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

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

27 We recently identified the Rab GTPase-activating protein (GAP) AS160 as a putative

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

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

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

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

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

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

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

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

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

37 ub2, and Cdc16) domain present in most known Rab GTPase-activating proteins (GAPs).

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

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

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

43 Coupling of Rab GTPase activation and SNARE complex assembly during

44 Mutation of amino acids implicated in Rab GTPase activation by other TBC domain-containing GAP

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

46 icrodomains may be a key factor for coupling Rab GTPase activation to SNARE complex assembly.

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

48 rate sites (4P); 2) AS160 mutated to abolish Rab GTPase activity (R/K); and 3) double mutant AS160 co

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

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

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

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

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

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

55 1 is able to regulate the phosphorylation of Rab GTPases and indicate that monitoring phosphorylation

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

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

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

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 in cholesterol and triglyceride metabolism, Rab GTPases, and many membrane and endoplasmic reticulum

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

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

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

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

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

75 Rab GTPases are central for autophagy but their regulati

76 Rab GTPases are considered master regulators of membrane

77 Rab GTPases are critical regulators of membrane traffick

78 Individual Rab GTPases are distributed to specific organelles and t

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

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

81 Rab GTPases are highly conserved components of vesicle t

82 Rab GTPases are highly conserved components of vesicle t

83 Rab GTPases are key cellular regulators of membrane traf

84 Rab GTPases are key regulators of membrane traffic pathw

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

86 Ypt-Rab GTPases are key regulators of the various steps of i

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

88 Inactive Rab GTPases are maintained in the cytosol by binding to

89 Rab GTPases are master regulators of membrane traffickin

90 Rab GTPases are molecular switches mobilizing intracellu

91 Rab GTPases are molecular switches that orchestrate vesi

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

93 The Rab GTPases are the largest family of proteins regulatin

94 Rab-GTPases are important molecular switches regulating

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

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

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

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

99 ukaryotic organisms and function as GAPs for Rab GTPases as well as GTPases that control cytokinesis.

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

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

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

103 d proteins are required to displace GDI from Rab GTPases before Rab activation by guanosine diphospha

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

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

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

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

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

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

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

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

112 Rab GTPases control membrane traffic and receptor-mediat

113 Rab GTPases control specific membrane compartments, from

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

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

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

117 Rab GTPases define the vesicle trafficking pathways unde

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

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

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

121 The glutamine from the Rab GTPase does not stabilize the transition state as ex

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

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

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

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

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

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

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

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

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

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

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

133 The Rab GTPase family comprises approximately 70 GTP-binding

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

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

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

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

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

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

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

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

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

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 Loss of function in glo-4 or in its target Rab GTPase, glo-1, causes neuronal defects resembling th

149 However, no Ypt/Rab GTPase has been shown to regulate the motility of ex

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

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

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

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

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

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

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

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

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

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

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

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

167 nced green fluorescent protein (EGFP)-tagged Rab GTPases, including Rab6, are recruited to Chlamydia

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

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

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

171 e inclusion membrane, demonstrating that the Rab GTPase-interacting domain of Cpn0585 faces the host

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

173 Cpn0585-Rab GTPase interactions are direct and GTP dependent as

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

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

176 Rab GTPases, key regulators of vesicular transport, hydr

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

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

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

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

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

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

183 distinct biochemical reactions critical for Rab GTPase membrane cycling to redirect Rab1 to the path

184 We show that the Rab GTPase membrane trafficking regulators Rab8a, -17, a

185 americ retromer complex, and the Ypt6p Golgi Rab GTPase module.

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

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

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

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

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

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

192 ta suggest that RPM-1 positively regulates a Rab GTPase pathway to promote vesicular trafficking via

193 Rab GTPases play an essential role in vesicular transpor

194 A recent study describes a role for a Rab GTPase previously implicated in endoplasmic reticulu

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

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

201 ion of intracellular membranes also requires Rab GTPases, Rab effectors, SM proteins, and specific re

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

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

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

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

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

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

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

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

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

211 Rab GTPases recruit myosin motors to endocytic compartme

212 The Rab GTPases recruit peripheral membrane proteins to intr

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

214 Rab GTPases regulate all steps of membrane trafficking.

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

216 Rab GTPases regulate membrane trafficking by cycling bet

217 Because Rab GTPases regulate specific trafficking pathways, we s

218 Over 60 distinct Rab GTPases regulate specific vesicular transport steps

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

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

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

222 Rab GTPases regulate vesicle budding, motility, docking,

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

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

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

226 Rab GTPases represent the largest subfamily of Ras-relat

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

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

229 cterization of the 29 Caenorhabditis elegans Rab GTPases reveals that depletion of RAB-5 phenocopies

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

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

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

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

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

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

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

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

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

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

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

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

242 Activation of the rab GTPase, Sec4p, by its exchange factor, Sec2p, is nee

243 Rab GTPases serve as major control elements in the coord

244 Rab GTPases serve as molecular switches to regulate euka

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

246 es with fluorescent fusion protein endosomal Rab GTPases, such as ARA6/RabF1, RHA1/RabF2a, and ARA7/R

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

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

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

250 ing, which is rescued by overexpression of a Rab GTPase that regulates ER-->Golgi trafficking.

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

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

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

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

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

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

257 The human genome encodes approximately 70 Rab GTPases that localize to the surfaces of distinct me

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

259 nced green fluorescent protein (EGFP)-tagged Rab GTPases, the colocalization with Cpn0585 at the incl

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

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

262 Rab GTPases, the largest subgroup in the superfamily of

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

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

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

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

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

268 at Cpn0585 is involved in the recruitment of Rab GTPases to the inclusion membrane and that interferi

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

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

271 As Ypt7 is one of many Rab GTPases, ubiquitin-proteasome regulation may be invo

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 Recently, several Rab GTPases were found to associate with the inclusions

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

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 The Rab GTPase Ypt1 and its mammalian homolog Rab1 regulate

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

296 rocesses: it is an effector for the vacuolar Rab GTPase Ypt7p and is required for vacuolar SNARE comp

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.