ライフサイエンスコーパス: 26S proteasome

1 in a retardation of ABI5 degradation by the 26S proteasome.

2 ed RRB, by preventing its degradation by the 26S proteasome.

3 as a ubiquitin-independent substrate of the 26S proteasome.

4 tor Rpn13, thereby defining asymmetry in the 26S proteasome.

5 ed for degradation of tubulin, likely by the 26S proteasome.

6 peptides for the chaperonin TRiC/CCT and the 26S proteasome.

7 he ACS proteins for rapid degradation by the 26S proteasome.

8 of ubiquitin, are ultimately degraded by the 26S proteasome.

9 is via the SCF(SLY1) E3 ubiquitin ligase and 26S proteasome.

10 addition commits many to degradation by the 26S proteasome.

11 actions and Rpt(1-6)-20S interactions in the 26S proteasome.

12 dependent and -independent substrates of the 26S proteasome.

13 the Keap1-Cul3 E3 ligase and degraded by the 26S proteasome.

14 polyubiquitinated, and then degraded by the 26S proteasome.

15 quitylation and selective proteolysis by the 26S proteasome.

16 basis for a mechanistic understanding of the 26S proteasome.

17 construct a molecular model of the complete 26S proteasome.

18 itination and degradation of Exo70B2 via the 26S Proteasome.

19 o the cytosol where they are degraded by the 26S proteasome.

20 uitination and subsequent degradation by the 26S proteasome.

21 ose a model for polyubiquitin binding to the 26S proteasome.

22 uperior inhibitory activity against cellular 26S proteasome.

23 d mouse brains, suggesting impairment of the 26S proteasome.

24 hereby targeting them for degradation by the 26S proteasome.

25 the pathogen effector HopM1 through the host 26S proteasome.

26 degradation of cell-cycle regulators by the 26S proteasome.

27 ough their delivery of UPS substrates to the 26S proteasome.

28 its the deubiquitinating enzyme UCH37 to the 26S proteasome.

29 micin, indicating that it is degraded by the 26S proteasome.

30 substrates many of which are degraded by the 26S proteasome.

31 in degradation of the target protein in the 26S proteasome.

32 Degradation of Sml1 is dependent on the 26S proteasome.

33 ubiquitinated in planta and degraded by the 26S proteasome.

34 various layers of receptors upstream to the 26S proteasome.

35 own for targeting protein destruction by the 26S proteasome.

36 f proteins leads to their degradation by the 26S proteasome.

37 M) protein present in the cytosol and in the 26S proteasome.

38 signaling components for degradation by the 26S proteasome.

39 ine can influence substrate targeting to the 26S proteasome.

40 transactivator complex by the ATPases of the 26S proteasome.

41 They are degraded by the ubiquitin-dependent 26S proteasome.

42 ondria and its subsequent degradation by the 26S proteasome.

43 the protein interaction network of the yeast 26S proteasome.

44 e lysine 63 residues that are insensitive to 26S proteasome.

45 nals that are subsequently recognized by the 26S proteasome.

46 of TIMING OF CAB EXPRESSION 1 (TOC1) by the 26S proteasome.

47 n a retardation of SlGLK2 degradation by the 26S proteasome.

48 achinery to clear protein aggregates via the 26S proteasome.

49 (an E3 ubiquitin ligase) and degraded by the 26S proteasome.

50 ivities that direct proteolysis, such as the 26S proteasome.

51 that targets proteins for degradation by the 26S proteasome.

52 elongation and is gradually degraded by the 26S proteasome.

53 ligase complex, and their degradation by the 26S proteasome.

54 to the subsequent destruction of p53 by the 26S proteasome.

55 n-independent proteolytic destruction by the 26S proteasome.

56 o degradation mechanisms such as VCP and the 26S proteasome.

57 ec3 degradation is regulated by Pib1 and the 26S proteasome.

58 and Ubl binding to S5a is restricted to the 26S proteasome.

59 acterize the conformational landscape of the 26S proteasome.

60 ains that act as recognition signals for the 26S proteasome.

61 132, indicating the requirement of UBC24 and 26S proteasomes.

62 ssociation of ubiquitin (Ub) conjugates with 26S proteasomes.

63 nd each requires the other for assembly into 26S proteasomes.

64 red mouse and human hepatocytes, and 20S and 26S proteasomes.

65 slocates into nuclei and becomes degraded by 26S proteasomes.

66 UbcH5, resist degradation and disassembly by 26S proteasomes.

67 article triple-A ATPases (Rpt) of eukaryotic 26S proteasomes.

68 prior to their degradation, requires intact 26S proteasomes.

69 icroscopy structures of both human and yeast 26S proteasomes.

70 gase (HRD-ligase), and degraded by cytosolic 26S proteasomes.

71 vels also increased amounts of doubly capped 26S proteasomes.

72 The 26S proteasome, a molecular machine responsible for regu

73 e ubiquitin-proteasome system by eliminating 26S proteasomes, a process we termed proteaphagy.

74 0 and Rpn13 mapped to the apical part of the 26S proteasome, above the N-terminal coiled coils of the

75 tive photomorphogenic 1 (COP1) E3 ligase and 26S proteasome accompanied the loss of longitudinal F-ac

76 We identified Rpn6-dependent 26S proteasome activation as an essential feature of myo

77 roteasome-specific inhibitors both decreased 26S proteasome activities and prevented C2C12 differenti

78 The major finding was that 20S and 26S proteasome activities were significantly elevated (1

79 e AAA ATPase (RPT2a) causes a weak defect in 26S proteasome activity and leads to an enlargement of l

80 toward tumor vs normal cells, inhibition of 26S proteasome activity associated with endoplasmic reti

81 Here, we show that ADP-ribosylation promotes 26S proteasome activity in both Drosophila and human cel

82 Previous studies have demonstrated that 26S proteasome activity is diminished in human end-stage

83 Moreover, specific inhibition of 26S proteasome activity via siRNA-mediated knockdown of

84 PKalpha2(-/-) mice, which exhibited elevated 26S proteasome activity, had reduced levels of GTPCH I a

85 ockout (LDLr(-/-)) strain markedly increased 26S proteasome activity, IkappaB degradation, NF-kappaB

86 (P)H oxidase-mediated superoxide production, 26S proteasome activity, IkappaBalpha degradation, and n

87 (P)H oxidase-mediated superoxide production, 26S proteasome activity, IkappaBalpha degradation, and n

88 at highly aggregated proteins interfere with 26S proteasome activity.

89 of AMPK inhibited the high-glucose-enhanced 26S proteasome activity.

90 The newly identified NADH binding of 26S proteasomes advances our understanding of the molecu

91 ity of cellular proteins are degraded by the 26S proteasome after their ubiquitination.

92 that the non-proteolytic 19S subunit of the 26S proteasome also regulates the spreading of inactive

93 ed various cofactors that associate with the 26S proteasome and appear to influence its function.

94 involves Med13p destruction mediated by the 26S proteasome and cyclin C-Cdk8p kinase activity.

95 tress-induced molecular changes of the human 26S proteasome and determined that stress-induced 26S pr

96 regulatory element binding protein-1 through 26S proteasome and Erk1/2-dependent mechanisms.

97 zomib is a highly selective inhibitor of the 26S proteasome and has been approved for clinical use in

98 Activation of the 26S proteasome and increased expression of Rpn6 were det

99 UBLCP1 dephosphorylates the 26S proteasome and inhibits proteasome activity in vitro

100 ARF1-mediated GA perception and a functional 26S proteasome and involves the basic helix-loop-helix p

101 b is a selective and potent inhibitor of the 26S proteasome and is approved for the treatment of mult

102 ion requires incorporation of Rpn11 into the 26S proteasome and is dependent on ATP hydrolysis, sugge

103 measuring chymotrypsin-like activity of the 26S proteasome and messenger RNA expressions of muscle-s

104 biquitin on mitochondria, recruitment of the 26S proteasome and rapid degradation of multiple outer m

105 ailed description of the 20S core within the 26S proteasome and redefines the overall assignment of s

106 int to a specific role for RPN5 in the plant 26S proteasome and suggest that its two paralogous genes

107 two large and very different complexes, the 26S proteasome and the INO80 chromatin remodeler.

108 loped a method to gently and rapidly isolate 26S proteasomes and associated proteins without the need

109 nto cells results in reduced NADH-stabilized 26S proteasomes and decreased viability following redox

110 the diversity, functions, and regulation of 26S proteasomes and p97 complexes under different condit

111 involve singlet oxygen, ubiquitination, the 26S proteasome, and cellular degradation machinery.

112 bule stabilizing protein, is degraded by the 26S proteasome, and its degradation rate is accelerated

113 , enzymatic digestion and degradation by the 26S proteasome, and lead to lower neuronal damage and re

114 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar proteolytic pathway.

115 Thus, the double-capped 26S proteasomes are asymmetric in their polyubiquitin bi

116 Secondly, we established that 26S proteasomes are disassembled with a decline in activ

117 ely stabilized by MG132, an inhibitor of the 26S proteasome, as are the levels of expressed enhanced

118 uses degradation of their substrates via the 26S proteasome, as demonstrated for the wrinkled1 ERF/AP

119 Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear

120 w that this subunit plays a critical role in 26S proteasome assembly, histone dynamics, and plant dev

121 EM structure of the Saccharomyces cerevisiae 26S proteasome at a resolution of 7.4 A or 6.7 A (Fourie

122 However, pure 26S proteasomes bind and degrade K48- and K63-ubiquitina

123 t majority (if not all) of the double-capped 26S proteasomes, both 19S complexes, contain the ubiquit

124 Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol.

125 or Escherichia coli was not degraded by the 26S proteasome, but by its catalytic 20S core particle,

126 cells target proteins for degradation by the 26S proteasome by attaching a ubiquitin chain.

127 Turnover of the 26S proteasome by autophagy is an evolutionarily conserv

128 The inhibition of the 26S proteasome by Bortezomib leads to the accumulation o

129 e have determined the structure of the human 26S proteasome by electron microscopy and single particl

130 e base of the 19S regulatory particle of the 26S proteasome by identifying new precursor complexes an

131 Inhibition of the human 20S and 26S proteasome by these derivatives using an enzymatic a

132 igase regulates substrate recruitment to the 26S proteasome by ubiquitinating Rpn10, the proteasome's

133 odulation of the conformational space of the 26S proteasome by Ubp6 explains the effects of Ubp6 on t

134 ive autophagy receptor that targets inactive 26S proteasomes by concurrent interactions with ubiquity

135 Activities of the 20S and 26S proteasomes, calpain and cathepsin L, were measured

136 Moreover, ubiquitination of the 26S proteasome can be antagonized by proteasome-residing

137 rs reveals that 20 of the 33 subunits of the 26S proteasome can be cut by caspases, and we demonstrat

138 The 26S proteasome can be divided into two subcomplexes: the

139 that induce proteotoxic stress by impairing 26S proteasome capacity, we defined the transcriptional

140 the autophagy pathway, and inhibition of the 26S proteasome completely abrogates Parkin-mediated mito

141 The 26S proteasome complex (26S PC) integrity and function h

142 it PSMD12 (aka RPN5) of the 19S regulator of 26S proteasome complex, in unrelated individuals with in

143 utation in the alpha subunit F (PAF1) of the 26S proteasome complex.

144 y regulatory particles (RPs) constitutes the 26S proteasome complex.

145 autoregulatory de novo formation of 20S and 26S proteasome complexes.

146 uitment of preexisting activators to 20S and 26S proteasome complexes.

147 lysis of the relative locations of TPPII and 26S proteasomes confirmed the visual impression that the

148 The regulatory particle (RP) of the 26S proteasome contains a heterohexameric ring of AAA-AT

149 omonas reinhardtii, we observed that nuclear 26S proteasomes crowd around NPCs.

150 d reduced incorporation of 19S subunits into 26S proteasomes, decreased chymotrypsin-like activity, a

151 The ubiquitin-26S proteasome degradation system (UPS) in plants is inv

152 in a manner independent of transcription and 26S proteasome degradation.

153 The 26S proteasome degrades polyubiquitylated substrates by

154 The 26S proteasome degrades ubiquitinated proteins, and prot

155 All these results suggest that ubiquitin/26S proteasome-dependent degradation of S-RNase may be a

156 is an unstable protein that is degraded in a 26S proteasome-dependent manner.

157 -deficient mutant (LT(Delta69-83)), impaired 26S proteasome-dependent proteolysis of the CRL7 target

158 Here we report the structure of the human 26S proteasome determined by cryo-electron microscopy an

159 roteasome and determined that stress-induced 26S proteasome disassembly is conserved from yeast to hu

160 o down-regulation of ubiquitinated-proteins, 26S proteasome disassembly, and a rise in 20S proteasome

161 ticle and the 19S regulatory particle in the 26S proteasome, disrupting the proteasome structure in r

162 This study examined the hypothesis that 26S proteasome dysfunction in human end-stage heart fail

163 itinated sperm mitochondrial proteins to the 26S proteasome, explaining how the whole sperm mitochond

164 cient for PSMC1, an essential subunit of the 26S proteasome, fail to produce proplatelets.

165 t help shuttle ubiquitylated proteins to the 26S proteasome for breakdown.

166 ubiquitin ligase complex and targeted to the 26S proteasome for degradation.

167 itin-dependent delivery of substrates to the 26S proteasome for proteolysis.

168 s activation enhances the selectivity of the 26S proteasome for ubiquitinated proteins and links thei

169 with the Rpt4 and Rpt5 ATPases and enhances 26S proteasome formation in vivo and in vitro.

170 calculated difference maps between wild-type 26S proteasome from Saccharomyces cerevisiae and deletio

171 26S proteasomes from mice with tauopathy were physically

172 26S proteasomes from normal mice incubated with recombin

173 Associated with 26S proteasomes from rat muscle were a variety of known

174 n to regulate survival protein stability and 26S proteasome function.

175 thus implicating RPT2 specifically, and the 26S proteasome generally, in plant nucleosome assembly.

176 The central protease of eukaryotes, the 26S proteasome, has a 20S proteolytic core particle (CP)

177 We show here that mammalian 26S proteasomes have five associated ubiquitin ligases a

178 decrease in the peptidase activity of brain 26S proteasomes, higher levels of ubiquitinated proteins

179 The 26S proteasome holocomplex consists of a core particle (

180 where 12 of the 33 subunits that make up the 26S proteasome holoenzyme are represented in the genome

181 incubation with polyubiquitinated proteins, 26S proteasomes hydrolyzed peptides and proteins 2- to 7

182 ediates the degradation of NPR1 via the host 26S proteasome in a manner dependent on AvrPtoB's E3 lig

183 in basic protein (MBP), is hydrolyzed by the 26S proteasome in a ubiquitin-independent manner both in

184 sible for stress-triggered remodeling of the 26S proteasome in human cells.

185 Based on the conformational ensemble of the 26S proteasome in solution, we propose a mechanistic mod

186 asis of the interaction between Ubp6 and the 26S proteasome in the presence and absence of the inhibi

187 aded in a TdRF1-dependent manner through the 26S proteasome in vivo, the mitogen-activated protein ki

188 DmPI31 can activate 26S proteasomes in vitro, and increasing DmPI31 levels s

189 To learn how the presence of Usp14 on 26S proteasomes influences its different activities, we

190 Endoplasmic reticulum stress (ERS) and 26S proteasome inhibition, also associated with s-IBM, p

191 asome-dependent protein degradation with the 26S proteasome inhibitor MG132 largely restored c-Jun pr

192 development of the first clinically approved 26S proteasome inhibitor, bortezomib (BZ).

193 formed nuclear bodies in the presence of the 26S-proteasome inhibitors that block blue light-dependen

194 Ubp6 favors conformational switching of the 26S proteasome into an intermediate-energy conformationa

195 The 26S proteasome is a 2.5 MDa molecular machine that execu

196 The 26S proteasome is a 2.5-MDa, 32-subunit ATP-dependent pr

197 The 26S proteasome is a 2.5-MDa, ATP-dependent multisubunit

198 Protein degradation by the 26S proteasome is a fundamental process involved in a br

199 The 26S proteasome is a large cellular assembly that mediate

200 The eukaryotic 26S proteasome is a large multisubunit complex that degr

201 The 26S proteasome is a large protease complex that degrades

202 The 26S proteasome is a multi-enzyme protease that degrades

203 The 26S proteasome is an essential multicatalytic protease c

204 The 26S proteasome is at the executive end of the ubiquitin-

205 adation of polyubiquitylated proteins by the 26S proteasome is essential for the maintenance of prote

206 In addition to its proteolytic roles, the 26S proteasome is involved in regulating transcription a

207 Interestingly, the 26S proteasome is mislocalized into foci, which are colo

208 In eukaryotic cells, the 26S proteasome is responsible for the regulated degradat

209 The 26S proteasome is responsible for the selective, ATP-dep

210 The 26S proteasome is the end point of the ubiquitin- and AT

211 The 26S proteasome is the major protein degradation machiner

212 The 26S proteasome is the primary machinery that degrades ub

213 Here we report that the human 26S proteasome is ubiquitinated, by which the ubiquitin

214 rotein, due to increased degradation via the 26S proteasome, is also required for adipocyte different

215 eukaryotic protease acting downstream of the 26S proteasome; it removes tripeptides from the degradat

216 sequently ubiquitinated and degraded via the 26S proteasome, leading to derepression of auxin respons

217 iate with, and regulate the function of, the 26S proteasome, leading us to hypothesize that induction

218 We provide evidence that BTS facilitates 26S proteasome-mediated degradation of PYEL proteins in

219 SLF targets non-self S-RNases for ubiquitin/26S proteasome-mediated degradation, thereby only allowi

220 ), with the latter event targeting phot1 for 26S proteasome-mediated degradation.

221 quitin chains that typically target them for 26S proteasome-mediated degradation.

222 vascular endothelial function by suppressing 26S proteasome-mediated GTPCH I degradation in diabetes.

223 Histone covalent modifications and 26S proteasome-mediated proteolysis modulate many regula

224 The 26S proteasome non-ATPase regulatory subunit 13 mediated

225 The structural features of the 26S proteasome observed in this study are likely to be i

226 The 26S proteasome operates at the executive end of the ubiq

227 adation of PIF1 and HFR1 is dependent on the 26S proteasome pathway in vivo Genetic evidence shows th

228 elf subject to degradation via the ubiquitin-26S proteasome pathway, and identify an 18 amino acid se

229 events rapid degradation of ACS2/ACS6 by the 26S proteasome pathway, resulting in an increase in cell

230 tination and degradation of Mad1 through the 26S proteasome pathway, which in turn promotes the trans

231 proteolytic turnover via the ubiquitination-26S proteasome pathway.

232 it is degraded under dark conditions via the 26S proteasome pathway.

233 ated ACS6 protein is rapidly degraded by the 26S proteasome pathway.

234 ved in protein degradation via the ubiquitin-26S proteasome pathway.

235 h which the SLF interacts, via the ubiquitin-26S proteasome pathway.

236 y degraded in the dark through the ubiquitin/26S-proteasome pathway and is stabilized by light.

237 -terminal domain phosphatase 1 (UBLCP1) is a 26S proteasome phosphatase that regulates nuclear protea

238 The 26S proteasome plays a fundamental role in eukaryotic ho

239 The 26S proteasome plays an essential role in regulating man

240 in complex that resembles the 19S lid of the 26S proteasome, plays a central role in the regulation o

241 accompanied by an increased ratio of 20S to 26S proteasomes, preservation of protein degradation cap

242 more, we found that MG 132, an inhibitor for 26S proteasome, preserved cardiac GCH1 proteins and amel

243 ia the autophagy pathway rather than through 26S proteasome proteolysis.

244 The modular structure of the 26S proteasome provides insights into the sequence of ev

245 26S proteasomes purified from these treated cells or fro

246 pared enzymatic and regulatory properties of 26S proteasomes purified from wild-type mouse embryonic

247 The 26S proteasome recognizes a vast number of ubiquitin-dep

248 e propose that in situ ubiquitination of the 26S proteasome regulates its activity, which could funct

249 ictions and distinct from the PCI-containing 26S proteasome regulatory particle subunit Rpn6 structur

250 y of 26S immunoproteasomes, but not standard 26S proteasomes, releasing the 20S catalytic immunoprote

251 Hsp90 inhibition suppresses 26S proteasome remodeling, unanchored ubiquitin chain pr

252 s show that initiation of degradation at the 26S proteasome requires a partially unfolded region to f

253 of complex structures such as the eukaryotic 26S proteasome requires intricate mechanisms that ensure

254 Two canonical subunits of the 26S proteasome, Rpn10 and Rpn13, function as ubiquitin (

255 of these subunits significantly impairs the 26S proteasome's ability to bind, deubiquitinate, and de

256 The 26S proteasome shows similar nucleotide dependence.

257 s not previously known to associate with the 26S proteasome, some of which were tightly associated wi

258 Further, 26S proteasomes specifically recognize and cleave IPSs a

259 review will summarize the recent findings on 26S proteasome structure and discuss the mechanistic imp

260 ion triggers the selective processing of the 26S proteasome subunit Rpn10.

261 a truncated dominant-negative variant of the 26S proteasome subunit, Rpt2, indicating that exocyst de

262 fied the Bcl2 family member MCL1 and several 26S proteasome subunits among the most important and sel

263 or dietary protein, as the activities of the 26S proteasome subunits beta1, beta2, and beta5 were low

264 Differences in the abundance of the key 26S proteasome subunits Rpt6 and beta5 between the PKG-m

265 es, channel proteins, ubiquitin ligases, and 26S proteasome subunits, thereby optimizing degradation

266 vival genes were constituents of the 20S and 26S proteasome subunits.

267 The ubiquitin (Ub)/26S proteasome system (UPS) directs the turnover of nume

268 Ubiquitin-26S proteasome system (UPS) has been shown to play centr

269 The critical role of the ubiquitin-26S proteasome system in regulation of protein homeostas

270 emoval of specific proteins by the ubiquitin-26S proteasome system is also likely paramount.

271 s well as candidates whose control by the Ub/26S proteasome system is not yet appreciated.

272 Rpn13, one of the ubiquitin receptors on the 26S proteasome that is nonessential for proteasome funct

273 In the eukaryotic 26S proteasome, the 20S particle is regulated by six AAA

274 The 26S proteasome, the central eukaryotic protease, compris

275 it complexes: the 19S (PA700) portion of the 26S proteasome, the COP9 signalosome (CSN) and a novel c

276 targeted protein is rapidly degraded by the 26S proteasome, the major proteolysis machinery in eukar

277 However, it is not clear how the 26S proteasome, the ubiquitin-dependent protease that is

278 rovide a link between NF-kappaB RelA and the 26S proteasome, thereby facilitating RelA protein degrad

279 DEPTOR stability is governed by the 26S-proteasome through a largely unknown mechanism.

280 itin-interacting subunits and thus allow the 26S proteasome to function as a universal degradation ma

281 and the other potentially affecting the host 26S proteasome, to promote feeding cell formation.

282 ia their UBA domains, and associate with the 26S proteasome Ub receptor RPN10 via their N-terminal UB

283 ains to a ubiquitination reaction containing 26S proteasomes, UbcH5, an E3 (MuRF1 or CHIP), and a pro

284 Our results suggest that 26S proteasomes undergo active remodeling to generate a

285 The forked Ub chains bind poorly to 26S proteasomes unlike those synthesized with S5a presen

286 tain insights into the structural changes of 26S proteasome upon the binding and hydrolysis of ATP.

287 Ubiquitin/26S proteasome (UPS)-dependent proteolysis of a variety

288 In mammalian cells, the 26S proteasomes vary in composition.

289 The 26S proteasome was dysfunctional despite normal function

290 Enriched 26S proteasome was prepared and analyzed for protein car

291 The molecular architecture of the 26S proteasome was recently established by cryo-EM appro

292 n of RPN2a, a gene encoding a subunit of the 26S proteasome, was dramatically suppressed in Gr(Delta)

293 estingly, the activities of both the 20S and 26S proteasome were significantly higher in KO than WT m

294 nd the proteolytic activities of the 20S and 26S proteasomes were significantly upregulated during di

295 itin chains direct protein substrates to the 26S proteasome, where they are removed by the deubiquiti

296 ation by TGF-beta involves activation of the 26S proteasome, which is critically dependent on the reg

297 (spy-3) stimulated TCP14 proteolysis by the 26S proteasome, which was reversed by mutation in CULLIN

298 ven partially inhibited in cells or purified 26S proteasomes with various inhibitors, Rpn13 becomes e

299 ecruitment of PA28gamma and PA200 to 20S and 26S proteasomes within 2-6 h.

300 els of ERalpha are tightly controlled by the 26S proteasome; yet, how the clinical proteasome inhibit