ライフサイエンスコーパス: ESCRT

1 ESCRT dysfunction causes ubiquitinated transmembrane pro

2 ESCRT is believed to function as a signaling platform th

3 ESCRT proteins are implicated in myriad cellular process

4 ESCRT-II links these functions by initiating ESCRT-III f

5 ESCRT-III also acts during interphase to repair the NE u

6 ESCRT-III executes membrane scission during the budding

7 nctional cooperation of HD-PTP with ESCRT-0, ESCRT-I and ESCRT-III and support a model for regulation

8 (CHMP7), work together to recruit additional ESCRT-III proteins to holes in the nuclear membrane.

9 How LIP5 and IST1 affect ESCRT-mediated endosomal trafficking and development in

10 protein (Tsg101 in mammals) and Bro1p (ALIX) ESCRT-associated protein, both of which bind to the vira

11 at the other end, so that Vps4 'walks' along ESCRT-III until it encounters the ordered N-terminal dom

12 Although ESCRT-III subunits polymerize into spirals, how individu

13 mer with its cofactor Vta1, ADP.BeFx, and an ESCRT-III substrate peptide.

14 rting by promoting ubiquitination of Hrs (an ESCRT-0 subunit), which inhibits the Hrs association wit

15 ions by initiating ESCRT-III formation in an ESCRT-I-regulated manner.

16 tight interaction between ULK3 and IST1, an ESCRT-III subunit required for abscission.

17 entally derived diffusion coefficients of an ESCRT cargo protein and electron tomograms of Arabidopsi

18 Live imaging showed that an ESCRT-related protein (PDCD6) was enriched in ectosomes

19 report a 3.2 A structure of Vps4 bound to an ESCRT-III peptide substrate.

20 a novel membrane-binding activity within an ESCRT-III subunit that is essential for post-mitotic nuc

21 capture the Bro1 domain of ALIX, which is an ESCRTs recruiting cellular adaptor.

22 es involves tetraspanin CD63, syntenin-1 and ESCRT-associated adaptor protein ALIX.

23 l that the machinery of endosomal fusion and ESCRT proteins has similar temporal localization on endo

24 east upon nutrient starvation in a Grh1- and ESCRT-I-, -II-, and -III-dependent process.

25 peration of HD-PTP with ESCRT-0, ESCRT-I and ESCRT-III and support a model for regulation of ESCRT fu

26 nce (RNAi) assays, we found that ESCRT-I and ESCRT-III complexes are required for efficient entry of

27 this study, we demonstrated that ESCRT-I and ESCRT-III complexes are required for efficient entry of

28 (DN) forms of the components of ESCRT-I and ESCRT-III complexes, entering virions were partially tra

29 d DNA that expressed DN forms of ESCRT-I and ESCRT-III components.

30 ting complexes required for transport I) and ESCRT-III proteins and the viral RNA in tombusvirus repl

31 vivo and assayed the ability of retromer and ESCRT microdomains to regulate one another.

32 regulatory interactions between retromer and ESCRT that balance degradative and recycling functions.

33 s turnover by the ubiquitin ligase Rsp5p and ESCRT attenuated the filamentous-growth pathway.

34 components of ESCRT-I (Tsg101 and Vps28) and ESCRT-III (Vps2B, Vps20, Vps24, Snf7, Vps46, and Vps60)

35 continuous, stochastic exchange of Vps4 and ESCRT-III components, rather than steady growth of fixed

36 -I) component ELCH (ELC) and is localized at ESCRT-I-positive late endosomes likely through its PI3P

37 show that ESCRT-II and the ESCRT-II-binding ESCRT-III subunit CHMP6 cooperate with ESCRT-I to recrui

38 r thrombin, independent of ubiquitin-binding ESCRTs and receptor ubiquitination.

39 ike kinase 3 (ULK3) phosphorylates and binds ESCRT-III subunits via tandem MIT domains, and thereby,

40 tein interfaces halt Snf7 assembly and block ESCRT function.

41 e binding sequence, and the presence of both ESCRT-III and microtubule binding elements may underlie

42 lar membrane fission reactions are driven by ESCRT pathways, which culminate in disassembly of ESCRT-

43 dissected the functions of co-opted cellular ESCRT-I (endosomal sorting complexes required for transp

44 to bushy stunt virus (TBSV) co-opts cellular ESCRT (endosomal sorting complexes required for transpor

45 that Vps4, the key regulator of the cellular ESCRT machinery, is necessary for efficient entry and eg

46 We show that in Saccharomyces cerevisiae, ESCRT-III complexes are stabilized and ILV membrane scis

47 teraction with activated PAR1 and the CHMP4B ESCRT-III subunit, suggesting that ARRDC3 regulates ALIX

48 hanism of ALIX regulation in three classical ESCRT-mediated processes revealed that phosphorylation o

49 Our analysis suggests how common ESCRT-III filament architectures could stabilize differe

50 ans coelomocyte, we visualized complementary ESCRT-0 and RME-8/SNX-1 microdomains in vivo and assayed

51 The assembly of the core ESCRT-III subunit CHMP4B/Snf7 is preferentially nucleate

52 Under conditions of necroptotic cell death, ESCRT-III controls the duration of plasma membrane integ

53 odels in the context of prior work detailing ESCRT machinery and the HIV-1 release process.

54 The ATPase Vps4 remodels and disassembles ESCRT-III, but the manner in which Vps4 activity is coor

55 rane fission by remodeling and disassembling ESCRT-III filaments.

56 s of maturation including anillin dispersal, ESCRT-III recruitment, and the formation of microtubule

57 Separation of the functionally distinct ESCRT-0 and SNX-1/RME-8 microdomains was also compromise

58 tor that recruits Cmp7p/CHMP7 and downstream ESCRT factors to the nuclear envelope.

59 utations also prevent assembly of downstream ESCRT-III components at the reforming NE and proper esta

60 These actions recruit the downstream ESCRT machinery to SV pools, thereby initiating SV prote

61 model in which Ist1-Did2 interactions during ESCRT-III polymerization coordinate Vps4 activity with t

62 The early ESCRTs (ESCRT-0 and -I) are likely involved in cargo sor

63 s cargo sorting mediated by one of the early ESCRTs.

64 ating and regulatory receptors via endosomal ESCRT sorting.

65 sed the molecular architecture of the entire ESCRT binding region of HD-PTP using small angle X-ray s

66 The early ESCRTs (ESCRT-0 and -I) are likely involved in cargo sorting, wh

67 ur findings underscore essential actions for ESCRT-III in membrane remodeling, cargo selection, and c

68 , suggesting novel regulatory mechanisms for ESCRT-mediated NE modulation.

69 finement, we propose a new working model for ESCRT-mediated HIV-1 release that reconciles disparate a

70 s to provide a range of potential models for ESCRT-mediated virus abscission.

71 Acb1 secretion that reveals requirements for ESCRT-I, -II, and -III but, surprisingly, without the in

72 I domain, suggesting interplay with the host ESCRT system.

73 However, how ESCRT-III activation is coordinated by the upstream ESCR

74 However, ESCRT assembly, regulation, and function are complex, an

75 al copolymer composed of two different human ESCRT-III subunits, charged multivesicular body protein

76 AL SORTING COMPLEX REQUIRED FOR TRANSPORT I (ESCRT-I) component ELCH (ELC) and is localized at ESCRT-

77 al-sorting complex required for transport I (ESCRT-I).

78 el ubiquitin-dependent pathways: the ESCRT-I-ESCRT-II-Vps20 pathway and the ESCRT-0-Bro1 pathway.

79 nuclear membrane proteins, and the ESCRT-II/ESCRT-III hybrid protein Cmp7p (CHMP7), work together to

80 orting complexes required for transport III (ESCRT III) machinery.

81 orting complexes required for transport III (ESCRT-III) proteins have been implicated in sealing the

82 sorting complex required for transport III (ESCRT-III) subunits polymerize on endosomal membranes to

83 sorting complex required for transport III (ESCRT-III)-associated proteins.

84 sorting complex required for transport-III (ESCRT-III) machinery has recently been shown to seal hol

85 sorting complex required for transport-III (ESCRT-III) machinery localizes to sites of annular fusio

86 while crescent-like structures are formed in ESCRT-III deletion yeasts replicating TBSV RNA.

87 We characterize novel mutations in ESCRT-III Snf7 that trigger activation, and identify a n

88 on of Gag (p6(Gag)), plays a central role in ESCRT recruitment to the site of virus budding.

89 busvirus-induced spherule-like structures in ESCRT-I or ESCRT-III deletion yeasts replicating TBSV RN

90 or transport (ESCRT) proteins, which include ESCRT-0, -I, -II, and -III, play a central role in endos

91 stranded RNA (dsRNA) targeting an individual ESCRT-I or ESCRT-III gene and viral bacmid DNA or viral

92 nits polymerize into spirals, how individual ESCRT-III subunits are activated and assembled together

93 ESCRT-II links these functions by initiating ESCRT-III formation in an ESCRT-I-regulated manner.

94 to sites of NPC assembly is mediated by its ESCRT-II domain and the LAP2-emerin-MAN1 (LEM) family of

95 tion that renders ALIX unable to perform its ESCRT functions.

96 The major ESCRT-III subunit Snf7 localizes transiently to CUPS and

97 ARMMs, including ARRDC1, TSG101 and multiple ESCRT complex proteins.

98 tor protein ALIX is a key player in multiple ESCRT-III-mediated membrane remodeling processes.

99 l for concomitant interactions with multiple ESCRTs, which contrasts with the compact conformation of

100 body (MVB) pathway using a dominant negative ESCRT (endosomal sorting complexes required for transpor

101 We found that ESCRT-III components (but not ESCRT-I components) are required for efficient nuclear e

102 We demonstrate that ESCRT-0, but not ESCRT-I or ESCRT-II, is able to associate stably with th

103 The components of ESCRT-III (but not ESCRT-I) are also necessary for efficient nuclear egress

104 Surprisingly, in the absence of ESCRT function in C. elegans, cytokinetic abscission is

105 As a consequence of the action of ESCRT-III, cells undergoing necroptosis can express chem

106 nated cargo and organizing the activities of ESCRT.

107 monstrate the plasma membrane association of ESCRT protein Hrs during macropinocytosis and suggest th

108 orting (Vps) protein Vps27 is a component of ESCRT-0 involved in the multivesicular body (MVB) sortin

109 Another component of ESCRT-0, the FgVps27-interacting partner FgHse1, also pl

110 In this study, the core components of ESCRT-I (Tsg101 and Vps28) and ESCRT-III (Vps2B, Vps20,

111 ant negative (DN) forms of the components of ESCRT-I and ESCRT-III complexes, entering virions were p

112 The components of ESCRT-III (but not ESCRT-I) are also necessary for effic

113 ound to interact with Vps4 and components of ESCRT-III, and these interactions may suggest the format

114 Ac146) interact with Vps4 and components of ESCRT-III.

115 Likewise, depletion of ESCRT-0 components Hrs or Stam in combination with Rme-8

116 to the cycle of assembly and disassembly of ESCRT-III complexes at membranes.

117 pathways, which culminate in disassembly of ESCRT-III polymers by the AAA ATPase Vps4.

118 ulation of ESCRT function by displacement of ESCRT subunits, which is crucial in determining the fate

119 ved, we used siRNA to suppress expression of ESCRT (endosomal sorting complex required for transport)

120 viral bacmid DNA that expressed DN forms of ESCRT-I and ESCRT-III components.

121 cargo deubiquitination at the initiation of ESCRT-III complex assembly.

122 While NE localization of ESCRT-III is dependent upon the ESCRT-III component CHMP

123 C-terminal MIT-interacting motifs (MIMs) of ESCRT-III subunits, but it is unclear how the enzyme the

124 Perturbations of ESCRT proteins have a selective effect on long-range Hh

125 vides a platform to direct NE recruitment of ESCRT-III during mitotic exit.

126 ur work reveals a two-pronged recruitment of ESCRT-III to the cytokinetic bridge and implicates ALIX

127 RT-III and support a model for regulation of ESCRT function by displacement of ESCRT subunits, which

128 An all-or-none step led to final release of ESCRT-III and Vps4.

129 Although the role of ESCRT protein Hrs has been extensively studied with resp

130 Here, we examined the role of ESCRT-0 component Hrs (hepatocyte growth factor-regulate

131 y, we determined X-ray crystal structures of ESCRT-III subunit Snf7, the yeast CHMP4 ortholog, in its

132 a4 binding to Vps20, which is the subunit of ESCRT-III that initiates assembly of the complex.

133 se results indicate that the two subunits of ESCRT-0 function together to bind and sequester cargoes

134 coordinate Vps4 activity with the timing of ESCRT-III disassembly.

135 a biophysical explanation for the timing of ESCRT-III recruitment and membrane scission in HIV-1 bud

136 o be important for determining the timing of ESCRT-III-mediated membrane scission.

137 are important in the physiological roles of ESCRTs and Akt.

138 ation of Hh regulates the secretion of Hh on ESCRT-derived exovesicles, which in turn act as a vehicl

139 demonstrate that ESCRT-0, but not ESCRT-I or ESCRT-II, is able to associate stably with the mono-ubiq

140 duced spherule-like structures in ESCRT-I or ESCRT-III deletion yeasts replicating TBSV RNA, demonstr

141 A (dsRNA) targeting an individual ESCRT-I or ESCRT-III gene and viral bacmid DNA or viral bacmid DNA

142 of stimulating Vps4 in the context of other ESCRT-III subunits.

143 , allows the recruitment of Tsg101 and other ESCRTs to virus assembly sites where they mediate buddin

144 n a manner regulated by Ist1, which promotes ESCRT-III assembly and inhibits the incorporation of ups

145 Our findings show that the Rab35/ESCRT pathway facilitates the activity-dependent removal

146 rate but redundant pathways exist to recruit ESCRT-III proteins to the midbody.

147 quitinated vacuole membrane proteins recruit ESCRTs to the vacuole surface, where they mediate cargo

148 ress complex" that is involved in recruiting ESCRT-III components to a virus egress domain on the nuc

149 ar mechanisms that enable HD-PTP to regulate ESCRT function are unknown.

150 est the role of membrane shape in regulating ESCRT assembly, we nanofabricated templates for invagina

151 with the compact conformation of the related ESCRT regulator Alix.

152 of Acb1 in Saccharomyces cerevisiae requires ESCRT-I, -II, and -III and Grh1.

153 rt)-interacting motifs of CHMP5 and a second ESCRT-III protein, CHMP1B, was determined at 1 A resolut

154 examers (four or more) draw together several ESCRT-III filaments.

155 unctional divergence of structurally similar ESCRT-III subunits.

156 ing the details of participation of specific ESCRT complexes in AcMNPV infection.

157 little is known about the roles of specific ESCRT complexes in AcMNPV infection.

158 Here we have analysed the role of specific ESCRT components in HPV infection, and we find an essent

159 alphai or PI3K signaling and siRNA targeting ESCRTs blocks CXCR4-promoted degradation of DEPTOR, an e

160 rine and threonine content, and a C-terminal ESCRT-III domain, suggesting interplay with the host ESC

161 RNAi depletion studies confirmed that ESCRT-III proteins, particularly CHMP2A, function in eHA

162 Further, we demonstrate that ESCRT-0 component Hrs is an effector of Rab35, thus prov

163 We demonstrate that ESCRT-0, but not ESCRT-I or ESCRT-II, is able to associa

164 In this study, we demonstrated that ESCRT-I and ESCRT-III complexes are required for efficie

165 uired for transport) proteins and found that ESCRT II and IV significantly control exosome release.

166 NA interference (RNAi) assays, we found that ESCRT-I and ESCRT-III complexes are required for efficie

167 We found that ESCRT-III components (but not ESCRT-I components) are re

168 Overall, our results indicate that ESCRT-0 components play critical roles in a variety of c

169 Using an elastic model, we show that ESCRT protein shapes are sufficient to spontaneously cre

170 Here, we show that ESCRT-II and the ESCRT-II-binding ESCRT-III subunit CHMP

171 Here, we showed that ESCRT is required for optimal antigen processing; corres

172 e light-sheet microscopy, we have shown that ESCRT-III subunits polymerize rapidly on yeast endosomes

173 Current models suggest that ESCRT-III complexes surround ubiquitinated cargoes to tr

174 The ESCRT machinery is one such component that seems to play

175 The ESCRT machinery mediates reverse membrane scission.

176 The ESCRT proteins are an ancient system that buds membranes

177 The ESCRT-III component charged multivesicular body protein

178 The ESCRT-III core protein Shrub has a central role in endos

179 The ESCRT-III machinery is required for formation of these b

180 The ESCRT-III subunit CHMP4B is a key effector in abscission

181 e of the major mechanisms that activates the ESCRT function of ALIX.

182 esis remains poorly understood, although the ESCRT-binding protein ALIX has been implicated.

183 ytokinesis, mediated by both dynamin and the ESCRT (endosomal sorting complex required for transport)

184 by LAPTM4B, PtdIns(4,5)P2 signaling, and the ESCRT complex and define a mechanism by which the oncopr

185 ents of the PtdIns 3-kinase complex, and the ESCRT machinery.

186 microtubule-severing enzyme spastin and the ESCRT protein IST1 at ER-endosome contacts drives endoso

187 : the ESCRT-I-ESCRT-II-Vps20 pathway and the ESCRT-0-Bro1 pathway.

188 Here, we show that ESCRT-II and the ESCRT-II-binding ESCRT-III subunit CHMP6 cooperate with

189 of inner nuclear membrane proteins, and the ESCRT-II/ESCRT-III hybrid protein Cmp7p (CHMP7), work to

190 on mechanism that relies on Aurora B and the ESCRT-III subunit CHMP4C to delay abscission in response

191 h2 and the "open" forms of both Chm7 and the ESCRT-III, Snf7, and between Chm7 and Snf7.

192 rongest interaction with LIP5, SKD1, and the ESCRT-III-related proteins CHMP1A in yeast two hybrid as

193 ntal structure-function relationships at the ESCRT-HIV-1 interface.

194 e molecular interplay among viral BFRF1, the ESCRT adaptor Alix, and the ubiquitin ligase Itch.

195 d endosomal recruitment are regulated by the ESCRT components LIP5 and IST1.

196 ing by enabling Chs3 to be recognized by the ESCRT machinery and degraded in the vacuole.

197 V formation are directed specifically by the ESCRT-III complex in vivo in a manner regulated by Ist1,

198 ordered N-terminal domain to destabilize the ESCRT-III lattice.

199 tein structures, with Vps4 disassembling the ESCRT-III polymers that are central to the many membrane

200 Our results describe a novel role for the ESCRT machinery in cell division and demonstrate a conse

201 Our data reveal a novel role for the ESCRT pathway in promoting intracellular signaling, whic

202 of viral budding, replacing the need for the ESCRT proteins that other viruses utilize.

203 these data support an important role for the ESCRT-I complex in the regulation of productive free upt

204 However, the ESCRT-III/Vps4 system alone is not sufficient for ILV fo

205 ectosomes, thereby generally implicating the ESCRT machinery in EV biogenesis.

206 omain on the nuclear membrane.IMPORTANCE The ESCRT system is hijacked by many enveloped viruses to me

207 Here, we study the effects of inhibiting the ESCRT-associated AAA+ ATPase VPS4 on EV release from cul

208 covered a novel role for its interactor, the ESCRT-I protein TSG101: it directly participates in miti

209 During their 3-45 s lifetimes, the ESCRT-III assemblies accumulated 75-200 Snf7 and 15-50 V

210 e many membrane-remodeling activities of the ESCRT (endosomal sorting complexes required for transpor

211 We found that 50% of the ESCRT cargo would escape from a single budding profile i

212 clear envelope formation, recruitment of the ESCRT factors CHMP7, CHMP2A, and IST1/CHMP8 all depend o

213 tion, can also target the degradation of the ESCRT protein-charged multivesicular body protein (CHMP2

214 Disruption of the ESCRT transport system also resulted in increased exocyt

215 Vps4, the key regulator for recycling of the ESCRT-III complex, is required for efficient infection b

216 Further, depletion of the ESCRT-III component and Aurora B substrate CHMP4C enable

217 ssion, where it catalyzes disassembly of the ESCRT-III lattice.

218 Addition of the ESCRT-III subunit binding partner of Ist1, Did2, also co

219 o parallel ubiquitin-dependent pathways: the ESCRT-I-ESCRT-II-Vps20 pathway and the ESCRT-0-Bro1 path

220 -Barr virus (EBV) BFRF1 protein recruits the ESCRT-associated protein Alix to modulate NE structure a

221 step in cellular processes that require the ESCRT function.

222 These results demonstrate that the ESCRT machinery, and in particular VPS4, plays a critica

223 These data suggest that the ESCRT proteins mediate ectosome release and thereby infl

224 Here, we show that the ESCRT-II/III chimera, Chm7, is recruited to a nuclear en

225 ts may underlie the recent findings that the ESCRT-III disassembly function of Vps4 and the microtubu

226 ole as a diffusion barrier, we find that the ESCRT-III protein SNF7 remains associated with ILVs and

227 udy links the BAR protein superfamily to the ESCRT pathway for MP biogenesis in mammalian cardiac ven

228 induces Rab35 activation and binding to the ESCRT-0 protein Hrs, which we have identified as a novel

229 alization of ESCRT-III is dependent upon the ESCRT-III component CHMP7 [3], it is unclear how this co

230 n into Rab5-positive early endosomes via the ESCRT machinery.

231 alpha-syn, which is transported via the ESCRT pathway through multivesicular bodies for degradat

232 by initiating SV protein degradation via the ESCRT pathway.

233 ocytic adaptor that also associates with the ESCRT-0 complex members HRS and STAM on endosomes.

234 )L/I consensus motif that interacts with the ESCRT-III protein Alix.

235 barrier relies on membrane remodeling by the ESCRTs, which seal nuclear envelope holes and contribute

236 Three "classical" functions of the ESCRTs have dominated research into these proteins since

237 Our findings demonstrate that the ESCRTs can function at both the late endosome and the va

238 ough the kinetics seems to be delayed due to ESCRT deletion.

239 Ist1 is structurally homologous to ESCRT-III subunits and has been reported to inhibit Vps4

240 a wide variety of proteins that localize to ESCRT-III polymers.

241 omal sorting complex required for transport (ESCRT) [10-12], small GTPases, and ubiquitinated protein

242 omal sorting complex required for transport (ESCRT) activity and regulated by neuronal activity.

243 omal sorting complex required for transport (ESCRT) and are implicated in intracellular trafficking.

244 omal sorting complex required for transport (ESCRT) machinery and SV-associated GTPase Rab35 are key

245 omal sorting complex required for transport (ESCRT) machinery during budding.

246 omal sorting complex required for transport (ESCRT) machinery from biological membranes is a critical

247 al sorting complexes required for transport (ESCRT) machinery functions in HIV-1 budding, cytokinesis

248 omal sorting complex required for transport (ESCRT) machinery into endosome intralumenal vesicles (IL

249 omal sorting complex required for transport (ESCRT) machinery is necessary for budding of many envelo

250 omal sorting complex required for transport (ESCRT) machinery is purposely disengaged.

251 omal sorting complex required for transport (ESCRT) machinery is required for the nuclear egress of E

252 al sorting complexes required for transport (ESCRT) machinery mediates the physical separation betwee

253 omal sorting complex required for transport (ESCRT) machinery play essential roles in topologically e

254 omal sorting complex required for transport (ESCRT) machinery responsible for sorting ubiquitinated r

255 omal sorting complex required for transport (ESCRT) machinery to facilitate the release of viral part

256 omal sorting complex required for transport (ESCRT) machinery to SV pools.

257 omal sorting complex required for transport (ESCRT) machinery, which selectively targets ubiquitin-mo

258 al sorting complexes required for transport (ESCRT) machinery.

259 omal sorting complex required for transport (ESCRT) machinery.

260 omal sorting complex required for transport (ESCRT) machinery.

261 omal sorting complex required for transport (ESCRT) machinery.

262 omal sorting complex required for transport (ESCRT) machinery.

263 al sorting complexes required for transport (ESCRT) pathway facilitates multiple fundamental membrane

264 omal sorting complex required for transport (ESCRT) pathway on the propagation of alpha-syn.

265 omal Sorting Complex Required for Transport (ESCRT) pathway.

266 of ENDOSOMAL COMPLEX REQUIRED FOR TRANSPORT (ESCRT) protein complexes.

267 omal sorting complex required for transport (ESCRT) proteins are recruited to the midbody and direct

268 al sorting complexes required for transport (ESCRT) proteins mediate fundamental membrane remodeling

269 al sorting complexes required for transport (ESCRT) proteins, which include ESCRT-0, -I, -II, and -II

270 omal sorting complex required for transport (ESCRT) was recently found to mediate important morphogen

271 al sorting complexes required for transport (ESCRT) were also associated with the TZs.

272 al Sorting Complexes Required for Transport (ESCRT), which target ubiquitylated receptors to intra-lu

273 al sorting complexes required for transport (ESCRT)-0 component Hrs [hepatocyte growth factor-regulat

274 omal Sorting Complex Required for Transport (ESCRT)-III proteins mediate membrane remodeling and the

275 al sorting complexes required for transport (ESCRT)-III subunit charged multivesicular body protein 4

276 omal sorting complex required for transport (ESCRT).

277 al sorting complexes required for transport (ESCRT-III) polymers from cellular membranes.

278 omal-sorting-complex-required-for-transport (ESCRT) protein CHMP5, known to be required for the forma

279 al sorting complexes required for transport (ESCRTs) constitute hetero-oligomeric machines that catal

280 al sorting complexes required for transport (ESCRTs) to bud virions from the membrane.

281 al sorting complexes required for transport (ESCRTs).

282 Knockdown of two ESCRT-related proteins, PDCD6 and VPS4, attenuated ectos

283 better understand the mechanisms underlying ESCRT-mediated formation of ILVs, we exploited the rapid

284 g for the activation of the spatially unique ESCRT-III-mediated membrane remodeling.

285 s crucial insights into the spatially unique ESCRT-III-mediated membrane remodeling.

286 y and inhibits the incorporation of upstream ESCRT components into ILVs.

287 II activation is coordinated by the upstream ESCRT components at endosomes remains unclear.

288 We show that upstream ESCRTs regulate Snf7 activation at both its N-terminal c

289 r MsVps4 assembly, ATPase activity in vitro, ESCRT-III disassembly in vitro and HIV-1 budding.

290 e-deletion mutant, we showed that the Vps23p ESCRT-I protein (Tsg101 in mammals) and Bro1p (ALIX) ESC

291 al role of Snf7p (CHMP4), Vps20p, and Vps24p ESCRT-III proteins in tombusvirus replication in yeast a

292 intraluminal vesicles with the help of Vps4, ESCRT-III/Snf7 promotes direct engulfment of preexisting

293 re likely involved in cargo sorting, whereas ESCRT-III and Vps4 function to sever the neck of the for

294 nding ESCRT-III subunit CHMP6 cooperate with ESCRT-I to recruit CHMP4B, with ALIX providing a paralle

295 r in which Vps4 activity is coordinated with ESCRT-III function remains unclear.

296 nding domain of Raf also coprecipitates with ESCRT (endosomal sorting complex required for transport)

297 that associates with MVB by interacting with ESCRT-III subunit SNF7 and mediates PHT1;1 trafficking t

298 se the functional cooperation of HD-PTP with ESCRT-0, ESCRT-I and ESCRT-III and support a model for r

299 Recent experimental results with ESCRT proteins reveal a novel budding mechanism, with pr

300 terious spiral filaments formed by the yeast ESCRT-III protein Snf7.