ライフサイエンスコーパス: ERAD

1 ERAD activity in the brain decreased with aging, and upr

2 ERAD and VCP/p97 have been implicated in a multitude of

3 ERAD deficiency affected ER-mitochondria contacts and mi

4 ERAD substrates are classified into three categories bas

5 ERAD substrates are ubiquitinated by the action of the H

6 ERAD-defective cell lines likewise exhibited reduced qua

7 ERAD-L is mediated by the Hrd1 complex (composed of Hrd1

8 king between the ER and Golgi retarded COX-2 ERAD.

9 ation of UBC6e causes upregulation of active ERAD enhancers and so increases clearance not only of te

10 N; more ER-associated degradation of alpha3 (ERAD); larger differences in Na,K-ATPase subunit distrib

11 Although ERAD components involved in degradation of luminal subst

12 Our results identify membralin as an ERAD component and demonstrate a critical role for ERAD

13 genome-wide library screen, we identified an ERAD branch required for quality control of a subset of

14 onstrate that the ER protein membralin is an ERAD component, which mediates degradation of ER luminal

15 Gp78 is an ERAD-associated E3 ubiquitin ligase that induces degrada

16 esults, suggest how a polypeptide loop of an ERAD-L substrate moves through the ER membrane.

17 By 72 h, ER stress is alleviated and ERAD proceeds unhindered.

18 e, impairs lipid droplet (LD) biogenesis and ERAD, suggesting a role for LDs in ERAD.

19 Hrd1 and ERAD are essential components of the adaptive ER stress

20 translocon proteins (SEL1L and/or HRD1) and ERAD-associated lectins OS9 and XTP3-B.

21 Functional roles for toxin instability and ERAD in PTS1 translocation have not been established.

22 embrane are discarded through the ERAD-L and ERAD-M pathways, respectively.

23 The current notion is that ERAD-L and ERAD-M substrates are exclusively handled by Hrd1, where

24 gron: ERAD-L (lumen), ERAD-M (membrane), and ERAD-C (cytosol) substrates.

25 it rate) as direct inhibitors of VCP/p97 and ERAD.

26 ther substantiated the link between RFFL and ERAD by showing an interaction between RFFL and VCP in v

27 explored the role of the integrated UPR and ERAD in oligodendrocytes in regulating myelin protein pr

28 this study imply that the integrated UPR and ERAD in oligodendrocytes maintain myelin thickness in ad

29 en the oxidative protein folding and UPR and ERAD pathways.

30 ate BiP availability, which both the UPR and ERAD redeem.

31 arkers associated with inhibition of UPS and ERAD functions, which induces irresolvable proteotoxic s

32 lin binding protein and membralin-associated ERAD substrate.

33 Ectopically expressed Ank4 blocks ERAD to phenocopy O. tsutsugamushi infection.

34 eostasis in exponentially growing cells, but ERAD became relevant when the gene dosage was affected,

35 ER-associated degradation (a process called ERAD).

36 Multispanning ER membrane proteins, called ERAD-M substrates, are retrotranslocated to the cytosol

37 ency specifically in oligodendrocytes caused ERAD impairment, the UPR activation, and attenuation of

38 DNAJB9 may be a rate-limiting factor in CFTR ERAD pathway.

39 rst ER luminal co-chaperone involved in CFTR ERAD, and DNAJB9 could be a novel therapeutic target for

40 Arabidopsis has a similar Hrd1-containing ERAD machinery; however, our knowledge of this complex i

41 , the ER membrane (ERAD-M), and the cytosol (ERAD-C).

42 argin and tunicamycin dramatically decreased ERAD, while increasing maladaptive ER stress proteins an

43 Our study defines ERAD as an essential proteostasis mechanism to safeguard

44 asmic reticulum (ER)-associated degradation (ERAD) (Schumacher et al. 2015).

45 esponse (UPR) and ER-associated degradation (ERAD) are the primary ER quality control mechanism.

46 esponse (UPR) and ER-associated degradation (ERAD) are the primary mechanism that maintains ER protei

47 ndoplasmic reticulum-associated degradation (ERAD) as a protein quality checkpoint that controls the

48 ndoplasmic reticulum-associated degradation (ERAD) complex, participates in IP3R1 degradation and Ca(

49 We show that the ER-associated degradation (ERAD) E3 ubiquitin ligase Doa10 controls cytoplasmic lev

50 rously when these ER-associated degradation (ERAD) factors are crippled, suggesting that reflux may w

51 asmic reticulum (ER)-associated degradation (ERAD) following post-translational glycosylation of Asn-

52 ting in increased ER-associated degradation (ERAD) gene expression and degradation of ER resident pro

53 ndoplasmic reticulum-associated degradation (ERAD) governs the function of quiescent HSCs.

54 asmic reticulum (ER)-associated degradation (ERAD) in plants have revealed homologs in yeast and anim

55 ndoplasmic reticulum-associated degradation (ERAD) in response to the catalytic removal of terminal a

56 rnover occurs via ER-associated degradation (ERAD) involving ubiquitin (Ub)-dependent proteasomal deg

57 ndoplasmic reticulum-associated degradation (ERAD) is a unique mechanism to degrade misfolded protein

58 ndoplasmic reticulum-associated degradation (ERAD) is a well-studied pathway that ensures quality con

59 ndoplasmic reticulum-associated degradation (ERAD) is an essential quality control mechanism of the f

60 ndoplasmic-reticulum-associated degradation (ERAD) is an important protein quality control system whi

61 ER-associated degradation (ERAD) is essential for protein quality control in the ER

62 t that Sel1L-Hrd1 ER-associated degradation (ERAD) is responsible for the clearance of misfolded pro-

63 asmic reticulum (ER)-associated degradation (ERAD) is the movement, or retrotranslocation, of ubiquit

64 vestigate how the ER-associated Degradation (ERAD) machinery can accomplish retrotranslocation of a m

65 components of the ER-associated degradation (ERAD) machinery to retrotranslocate to the cytosol and i

66 components of the ER-associated degradation (ERAD) machinery.

67 components of the ER-associated degradation (ERAD) machinery.

68 ndoplasmic Reticulum-associated degradation (ERAD) of Cystic fibrosis transmembrane-conductance regul

69 ndoplasmic reticulum-associated degradation (ERAD) of MHC class I molecules.

70 uality control by ER-associated degradation (ERAD) of misfolded proteins that accumulate during ER st

71 ress by promoting ER-associated degradation (ERAD) of misfolded proteins.

72 via promotion of ER-associated degradation (ERAD) of nascent pro-cathepsin D (pCatD) and consequent

73 e involved in the ER-associated degradation (ERAD) of not only the tumor metastatic suppressor KAI1 b

74 erol-accelerated, ER-associated degradation (ERAD) of reductase, one of several mechanisms for feedba

75 asmic reticulum (ER)-associated degradation (ERAD) of ubiquitinated HMG CoA reductase (HMGCR), the ra

76 e/vacuole through ER-associated degradation (ERAD) or ER-phagy.

77 ndoplasmic reticulum-associated degradation (ERAD) pathway facilitates the disposal of terminally mis

78 recognized by the ER-associated degradation (ERAD) pathway for removal.

79 ndoplasmic reticulum-associated degradation (ERAD) pathway via a series of tightly coupled steps: sub

80 Blocking the ER-associated degradation (ERAD) pathway with a dominant-negative form of the ERAD

81 asmic reticulum (ER)-associated degradation (ERAD) pathway, a cellular protein quality control proces

82 ndoplasmic reticulum-associated degradation (ERAD) pathway, exhibit delayed UPR activation after lith

83 ndependent of the ER-associated degradation (ERAD) pathway.

84 raded through the ER-associated degradation (ERAD) pathway.

85 ndoplasmic reticulum-associated degradation (ERAD) pathway.

86 te a glycan-based ER-associated degradation (ERAD) signal.

87 ndoplasmic reticulum-associated degradation (ERAD) substrates, and generation of irresolvable proteot

88 that promotion of ER-associated degradation (ERAD) through upregulation of ERAD-enhancing alpha-manno

89 tudies implicated ER-associated degradation (ERAD), a pathway that retrotranslocates misfolded ER pro

90 for clearance by ER-associated degradation (ERAD), a sophisticated process that mediates the ubiquit

91 ality control and ER-associated degradation (ERAD), acts as a timer enzyme, modifying N-linked sugar

92 ndoplasmic reticulum-associated degradation (ERAD), and autophagy.

93 stress, promotes ER-associated degradation (ERAD), and reduces IRE1 signaling in the UPR pathway.

94 subunits undergo ER-associated degradation (ERAD), but this degradation process remains poorly under

95 ndoplasmic reticulum-associated degradation (ERAD), by which misfolded ER proteins are ubiquitinated

96 ndoplasmic reticulum-associated degradation (ERAD), mitochondrial-associated degradation (MAD), chrom

97 of HRD1-mediated ER-associated degradation (ERAD), or of the UPR, in particular the ATF6alpha branch

98 lin is triaged by ER-associated degradation (ERAD).

99 asmic reticulum (ER)-associated degradation (ERAD).

100 lded proteins for ER-associated degradation (ERAD).

101 y are cleared via ER-associated degradation (ERAD).

102 trol mechanism of ER-associated degradation (ERAD).

103 a pathway called ER-associated degradation (ERAD).

104 ndoplasmic reticulum-associated degradation (ERAD).

105 ) are degraded by ER-associated degradation (ERAD).

106 are eliminated by ER-associated degradation (ERAD).

107 ed process termed ER-associated degradation (ERAD).

108 e ER membrane for ER-associated degradation (ERAD).

109 ally selected for ER-associated degradation (ERAD).

110 ndoplasmic reticulum-associated degradation (ERAD).

111 process known as ER-associated degradation (ERAD).

112 ndoplasmic-reticulum-associated degradation (ERAD).

113 esponse (UPR) and ER-associated degradation (ERAD).

114 a major driver of ER-associated degradation (ERAD).

115 proteins undergo ER-associated degradation (ERAD-L): They are retrotranslocated into the cytosol, po

116 ulatory branch of ER-associated degradation (ERAD-R) has a role in shaping the early secretory pathwa

117 ticulum (ER)-associated protein degradation (ERAD) machinery efficiently targets terminally misfolded

118 gh either ER-associated protein degradation (ERAD) or autophagy.

119 oits this ER-associated protein degradation (ERAD) pathway to downregulate HLA class I molecules in v

120 The ER-associated protein degradation (ERAD) pathway, an important UPR function for destruction

121 ed by the ER-associated protein degradation (ERAD) pathway, but very little is known about turnover o

122 er of the ER-associated protein degradation (ERAD) pathway.

123 ed in the ER-associated protein degradation (ERAD) system in eukaryotic organisms(1-4).

124 ic reticulum-associated protein degradation (ERAD), membrane proteins are ubiquitinated, extracted fr

125 omplex of ER-associated protein degradation (ERAD).

126 ic reticulum-associated protein degradation (ERAD).

127 ss termed ER-associated protein degradation (ERAD).

128 ortant in ER-associated protein degradation (ERAD).

129 is termed ER-associated protein degradation (ERAD).

130 ic reticulum-associated protein degradation (ERAD).

131 process termed "ER-associated degradation" (ERAD).

132 location of their degradation signal/degron: ERAD-L (lumen), ERAD-M (membrane), and ERAD-C (cytosol)

133 minus of Sil1 results in the Doa10-dependent ERAD of this mutant protein.

134 ld efficiently route Gas1* to Hrd1-dependent ERAD and provide evidence that it contains a GPI anchor,

135 Using different ERAD substrates, we found that both proteins participate

136 this interaction to Grp170's function during ERAD.

137 stablish a general function of Grp170 during ERAD and suggest that positioning this client-release fa

138 cytosol as full-length intermediates during ERAD, and we have investigated how they maintain substra

139 (NEF) Grp170 plays an important role during ERAD of the misfolded glycosylated client null Hong Kong

140 dation-reduction cycles and may also enhance ERAD, which requires reduced protein substrates.

141 evalonate-derived products owing to enhanced ERAD of HMGCR rather than from reduced synthesis of MK-4

142 rapped in these high-MW complexes, enhancing ERAD of Akita proinsulin and restoring WT insulin secret

143 s diminished, retrotranslocated NRF1 escapes ERAD and is activated into a mature transcription factor

144 regulator of HSC identity(5), as a bona fide ERAD substrate that became aggregated in the endoplasmic

145 gated in the endoplasmic reticulum following ERAD deficiency.

146 ubstrate retrotranslocation in vitro and for ERAD in vivo.

147 ant Hrd3KR that is selectively defective for ERAD of soluble proteins.

148 rovide evidence that LDs are dispensable for ERAD in mammalian cells.

149 to retrograde COX-2 transport to the ER for ERAD.

150 to Hrd1p, an ubiquitin ligase essential for ERAD in Saccharomyces cerevisiae.

151 a eukaryotic chaperone that is essential for ERAD, and is transiently expressed by O. tsutsugamushi d

152 linkage switching reaction is essential for ERAD, oleic acid and acid pH resistance in yeast.

153 gging terminally misfolded glycoproteins for ERAD.

154 misfolded glycoproteins in the ER lumen for ERAD requires the lectin Yos9, which recognizes the glyc

155 enhancing the targeting of MIDY mutants for ERAD to restore WT insulin production.

156 fide bonds and priming the Akita protein for ERAD.

157 RHBDL4 is required for ERAD of some substrates, such as the pre-T-cell receptor

158 omponent and demonstrate a critical role for ERAD in AD pathogenesis.

159 results of this study demonstrate a role for ERAD in neuroendocrine cells and serve as a clinical exa

160 the cytosol, which is an essential step for ERAD, has broad-spectrum anti-flavivirus activity.

161 olding intermediates from being targeted for ERAD.

162 own components of the canonical glycoprotein ERAD pathway.

163 homeostasis and indicate inhibition of HMGCR ERAD contributes to SCD pathogenesis.

164 ion of mutant UBIAD1 and inhibition of HMGCR ERAD.

165 ndispensable component of the mammalian Hrd1 ERAD complex and ER homeostasis, which is essential for

166 f the physiological importance of Sel1L-Hrd1 ERAD.

167 The Sel1L/Hrd1 ERAD genes are enriched in the quiescent and inactive HS

168 , as a novel protein substrate of Sel1L/Hrd1 ERAD, which accumulates upon Sel1L deletion and HSC acti

169 These findings suggest that impaired ERAD in oligodendrocytes reduces myelin thickness in the

170 Of note, deletion of SCJ1 impairs ERAD of model substrates and causes the accumulation of

171 O. tsutsugamushi also impedes ERAD during this time period.

172 a new approach to evaluate Hrd3 functions in ERAD.

173 their requirements and diverse functions in ERAD.

174 The function of Htm1 in ERAD relies on its association with Pdi1, which appears

175 he mechanisms of specific E2/E3 interplay in ERAD, but also offers a basis to understand how RING E3s

176 he protein partners specifically involved in ERAD of NKCC2.

177 D1 complex, the other E3 complex involved in ERAD.

178 wn what ER luminal factor(s) are involved in ERAD.

179 nesis and ERAD, suggesting a role for LDs in ERAD.

180 echanistic studies of the roles of RHBDL4 in ERAD and other important cellular pathways.

181 that Hrd3 has a direct and critical role in ERAD in addition to Hrd1 stabilization.

182 ectins, and translocon components, including ERAD E3 ubiquitin ligase HRD1, diminished suppression of

183 sors, thapsigargin and tunicamycin increased ERAD, as well as adaptive ER stress proteins, and minima

184 release and is sequestered in ER to inhibit ERAD.

185 CP26 targets the Hrd1 complex, inhibits ERAD, and induces ER stress.

186 during the infection period when it inhibits ERAD.

187 Repressing the initial ERAD recognition step by inhibiting Grp94 enhances the f

188 To initiate ERAD, ADP-BiP is often recruited to the misfolded client

189 , indicating that the ubx4Delta phenotype is ERAD-independent.

190 ing of dissociated PTS1 as a trigger for its ERAD-mediated translocation to the cytosol.

191 Here we establish key ERAD machinery components used to triage the Akita proin

192 did not occur in yeast strains in which key ERAD or proteasomal pathway genes had been disrupted, in

193 MfSTMIR promoted the degradation of a known ERAD substrate, CPY*.

194 nzyme Ubc7, but was independent of the known ERAD ubiquitin ligases Doa10 and Hrd1 as well as the rec

195 ization of the misfolded part, the ER lumen (ERAD-L), the ER membrane (ERAD-M), and the cytosol (ERAD

196 r degradation signal/degron: ERAD-L (lumen), ERAD-M (membrane), and ERAD-C (cytosol) substrates.

197 evolutionarily conserved, but the mammalian ERAD system uses additional ubiquitin ligases to assist

198 lease of UBIAD1 from HMGCR, allowing maximal ERAD and ER-to-Golgi transport of UBIAD1.

199 BIAD1 from reductase, permitting its maximal ERAD and ER-to-Golgi transport of UBIAD1.

200 Mechanistically, ERAD deficiency via Sel1L knockout leads to activation o

201 This study clarifies a Grp94-mediated ERAD pathway for GABAA receptors, which provides a novel

202 demonstrate the presence of an OS9-mediated ERAD pathway in renal cells that degrades immature NKCC2

203 t stabilization of both luminal and membrane ERAD substrates, but unlike Hrd1, which plays an essenti

204 art, the ER lumen (ERAD-L), the ER membrane (ERAD-M), and the cytosol (ERAD-C).

205 e intracellular bacterial pathogen modulates ERAD to satisfy its nutritional virulence requirements.

206 Neither Hrd1 nor ERAD has been studied in the heart, or in cardiac myocyt

207 moved to the cytoplasm as part of the normal ERAD pathway, where they are part of a solely proteinace

208 chor, ruling out that a GPI anchor obstructs ERAD.

209 tions that a GPI anchor sterically obstructs ERAD.

210 L-HRD1 complex, the most conserved branch of ERAD(4), is highly expressed in HSCs.

211 Different branches of ERAD are involved in degradation of malfolded secretory

212 in is an essential ATPase for degradation of ERAD substrates.

213 n in PEL cells was increased by depletion of ERAD components, and suppression of CatD by vIL-6 overex

214 cardiomyopathy, suggesting dysregulation of ERAD and inefficient clearance of proteins targeted for

215 o the long known ATP-dependent extraction of ERAD substrates during retrotranslocation, the Cdc48 com

216 Sustained inhibition of ERAD using RNA interference results in an O. tsutsugamus

217 e identification and selective modulation of ERAD components specific to NKCC2 and its disease-causin

218 Accordingly, the degradation rate of ERAD substrates is attenuated in cells lacking membralin

219 understanding and biological significance of ERAD-mediated regulation of lipid metabolism in mammalia

220 the glycan trimming and dislocation steps of ERAD.

221 d ubiquitination of IGF2R and suppression of ERAD proteins effected increased IGF2R expression and lo

222 s the channel that mediates the transport of ERAD substrates to the cytosol.

223 d degradation (ERAD) through upregulation of ERAD-enhancing alpha-mannosidase-like proteins (EDEMs) p

224 SP19 with Derlin-1 nor significant effect on ERAD by USP19 depletion.

225 pulating the cellular folding environment or ERAD pathways can alter the kinetics of mutant alpha deg

226 tion of gp78/AMFR in male mice disrupts P450 ERAD, resulting in statistically significant stabilizati

227 oxifen) as P450 substrates, reveal that P450 ERAD disruption could influence therapeutic drug respons

228 and identified new drugs against the VCP/p97/ERAD pathway in human diseases.

229 Depletion of particular ERAD-associated isomerases, lectins, and translocon comp

230 n by the ER--associated degradation pathway (ERAD).

231 owever, it remains unknown whether the plant ERAD system contains a plant-specific E3 ligase.

232 teins (GPI-APs) are, however, generally poor ERAD substrates and are targeted mainly to the vacuole/l

233 proteins Hrd1 and Doa10 are the predominant ERAD ubiquitin-protein ligases (E3s).

234 contribution to antigen cross-presentation, ERAD, and transport of internalized antigens into the cy

235 appears to act downstream of Hrd1 to promote ERAD via cooperation with the BAG6 chaperone complex.

236 ain sequestered in the ER to block reductase ERAD.

237 ssociated UBIAD1 variant inhibited reductase ERAD, thereby stabilizing the enzyme and contributing to

238 ansport enables UBIAD1 to modulate reductase ERAD such that synthesis of nonsterol isoprenoids is mai

239 that UBIAD1-mediated inhibition of reductase ERAD underlies cholesterol accumulation associated with

240 iency and SCD-associated UBIAD1 on reductase ERAD and cholesterol synthesis.

241 UBIAD1 as a central player in the reductase ERAD pathway and regulation of isoprenoid synthesis.

242 mutant VCP-overexpressing hearts up-regulate ERAD complex components and have elevated levels of ubiq

243 ncreasing folding capacity and up-regulating ERAD components that remove non-native proteins.

244 eded for the solubility of retrotranslocated ERAD-M intermediates.

245 n vivo assay, we show that retrotranslocated ERAD-M substrates are moved to the cytoplasm as part of

246 The same ERAD machinery also controls the flux through various me

247 endogenous levels of EDEM1, OS-9, and SEL1L (ERAD enhancers).

248 and Hrd1 and inhibits degradation of several ERAD substrates.

249 Cdc48-Npl4-Ufd1 were present in solubilized ERAD-M substrates.

250 is gated by autoubiquitination and a soluble ERAD substrate.

251 In contrast, for three other spontaneous ERAD model substrates (NS1, NHK-alpha1AT, and BST-2/Teth

252 Thus, O. tsutsugamushi temporally stalls ERAD until ERAD-derived amino acids are needed to suppor

253 re to elucidate roles for Hrd1 in ER stress, ERAD, and viability in cultured cardiac myocytes and in

254 of retrotranslocation of luminal substrates (ERAD-L), recapitulating key steps in a basic process in

255 This complex targets ERAD enhancers for degradation, a function that depends

256 The current notion is that ERAD-L and ERAD-M substrates are exclusively handled by

257 Our data reveal that ERAD branches have remarkable specificity for their memb

258 Thus, our work shows that ERAD-C substrates can be systematically generated via sy

259 The levels of proteins that comprise the ERAD machinery are thus carefully tuned and adjusted to

260 adation protein 1), and is necessary for the ERAD activity of the Sel1L-Hrd1 complex.

261 ecific E3 ligase MfSTMIR participates in the ERAD pathway by interacting with MtUBC32 and MtSec61gamm

262 activity include expression of genes in the ERAD pathway, providing a potential strategy for patient

263 However, whether LDs are involved in the ERAD process remains an outstanding question.

264 refore, upregulation of EDEM function in the ERAD protects against ER proteinopathy in vivo and thus

265 Constituents of the ERAD complex and its role in neurodegeneration are not y

266 pathway with a dominant-negative form of the ERAD core component, valosin-containing protein (VCP), i

267 this mechanism results in dysfunction of the ERAD pathway by a delayed turnover of substrates.

268 on-mediated regulation requires parts of the ERAD pathway.

269 Central regulators of the ERAD system are membrane-bound ubiquitin ligases, which

270 Here we describe a novel feature of the ERAD system that entails differential activation of Ubc7

271 ich facilitates future investigations of the ERAD-C pathway.

272 lumen or membrane are discarded through the ERAD-L and ERAD-M pathways, respectively.

273 In the ER, CT targets to the ERAD machinery composed of the E3 ubiquitin ligase Hrd1-

274 th type II Bartter syndrome is linked to the ERAD pathway and that future therapeutic strategies shou

275 degradation of the membrane proteins via the ERAD-C pathway.

276 MfSTMIR interacted with the ERAD-associated ubiquitin-conjugating enzyme MtUBC32 and

277 pha1 subunits and positively regulates their ERAD.

278 ves as a critical "retrochaperone" for these ERAD-M substrates.

279 trotranslocation and ubiquitination of these ERAD substrates, knockdown of gp78 does not affect eithe

280 spectrometry approaches, we showed that this ERAD branch is defined by an ER membrane complex consist

281 can-mediated process, can also contribute to ERAD in an unconventional, catalysis-independent manner.

282 ormally decreased susceptibility of Gas1* to ERAD is caused by canonical remodeling of its GPI anchor

283 argets terminally misfolded glycoproteins to ERAD.

284 onself" or misfolded protein and sorts HA to ERAD for degradation, resulting in inhibition of IAV rep

285 athway, which has remarkable similarities to ERAD in the endoplasmic reticulum, operates in post-ER o

286 binding to retrotranslocated, ubiquitinated ERAD-M substrates is required for their solubility; remo

287 ed in knockin mice expressing ubiquitination/ERAD-resistant HMGCR.

288 omeric species that are competent to undergo ERAD.

289 . tsutsugamushi temporally stalls ERAD until ERAD-derived amino acids are needed to support its growt

290 though oxidative protein folding and the UPR/ERAD pathways each are well-understood, very little is k

291 Protein quality control via ERAD is, therefore, a critical checkpoint that governs H

292 e ER stress, resulting in HA degradation via ERAD and consequent inhibition of IAV replication.

293 nnose is necessary for their degradation via ERAD, but whether this modification is specific to misfo

294 tes are exclusively handled by Hrd1, whereas ERAD-C substrates are recognized by Doa10.

295 a new layer of homeostatic control, in which ERAD activity itself is regulated posttranscriptionally

296 in quality control vesicles (QCVs) to which ERAD substrates are transported and in which they intera

297 Mice with ERAD deficiency in brown adipocytes were cold sensitive

298 esting that reflux may work in parallel with ERAD.

299 Yeast ERAD employs two integral ER membrane E3 Ub ligases: Hrd

300 protein degradation as directed by the yeast ERAD RING E3 ligases, Hrd1 and Doa10.