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 ESCRT also mediate Kir2.1 degradation in human

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

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

8 egulatory particle in the sterol-accelerated ERAD of reductase that may be applicable to the ERAD of

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

10 trates, they can also be fused to additional ERAD substrates to interrogate substrate-specific pathwa

11 While in yeast and animals, the alternative ERAD-L/ERAD-M pathway regulates HMGR activity by control

12 y also highlight the close connections among ERAD, lipid droplets, and lipid droplet-associated prote

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

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 eport the development of a system to analyze ERAD based on mutants of split or intact Venus fluoresce

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 se of known glycoprotein quality control and ERAD components.

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

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

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

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

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

25 pathway requires its E3 ubiquitin ligase and ERAD activity to directly degrade MAVS, whereas the othe

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

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

28 Using proteasome and ERAD inhibitors, we showed that ERAD is required for pro

29 ian Sel1L is required for Hrd1 stability and ERAD function both in vitro and in vivo.

30 itin ligase, promoted NCC ubiquitination and ERAD, the Hsp70/Hsp90 organizer protein stabilized NCC t

31 A coordinator of the UPR and ERAD processes has long been sought.

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

33 lin binding protein and membralin-associated ERAD substrate.

34 Blocking ERAD activity diminished the interaction of Rtp6 with GA

35 as well as receptor signaling upon blocking ERAD function, and by the interaction of GABAB receptors

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

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

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

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

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

41 receptor, between ER-associated degradation (ERAD) and an ERQC autophagy pathway.

42 ndoplasmic reticulum-associated degradation (ERAD) as shown by the accumulation of receptors in the e

43 asmic reticulum (ER)-associated degradation (ERAD) by the ubiquitin E3 ligase HRD1, and E2 ubiquitin

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

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

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

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

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

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

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

51 participation in ER-associated degradation (ERAD) lost their ability to degrade MAVS, but surprising

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

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

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

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

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

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

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

59 asmic reticulum (ER)-associated degradation (ERAD) of misfolded secretory proteins, reflecting the fa

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

61 asmic reticulum (ER)-associated degradation (ERAD) of the cholesterol biosynthetic enzyme 3-hydroxy-3

62 d the role of the ER-associated degradation (ERAD) pathway during BKPyV intracellular trafficking in

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

64 ndoplasmic reticulum-associated degradation (ERAD) pathway that functions to remove unfolded/misfolde

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

66 asmic reticulum (ER)-associated degradation (ERAD) pathway.

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

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

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

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

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

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

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

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

75 asmic reticulum (ER)-associated degradation (ERAD), although the mechanisms governing this process re

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

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

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

79 are essential for ER-associated degradation (ERAD), including valosin-containing protein (VCP) and Hr

80 llectively termed ER-associated degradation (ERAD), misfolded proteins are retrotranslocated to the c

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

82 ndoplasmic reticulum-associated degradation (ERAD).

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

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

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

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

87 ndoplasmic reticulum-associated degradation (ERAD).

88 onent involved in ER-associated degradation (ERAD).

89 nd elimination by ER-associated degradation (ERAD).

90 r to ER export or ER-associated degradation (ERAD).

91 ndoplasmic reticulum-associated degradation (ERAD).

92 ndoplasmic reticulum-associated degradation (ERAD).

93 ndoplasmic reticulum-associated degradation (ERAD).

94 llectively termed ER-associated degradation (ERAD).

95 teasome-mediated, ER-associated degradation (ERAD).

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

97 ndoplasmic reticulum-associated degradation (ERAD).

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 ibutes to ER-associated protein degradation (ERAD) by initiating the formation of degradation signals

104 cipate in ER-associated protein degradation (ERAD) in yeast.

105 ticulum (ER)-associated protein degradation (ERAD) machinery determines the number of cell surface GA

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

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

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

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

110 ticulum (ER)-associated protein degradation (ERAD) pathway.

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

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

113 ways, the ER-associated protein degradation (ERAD), monitors the folding of membrane and secretory pr

114 ic reticulum-associated protein degradation (ERAD).

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

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

117 ss called ER-associated protein degradation (ERAD).

118 ticulum (ER)-associated protein degradation (ERAD).

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

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

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

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

123 nosidases (MNS1 to MNS5) in glycan-dependent ERAD.

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

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

126 this interaction to Grp170's function during ERAD.

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

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

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

130 nd represent one of the few known endogenous ERAD substrates.

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

132 action of GABAB receptors with the essential ERAD components Hrd1 and p97.

133 Our further analyses revealed that the five ERAD-Lm substrates examined are classified into three su

134 ubstrate retrotranslocation in vitro and for ERAD in vivo.

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

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

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

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

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

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

141 rol compartment (ERQC), a staging ground for ERAD.

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

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

144 fide bonds and priming the Akita protein for ERAD.

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

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

147 n, our results reveal a fundamental role for ERAD in sterol homeostasis, with the two branches of thi

148 olding intermediates from being targeted for ERAD.

149 translocation motor, shunts S168R-GnRHR from ERAD to ERQC autophagy.

150 own components of the canonical glycoprotein ERAD pathway.

151 rol in the cell allowed GGPP-stimulated Hmg2 ERAD.

152 In a forward genetic screen for host ERAD components hijacked by US11 in near-haploid KBM7 ce

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

154 there has been great progress in identifying ERAD components, how these factors accurately identify s

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

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

157 dly, GRP94 does not collaborate with OS-9 in ERAD of misfolded substrates, nor is the chaperone requi

158 their requirements and diverse functions in ERAD.

159 a new approach to evaluate Hrd3 functions in ERAD.

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

161 he protein partners specifically involved in ERAD of NKCC2.

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

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

164 man cells and uncovered its participation in ERAD substrate retention, retrieval to the ER, and subse

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

166 These results clarify the role of USP19 in ERAD and suggest a novel DUB regulation that involves ch

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

168 stasis modulators reported so far, including ERAD inhibitors, trigger cellular stress and lead to ind

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

170 Furthermore, inhibiting ERAD did not prevent entry of capsid protein VP1 into th

171 during the infection period when it inhibits ERAD.

172 In addition, Aup1 knockdown inhibits ERAD of Insig-1, another substrate for gp78, as well as

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

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

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

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

177 in yeast and animals, the alternative ERAD-L/ERAD-M pathway regulates HMGR activity by controlling pr

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

179 el1L's physiological importance in mammalian ERAD, however, remains to be established.

180 d the central component of a novel mammalian ERAD complex.

181 dentification of key components of mammalian ERAD, including Derlin-1, p97, VIMP and SEL1L.

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

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

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

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

186 cosylated form of GRP94 in an OS-9-mediated, ERAD-independent, lysosomal-like mechanism.

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

188 he retention or degradation of the misfolded ERAD substrate Null Hong Kong.

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

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

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

192 Our data show that TMEM129 is a novel ERAD E3 ligase and the central component of a novel mamm

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

194 tions that a GPI anchor sterically obstructs ERAD.

195 unction as a hub for membrane association of ERAD machinery components, a key organizer of the ERAD c

196 Since the other branch of ERAD is required for HMGR regulation, our results reveal

197 1 ligase activity toward a specific class of ERAD substrates.

198 ed, Yos9 also binds the protein component of ERAD substrates.

199 proteasome targeting, are key components of ERAD.

200 ough whether direct ubiquitin conjugation of ERAD substrates is required for dislocation has been dif

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

202 complex permits the selective degradation of ERAD-resistant membrane proteins via ERQC autophagy.

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

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

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

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

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

208 and p97/VCP contributes to the regulation of ERAD in mammalian cells.

209 otential to play a role in the regulation of ERAD.

210 R proteins, further highlighting the role of ERAD in cellular homeostasis.

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

212 the glycan trimming and dislocation steps of ERAD.

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

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

215 t the ERAD E3 gp78 can ubiquitinate not only ERAD substrates, but also the machinery protein Ubl4A, a

216 cetyltransferase to show that it is the only ERAD factor requiring N-terminal acetylation.

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

218 tudied ER-associated degradation pathway, or ERAD.

219 ssed USP19 interacts with Derlin-1 and other ERAD machinery factors in the membrane, endogenous USP19

220 es within a complex containing various other ERAD components, including Derlin-1, Derlin-2, VIMP and

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

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

223 We show that two polytopic ERAD substrates, mutated transporter of the mating type

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

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

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

227 s with opposing activities, can both promote ERAD.

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

229 Elevation of JB12 promotes ERAD of S168R-GnRHR, with E90K-GnRHR being resistant.

230 ain sequestered in the ER to block reductase ERAD.

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

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

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

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

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

236 ozyme Hmg2 also undergoes feedback-regulated ERAD in response to the early pathway-derived isoprene g

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

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

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

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

241 Our results suggest a shared ERAD pathway for glycosylated and nonglycosylated protei

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

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

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

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

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

247 highly structured, and able to fully support ERAD in vivo.

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

249 There is also increasing evidence that ERAD controls other ER-related functions through regulat

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

251 oteasome and ERAD inhibitors, we showed that ERAD is required for productive entry.

252 asomal degradation of GABAB receptors by the ERAD machinery is a potent mechanism regulating the numb

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

254 ific recognition of linear peptides from the ERAD substrate, carboxypeptidase Y G255R (CPY*), and bin

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

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

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

258 l degradation following recruitment into the ERAD pathway has been described.

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

260 machinery components, a key organizer of the ERAD complex.

261 ically recognized by other components of the ERAD machinery, which ultimately results in the disposal

262 es, potentially by acting on elements of the ERAD machinery.

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

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

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

266 instead most likely required to support the ERAD of alphaENaC.

267 It tethers the ERAD ubiquitin-conjugating enzyme (E2), Ubc7p, to the ER

268 Here we demonstrate that the ERAD E3 gp78 can ubiquitinate not only ERAD substrates,

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

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

271 D of reductase that may be applicable to the ERAD of other substrates.

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

273 pha1 subunits and positively regulates their ERAD.

274 aOR-Cys(27) precursors with CNX led to their ERAD.

275 ependent fluorescent proteins are themselves ERAD substrates, they can also be fused to additional ER

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

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

278 ile MNS1 to MNS3 appear dispensable for this ERAD process.

279 Thus, ERAD-Lm substrates are degraded through much more divers

280 ting a large fraction of hdeltaOR-Cys(27) to ERAD.

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

282 argets terminally misfolded glycoproteins to ERAD.

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

284 g misfolded/incompletely folded receptors to ERAD, possibly in altered cellular conditions.

285 e degradation intermediates are resistant to ERAD.

286 gest that it recruits HRD1, which targets to ERAD the substrate presented by the OS-9 lectin at the E

287 biquitinating and inactivating ubiquitinated ERAD components that normally promote toxin retro-transl

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

289 omeric species that are competent to undergo ERAD.

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

291 everely destabilized GC variant achieved via ERAD inhibition in fibroblasts derived from patients wit

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 HR is globally misfolded and disposed of via ERAD, but inhibition of p97, the protein retrotranslocat

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

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

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

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

299 cleotide binding domain (NBD2*) from a yeast ERAD substrate, Ste6p*, resides at the cytoplasmic face

300 factor, a postulated nonubiquitinated yeast ERAD substrate, in mammalian cells.