A structurally conserved site in AUP1 binds the E2 enzyme UBE2G2 and is essential for ER-associated degradation

Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple ERAD pathways exist for targeting topologically distinct substrates, all pathways require substrate ubiquitination. Here, we characterize a ke...

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Published inPLoS biology Vol. 19; no. 12; p. e3001474
Main Authors Smith, Christopher E, Tsai, Yien Che, Liang, Yu-He, Khago, Domarin, Mariano, Jennifer, Li, Jess, Tarasov, Sergey G, Gergel, Emma, Tsai, Borong, Villaneuva, Matthew, Clapp, Michelle E, Magidson, Valentin, Chari, Raj, Byrd, R Andrew, Ji, Xinhua, Weissman, Allan M
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 08.12.2021
Public Library of Science (PLoS)
Subjects
Amino Acid Sequence - genetics
Amino acids
Binding
Binding sites
Biology and Life Sciences
Bridges
Cell Line, Tumor
CRISPR
Degradation
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum-Associated Degradation - genetics
Endoplasmic Reticulum-Associated Degradation - physiology
Experiments
Homeostasis
Humans
Hydrogen bonding
Hydrogen bonds
Hydrophobicity
Lipids
Mammals
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membrane Proteins - physiology
Membrane Proteins - ultrastructure
Membranes
Mutagenesis
Mutation
Physical Sciences
Plasmids
Protein Binding - genetics
Protein Domains - genetics
Proteins
Quality control
Research and Analysis Methods
Substrates
Ubiquitin
Ubiquitin-conjugating enzyme
Ubiquitin-Conjugating Enzymes - genetics
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitin-Conjugating Enzymes - physiology
Ubiquitin-Conjugating Enzymes - ultrastructure
Ubiquitin-protein ligase
Ubiquitination
Hong Kong China
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Abstract Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple ERAD pathways exist for targeting topologically distinct substrates, all pathways require substrate ubiquitination. Here, we characterize a key role for the UBE2G2 Binding Region (G2BR) of the ERAD accessory protein ancient ubiquitous protein 1 (AUP1) in ERAD pathways. This 27-amino acid (aa) region of AUP1 binds with high specificity and low nanomolar affinity to the backside of the ERAD ubiquitin-conjugating enzyme (E2) UBE2G2. The structure of the AUP1 G2BR (G2BRAUP1) in complex with UBE2G2 reveals an interface that includes a network of salt bridges, hydrogen bonds, and hydrophobic interactions essential for AUP1 function in cells. The G2BRAUP1 shares significant structural conservation with the G2BR found in the E3 ubiquitin ligase gp78 and in vitro can similarly allosterically activate ubiquitination in conjunction with ERAD E3s. In cells, AUP1 is uniquely required to maintain normal levels of UBE2G2; this is due to G2BRAUP1 binding to the E2 and preventing its rapid degradation. In addition, the G2BRAUP1 is required for both ER membrane recruitment of UBE2G2 and for its activation at the ER membrane. Thus, by binding to the backside of a critical ERAD E2, G2BRAUP1 plays multiple critical roles in ERAD.
AbstractList Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple ERAD pathways exist for targeting topologically distinct substrates, all pathways require substrate ubiquitination. Here, we characterize a key role for the UBE2G2 Binding Region (G2BR) of the ERAD accessory protein ancient ubiquitous protein 1 (AUP1) in ERAD pathways. This 27-amino acid (aa) region of AUP1 binds with high specificity and low nanomolar affinity to the backside of the ERAD ubiquitin-conjugating enzyme (E2) UBE2G2. The structure of the AUP1 G2BR (G2BRAUP1) in complex with UBE2G2 reveals an interface that includes a network of salt bridges, hydrogen bonds, and hydrophobic interactions essential for AUP1 function in cells. The G2BRAUP1 shares significant structural conservation with the G2BR found in the E3 ubiquitin ligase gp78 and in vitro can similarly allosterically activate ubiquitination in conjunction with ERAD E3s. In cells, AUP1 is uniquely required to maintain normal levels of UBE2G2; this is due to G2BRAUP1 binding to the E2 and preventing its rapid degradation. In addition, the G2BRAUP1 is required for both ER membrane recruitment of UBE2G2 and for its activation at the ER membrane. Thus, by binding to the backside of a critical ERAD E2, G2BRAUP1 plays multiple critical roles in ERAD.Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple ERAD pathways exist for targeting topologically distinct substrates, all pathways require substrate ubiquitination. Here, we characterize a key role for the UBE2G2 Binding Region (G2BR) of the ERAD accessory protein ancient ubiquitous protein 1 (AUP1) in ERAD pathways. This 27-amino acid (aa) region of AUP1 binds with high specificity and low nanomolar affinity to the backside of the ERAD ubiquitin-conjugating enzyme (E2) UBE2G2. The structure of the AUP1 G2BR (G2BRAUP1) in complex with UBE2G2 reveals an interface that includes a network of salt bridges, hydrogen bonds, and hydrophobic interactions essential for AUP1 function in cells. The G2BRAUP1 shares significant structural conservation with the G2BR found in the E3 ubiquitin ligase gp78 and in vitro can similarly allosterically activate ubiquitination in conjunction with ERAD E3s. In cells, AUP1 is uniquely required to maintain normal levels of UBE2G2; this is due to G2BRAUP1 binding to the E2 and preventing its rapid degradation. In addition, the G2BRAUP1 is required for both ER membrane recruitment of UBE2G2 and for its activation at the ER membrane. Thus, by binding to the backside of a critical ERAD E2, G2BRAUP1 plays multiple critical roles in ERAD.
Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple ERAD pathways exist for targeting topologically distinct substrates, all pathways require substrate ubiquitination. Here, we characterize a key role for the UBE2G2 Binding Region (G2BR) of the ERAD accessory protein ancient ubiquitous protein 1 (AUP1) in ERAD pathways. This 27-amino acid (aa) region of AUP1 binds with high specificity and low nanomolar affinity to the backside of the ERAD ubiquitin-conjugating enzyme (E2) UBE2G2. The structure of the AUP1 G2BR (G2BRAUP1) in complex with UBE2G2 reveals an interface that includes a network of salt bridges, hydrogen bonds, and hydrophobic interactions essential for AUP1 function in cells. The G2BRAUP1 shares significant structural conservation with the G2BR found in the E3 ubiquitin ligase gp78 and in vitro can similarly allosterically activate ubiquitination in conjunction with ERAD E3s. In cells, AUP1 is uniquely required to maintain normal levels of UBE2G2; this is due to G2BRAUP1 binding to the E2 and preventing its rapid degradation. In addition, the G2BRAUP1 is required for both ER membrane recruitment of UBE2G2 and for its activation at the ER membrane. Thus, by binding to the backside of a critical ERAD E2, G2BRAUP1 plays multiple critical roles in ERAD.
Endoplasmic reticulum–associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple ERAD pathways exist for targeting topologically distinct substrates, all pathways require substrate ubiquitination. Here, we characterize a key role for the UBE2 G2 B inding R egion (G2BR) of the ERAD accessory protein ancient ubiquitous protein 1 (AUP1) in ERAD pathways. This 27-amino acid (aa) region of AUP1 binds with high specificity and low nanomolar affinity to the backside of the ERAD ubiquitin-conjugating enzyme (E2) UBE2G2. The structure of the AUP1 G2BR (G2BR AUP1 ) in complex with UBE2G2 reveals an interface that includes a network of salt bridges, hydrogen bonds, and hydrophobic interactions essential for AUP1 function in cells. The G2BR AUP1 shares significant structural conservation with the G2BR found in the E3 ubiquitin ligase gp78 and in vitro can similarly allosterically activate ubiquitination in conjunction with ERAD E3s. In cells, AUP1 is uniquely required to maintain normal levels of UBE2G2; this is due to G2BR AUP1 binding to the E2 and preventing its rapid degradation. In addition, the G2BR AUP1 is required for both ER membrane recruitment of UBE2G2 and for its activation at the ER membrane. Thus, by binding to the backside of a critical ERAD E2, G2BR AUP1 plays multiple critical roles in ERAD.
Endoplasmic reticulum–associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple ERAD pathways exist for targeting topologically distinct substrates, all pathways require substrate ubiquitination. Here, we characterize a key role for the UBE2 G2 B inding R egion (G2BR) of the ERAD accessory protein ancient ubiquitous protein 1 (AUP1) in ERAD pathways. This 27-amino acid (aa) region of AUP1 binds with high specificity and low nanomolar affinity to the backside of the ERAD ubiquitin-conjugating enzyme (E2) UBE2G2. The structure of the AUP1 G2BR (G2BR AUP1 ) in complex with UBE2G2 reveals an interface that includes a network of salt bridges, hydrogen bonds, and hydrophobic interactions essential for AUP1 function in cells. The G2BR AUP1 shares significant structural conservation with the G2BR found in the E3 ubiquitin ligase gp78 and in vitro can similarly allosterically activate ubiquitination in conjunction with ERAD E3s. In cells, AUP1 is uniquely required to maintain normal levels of UBE2G2; this is due to G2BR AUP1 binding to the E2 and preventing its rapid degradation. In addition, the G2BR AUP1 is required for both ER membrane recruitment of UBE2G2 and for its activation at the ER membrane. Thus, by binding to the backside of a critical ERAD E2, G2BR AUP1 plays multiple critical roles in ERAD. This study shows that a 27-amino acid domain that binds the ubiquitin conjugating enzyme UBE2G2, and which is found in two different proteins (AUP1 and gp78), is critical for endoplasmic reticulum-associated degradation (ERAD).
Author Tarasov, Sergey G
Tsai, Borong
Gergel, Emma
Ji, Xinhua
Villaneuva, Matthew
Mariano, Jennifer
Clapp, Michelle E
Weissman, Allan M
Tsai, Yien Che
Li, Jess
Khago, Domarin
Chari, Raj
Byrd, R Andrew
Magidson, Valentin
Liang, Yu-He
Smith, Christopher E
AuthorAffiliation Georgia Institute of Technology, UNITED STATES
1 Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America
2 Center for Structural Biology, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland, United States of America
4 Optical Microscopy and Analysis Laboratory, Frederick National Laboratory for Cancer Research, Frederick, Maryland, United States of America
3 Genome Modification Core, Frederick National Laboratory for Cancer Research, Frederick, Maryland, United States of America
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Cites_doi 10.1083/jcb.201906047
10.1038/ncomms4832
10.1021/acssynbio.6b00343
10.1128/MCB.20.19.7214-7219.2000
10.1073/pnas.1409099111
10.1146/annurev-cellbio-111315-125036
10.1371/journal.pone.0072453
10.1074/jbc.C111.266452
10.1074/jbc.M307453200
10.1016/0076-6879(83)98152-1
10.1038/sj.onc.1210017
10.1101/cshperspect.a013185
10.1038/365176a0
10.1074/jbc.272.12.7946
10.1038/381272a0
10.1091/mbc.e12-07-0564
10.15252/embj.2020104863
10.1107/S0021889892009944
10.1074/jbc.M110.211326
10.1016/S0092-8674(02)00872-3
10.1002/j.1460-2075.1996.tb00560.x
10.1016/j.str.2017.03.016
10.1074/jbc.274.21.14685
10.1074/jbc.M110.190785
10.1073/pnas.0506618103
10.1016/j.molcel.2009.03.010
10.1016/j.molcel.2013.04.004
10.1074/jbc.M110.120766
10.7554/eLife.40009
10.1074/jbc.M007640200
10.1074/jbc.M806424200
10.1016/j.molcel.2013.04.005
10.1016/S0076-6879(05)99033-2
10.1016/j.cell.2016.05.048
10.1107/S0907444904019158
10.1038/s41556-020-0473-4
10.1038/nrm3173
10.1107/S0907444906019949
10.1042/BJ20041241
10.1038/ncb1558
10.1096/fj.201800960R
10.1016/j.molcel.2009.05.010
10.1091/mbc.e07-06-0601
10.1016/S0006-291X(03)00279-1
10.1073/pnas.0805371105
10.1038/35050524
10.1038/nm1686
10.1074/jbc.M008608200
10.1107/S2053230X19009786
10.1074/jbc.M111.284794
10.1016/bs.mie.2019.01.002
10.1038/sj.emboj.7600946
10.1158/0008-5472.CAN-16-2159
10.1242/jcs.044255
10.1083/jcb.116.1.57
10.1016/j.cell.2006.05.043
10.1107/S0907444909052925
10.1038/nature06004
10.1074/jbc.270.51.30408
10.1101/gad.933301
10.1073/pnas.96.20.11364
10.1083/jcb.200605196
10.1073/pnas.1016229108
10.1073/pnas.251401598
10.1074/jbc.M608999200
10.1126/science.278.5344.1806
10.7554/eLife.50903
10.1073/pnas.1112831108
10.1038/ncb2383
10.1016/j.semcdb.2018.09.013
10.1194/jlr.M033852
10.1016/j.molcel.2020.07.009
10.1016/S0014-5793(02)03660-8
10.1159/000134403
10.1074/jbc.M115.685867
10.1093/emboj/17.10.2759
10.1083/jcb.200309132
10.1074/jbc.RA117.001260
10.1038/srep30955
10.1016/j.isci.2020.101493
10.1016/S0021-9258(18)68646-6
10.1038/ncb1689
10.1016/j.molcel.2016.04.031
10.1038/emboj.2013.174
10.1091/mbc.e12-08-0631
10.1242/jcs.232850
10.1073/pnas.0808564106
10.1016/j.str.2012.09.020
10.1016/j.molcel.2018.11.015
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Issue 12
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Current Address: RCSB Protein Data Bank, Rutgers, The State University of New Jersey, Piscataway, New Jersey, United States of America
The authors have declared that no competing interests exist.
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References BK Sato (pbio.3001474.ref059) 2009; 34
KS Chakrabarti (pbio.3001474.ref069) 2017; 25
T Yang (pbio.3001474.ref084) 2002; 110
S Vashist (pbio.3001474.ref009) 2004; 165
PD Adams (pbio.3001474.ref089) 2010; 66
JN Lee (pbio.3001474.ref047) 2006; 281
YC Tsai (pbio.3001474.ref055) 2012; 23
LY Jiang (pbio.3001474.ref062) 2018; 293
S Liu (pbio.3001474.ref027) 2012; 20
A Brauweiler (pbio.3001474.ref082) 2007; 26
S Stefanovic-Barrett (pbio.3001474.ref041) 2018; 19
R Chari (pbio.3001474.ref078) 2017; 6
RN Sifers (pbio.3001474.ref053) 1988; 263
JA Olzmann (pbio.3001474.ref001) 2013; 5
JC Christianson (pbio.3001474.ref039) 2011; 14
S Neal (pbio.3001474.ref011) 2020; 23
R Das (pbio.3001474.ref017) 2009; 34
Y Liu (pbio.3001474.ref052) 1997; 272
T Biederer (pbio.3001474.ref014) 1997; 278
H Lin (pbio.3001474.ref085) 1999; 274
RW Hooft (pbio.3001474.ref092) 1996; 381
AA Gooden (pbio.3001474.ref079) 2020
ML van de Weijer (pbio.3001474.ref021) 2020; 79
NW Bays (pbio.3001474.ref005) 2001; 3
B Mueller (pbio.3001474.ref057) 2006; 175
B Chen (pbio.3001474.ref023) 2006; 103
MA Wangeline (pbio.3001474.ref010) 2017; 33
MB Metzger (pbio.3001474.ref044) 2008; 283
T Biederer (pbio.3001474.ref012) 1996; 15
T Sommer (pbio.3001474.ref013) 1993; 365
ML van de Weijer (pbio.3001474.ref076) 2014; 5
YS Tsao (pbio.3001474.ref056) 1992; 116
BG Peterson (pbio.3001474.ref067) 2019; 8
C Lips (pbio.3001474.ref077) 2020; 2020
SA Menzies (pbio.3001474.ref022) 2018; 7
Y Jo (pbio.3001474.ref061) 2011; 286
JP Jensen (pbio.3001474.ref065) 1995; 270
PM Deak (pbio.3001474.ref006) 2001; 276
E Nadav (pbio.3001474.ref032) 2003; 303
DJ van den Boomen (pbio.3001474.ref075) 2014; 111
J Spandl (pbio.3001474.ref037) 2011; 286
NF Bence (pbio.3001474.ref045) 2005; 399
Z Sun (pbio.3001474.ref002) 2019; 218
P Carvalho (pbio.3001474.ref008) 2006; 126
M Kaneko (pbio.3001474.ref020) 2016; 6
R Das (pbio.3001474.ref024) 2013; 32
M Kikkert (pbio.3001474.ref031) 2004; 279
YC Tsai (pbio.3001474.ref028) 2007; 13
RD Baldridge (pbio.3001474.ref066) 2016; 166
EJ Klemm (pbio.3001474.ref035) 2011; 286
T Gilon (pbio.3001474.ref042) 1998; 17
W Minor (pbio.3001474.ref088) 2006; 62
M Kaneko (pbio.3001474.ref033) 2002; 532
AB Mehrtash (pbio.3001474.ref004) 2019; 93
T Ravid (pbio.3001474.ref070) 2007; 9
A Stevanovic (pbio.3001474.ref038) 2013; 54
T Ravid (pbio.3001474.ref046) 2006; 25
ZS Hann (pbio.3001474.ref071) 2019; 75
D Morito (pbio.3001474.ref026) 2008; 19
D Lohmann (pbio.3001474.ref036) 2013; 8
JA Olzmann (pbio.3001474.ref049) 2011; 286
B Mueller (pbio.3001474.ref054) 2008; 105
P Emsley (pbio.3001474.ref090) 2004; 60
S Li (pbio.3001474.ref081) 2015; 290
M von Delbrück (pbio.3001474.ref016) 2016; 62
Z Kostova (pbio.3001474.ref018) 2009; 122
TK Watanabe (pbio.3001474.ref063) 1996; 74
T Gilon (pbio.3001474.ref043) 2000; 20
JL Goldstein (pbio.3001474.ref087) 1983; 98
R Swanson (pbio.3001474.ref007) 2001; 15
JH Claessen (pbio.3001474.ref072) 2010; 285
S Neal (pbio.3001474.ref058) 2019; 619
JC Christianson (pbio.3001474.ref051) 2008; 10
DM Walter (pbio.3001474.ref080) 2017; 77
R Laskowski (pbio.3001474.ref091) 1993; 26
HL Ploegh (pbio.3001474.ref048) 2007; 448
S Tiwari (pbio.3001474.ref029) 2001; 276
G Hassink (pbio.3001474.ref034) 2005; 388
K Bagola (pbio.3001474.ref015) 2013; 50
V Vasic (pbio.3001474.ref068) 2020; 22
MB Metzger (pbio.3001474.ref019) 2013; 50
AM Weissman (pbio.3001474.ref073) 2011; 12
X Wu (pbio.3001474.ref074) 2020; 368
Y Jo (pbio.3001474.ref060) 2011; 108
ML Burr (pbio.3001474.ref064) 2011; 108
S Fang (pbio.3001474.ref025) 2001; 98
KL Lorick (pbio.3001474.ref086) 1999; 96
Y Jo (pbio.3001474.ref050) 2013; 24
W Li (pbio.3001474.ref030) 2009; 106
A Bhattacharya (pbio.3001474.ref003) 2019; 132
DE Leto (pbio.3001474.ref040) 2019; 73
EA Whitcomb (pbio.3001474.ref083) 2019; 33
References_xml – volume: 368
  issue: 6489
  year: 2020
  ident: pbio.3001474.ref074
  article-title: Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex
  publication-title: Science
  contributor:
    fullname: X Wu
– volume: 218
  start-page: 3171
  issue: 10
  year: 2019
  ident: pbio.3001474.ref002
  article-title: Protein quality control in the secretory pathway
  publication-title: J Cell Biol
  doi: 10.1083/jcb.201906047
  contributor:
    fullname: Z Sun
– volume: 5
  start-page: 3832
  year: 2014
  ident: pbio.3001474.ref076
  article-title: A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation.
  publication-title: Nat Commun
  doi: 10.1038/ncomms4832
  contributor:
    fullname: ML van de Weijer
– volume: 6
  start-page: 902
  issue: 5
  year: 2017
  ident: pbio.3001474.ref078
  article-title: sgRNA Scorer 2.0: A Species-Independent Model To Predict CRISPR/Cas9 Activity.
  publication-title: ACS Synth Biol
  doi: 10.1021/acssynbio.6b00343
  contributor:
    fullname: R Chari
– volume: 20
  start-page: 7214
  issue: 19
  year: 2000
  ident: pbio.3001474.ref043
  article-title: Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair
  publication-title: Mol Cell Biol
  doi: 10.1128/MCB.20.19.7214-7219.2000
  contributor:
    fullname: T Gilon
– volume: 111
  start-page: 11425
  issue: 31
  year: 2014
  ident: pbio.3001474.ref075
  article-title: TMEM129 is a Derlin-1 associated ERAD E3 ligase essential for virus-induced degradation of MHC-I
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1409099111
  contributor:
    fullname: DJ van den Boomen
– volume: 33
  start-page: 467
  year: 2017
  ident: pbio.3001474.ref010
  article-title: Proteostatic Tactics in the Strategy of Sterol Regulation
  publication-title: Annu Rev Cell Dev Biol
  doi: 10.1146/annurev-cellbio-111315-125036
  contributor:
    fullname: MA Wangeline
– volume: 8
  start-page: e72453
  issue: 9
  year: 2013
  ident: pbio.3001474.ref036
  article-title: Monoubiquitination of ancient ubiquitous protein 1 promotes lipid droplet clustering
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0072453
  contributor:
    fullname: D Lohmann
– volume: 286
  start-page: 27872
  issue: 32
  year: 2011
  ident: pbio.3001474.ref049
  article-title: Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation
  publication-title: J Biol Chem
  doi: 10.1074/jbc.C111.266452
  contributor:
    fullname: JA Olzmann
– volume: 279
  start-page: 3525
  issue: 5
  year: 2004
  ident: pbio.3001474.ref031
  article-title: Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M307453200
  contributor:
    fullname: M Kikkert
– volume: 98
  start-page: 241
  year: 1983
  ident: pbio.3001474.ref087
  article-title: Receptor-mediated endocytosis of low-density lipoprotein in cultured cells
  publication-title: Methods Enzymol
  doi: 10.1016/0076-6879(83)98152-1
  contributor:
    fullname: JL Goldstein
– volume: 26
  start-page: 2263
  issue: 16
  year: 2007
  ident: pbio.3001474.ref082
  article-title: RING-dependent tumor suppression and G2/M arrest induced by the TRC8 hereditary kidney cancer gene
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1210017
  contributor:
    fullname: A Brauweiler
– volume: 5
  issue: 9
  year: 2013
  ident: pbio.3001474.ref001
  article-title: The mammalian endoplasmic reticulum-associated degradation system.
  publication-title: Cold Spring Harb Perspect Biol
  doi: 10.1101/cshperspect.a013185
  contributor:
    fullname: JA Olzmann
– volume: 365
  start-page: 176
  issue: 6442
  year: 1993
  ident: pbio.3001474.ref013
  article-title: A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
  publication-title: Nature
  doi: 10.1038/365176a0
  contributor:
    fullname: T Sommer
– volume: 272
  start-page: 7946
  issue: 12
  year: 1997
  ident: pbio.3001474.ref052
  article-title: Intracellular disposal of incompletely folded human alpha1-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides
  publication-title: J Biol Chem
  doi: 10.1074/jbc.272.12.7946
  contributor:
    fullname: Y Liu
– volume: 381
  start-page: 272
  issue: 6580
  year: 1996
  ident: pbio.3001474.ref092
  article-title: Errors in protein structures
  publication-title: Nature
  doi: 10.1038/381272a0
  contributor:
    fullname: RW Hooft
– volume: 24
  start-page: 169
  issue: 3
  year: 2013
  ident: pbio.3001474.ref050
  article-title: Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in lipid droplet-associated endoplasmic reticulum membranes
  publication-title: Mol Biol Cell
  doi: 10.1091/mbc.e12-07-0564
  contributor:
    fullname: Y Jo
– volume: 2020
  start-page: e104863
  year: 2020
  ident: pbio.3001474.ref077
  article-title: Who with whom: functional coordination of E2 enzymes by RING E3 ligases during poly-ubiquitylation
  publication-title: EMBO J
  doi: 10.15252/embj.2020104863
  contributor:
    fullname: C Lips
– volume: 26
  start-page: 283
  year: 1993
  ident: pbio.3001474.ref091
  article-title: PROCHECK: A program to check the stereochemical quality of protein structures
  publication-title: J Appl Crystallogr
  doi: 10.1107/S0021889892009944
  contributor:
    fullname: R Laskowski
– volume: 286
  start-page: 15022
  issue: 17
  year: 2011
  ident: pbio.3001474.ref061
  article-title: Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M110.211326
  contributor:
    fullname: Y Jo
– volume: 110
  start-page: 489
  issue: 4
  year: 2002
  ident: pbio.3001474.ref084
  article-title: Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
  publication-title: Cell
  doi: 10.1016/S0092-8674(02)00872-3
  contributor:
    fullname: T Yang
– volume: 15
  start-page: 2069
  issue: 9
  year: 1996
  ident: pbio.3001474.ref012
  article-title: Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway
  publication-title: EMBO J
  doi: 10.1002/j.1460-2075.1996.tb00560.x
  contributor:
    fullname: T Biederer
– volume: 25
  start-page: 794
  issue: 5
  year: 2017
  ident: pbio.3001474.ref069
  article-title: Conformational Dynamics and Allostery in E2:E3 Interactions Drive Ubiquitination: gp78 and Ube2g2
  publication-title: Structure
  doi: 10.1016/j.str.2017.03.016
  contributor:
    fullname: KS Chakrabarti
– volume: 274
  start-page: 14685
  issue: 21
  year: 1999
  ident: pbio.3001474.ref085
  article-title: Identification of rabbit reticulocyte E217K as a UBC7 homologue and functional characterization of its core domain loop
  publication-title: J Biol Chem
  doi: 10.1074/jbc.274.21.14685
  contributor:
    fullname: H Lin
– volume: 286
  start-page: 5599
  issue: 7
  year: 2011
  ident: pbio.3001474.ref037
  article-title: Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region.
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M110.190785
  contributor:
    fullname: J Spandl
– volume: 103
  start-page: 341
  issue: 2
  year: 2006
  ident: pbio.3001474.ref023
  article-title: The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0506618103
  contributor:
    fullname: B Chen
– volume: 34
  start-page: 212
  issue: 2
  year: 2009
  ident: pbio.3001474.ref059
  article-title: Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2009.03.010
  contributor:
    fullname: BK Sato
– volume: 50
  start-page: 516
  issue: 4
  year: 2013
  ident: pbio.3001474.ref019
  article-title: A structurally unique E2-binding domain activates ubiquitination by the ERAD E2, Ubc7p, through multiple mechanisms
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2013.04.004
  contributor:
    fullname: MB Metzger
– volume: 285
  start-page: 20732
  issue: 27
  year: 2010
  ident: pbio.3001474.ref072
  article-title: The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M110.120766
  contributor:
    fullname: JH Claessen
– volume: 7
  year: 2018
  ident: pbio.3001474.ref022
  article-title: The sterol-responsive RNF145 E3 ubiquitin ligase mediates the degradation of HMG-CoA reductase together with gp78 and Hrd1.
  publication-title: Elife
  doi: 10.7554/eLife.40009
  contributor:
    fullname: SA Menzies
– volume: 276
  start-page: 16193
  issue: 19
  year: 2001
  ident: pbio.3001474.ref029
  article-title: Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s).
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M007640200
  contributor:
    fullname: S Tiwari
– volume: 283
  start-page: 32302
  issue: 47
  year: 2008
  ident: pbio.3001474.ref044
  article-title: Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M806424200
  contributor:
    fullname: MB Metzger
– volume: 50
  start-page: 528
  issue: 4
  year: 2013
  ident: pbio.3001474.ref015
  article-title: Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2013.04.005
  contributor:
    fullname: K Bagola
– volume: 399
  start-page: 481
  year: 2005
  ident: pbio.3001474.ref045
  article-title: Application and analysis of the GFPu family of ubiquitin-proteasome system reporters
  publication-title: Methods Enzymol
  doi: 10.1016/S0076-6879(05)99033-2
  contributor:
    fullname: NF Bence
– volume: 166
  start-page: 394
  issue: 2
  year: 2016
  ident: pbio.3001474.ref066
  article-title: Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD
  publication-title: Cell
  doi: 10.1016/j.cell.2016.05.048
  contributor:
    fullname: RD Baldridge
– volume: 60
  start-page: 2126
  issue: Pt 12
  year: 2004
  ident: pbio.3001474.ref090
  article-title: Coot: model-building tools for molecular graphics
  publication-title: Acta Crystallogr D Biol Crystallogr
  doi: 10.1107/S0907444904019158
  contributor:
    fullname: P Emsley
– volume: 22
  start-page: 274
  issue: 3
  year: 2020
  ident: pbio.3001474.ref068
  article-title: Hrd1 forms the retrotranslocation pore regulated by auto-ubiquitination and binding of misfolded proteins
  publication-title: Nat Cell Biol
  doi: 10.1038/s41556-020-0473-4
  contributor:
    fullname: V Vasic
– volume: 12
  start-page: 605
  issue: 9
  year: 2011
  ident: pbio.3001474.ref073
  article-title: The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation
  publication-title: Nat Rev Mol Cell Biol
  doi: 10.1038/nrm3173
  contributor:
    fullname: AM Weissman
– volume: 62
  start-page: 859
  issue: Pt 8
  year: 2006
  ident: pbio.3001474.ref088
  article-title: HKL-3000: the integration of data reduction and structure solution—from diffraction images to an initial model in minutes
  publication-title: Acta Crystallogr D Biol Crystallogr
  doi: 10.1107/S0907444906019949
  contributor:
    fullname: W Minor
– volume: 388
  start-page: 647
  issue: Pt 2
  year: 2005
  ident: pbio.3001474.ref034
  article-title: TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
  publication-title: Biochem J
  doi: 10.1042/BJ20041241
  contributor:
    fullname: G Hassink
– volume: 9
  start-page: 422
  issue: 4
  year: 2007
  ident: pbio.3001474.ref070
  article-title: Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue
  publication-title: Nat Cell Biol
  doi: 10.1038/ncb1558
  contributor:
    fullname: T Ravid
– volume: 33
  start-page: 1235
  issue: 1
  year: 2019
  ident: pbio.3001474.ref083
  article-title: Stabilization of p27(Kip1)/CDKN1B by UBCH7/UBE2L3 catalyzed ubiquitinylation: a new paradigm in cell-cycle control.
  publication-title: FASEB J
  doi: 10.1096/fj.201800960R
  contributor:
    fullname: EA Whitcomb
– volume: 34
  start-page: 674
  issue: 6
  year: 2009
  ident: pbio.3001474.ref017
  article-title: Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2009.05.010
  contributor:
    fullname: R Das
– volume: 19
  start-page: 1328
  issue: 4
  year: 2008
  ident: pbio.3001474.ref026
  article-title: Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508
  publication-title: Mol Biol Cell
  doi: 10.1091/mbc.e07-06-0601
  contributor:
    fullname: D Morito
– volume: 303
  start-page: 91
  issue: 1
  year: 2003
  ident: pbio.3001474.ref032
  article-title: A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/S0006-291X(03)00279-1
  contributor:
    fullname: E Nadav
– volume: 105
  start-page: 12325
  issue: 34
  year: 2008
  ident: pbio.3001474.ref054
  article-title: SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0805371105
  contributor:
    fullname: B Mueller
– volume: 3
  start-page: 24
  issue: 1
  year: 2001
  ident: pbio.3001474.ref005
  article-title: Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
  publication-title: Nat Cell Biol
  doi: 10.1038/35050524
  contributor:
    fullname: NW Bays
– volume: 13
  start-page: 1504
  issue: 12
  year: 2007
  ident: pbio.3001474.ref028
  article-title: The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation
  publication-title: Nat Med
  doi: 10.1038/nm1686
  contributor:
    fullname: YC Tsai
– volume: 276
  start-page: 10663
  issue: 14
  year: 2001
  ident: pbio.3001474.ref006
  article-title: Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation.
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M008608200
  contributor:
    fullname: PM Deak
– volume: 75
  start-page: 552
  issue: Pt 8
  year: 2019
  ident: pbio.3001474.ref071
  article-title: Crystal structure of the Schizosaccharomyces pombe U7BR E2-binding region in complex with Ubc7
  publication-title: Acta Crystallogr F Struct Biol Commun
  doi: 10.1107/S2053230X19009786
  contributor:
    fullname: ZS Hann
– volume: 286
  start-page: 37602
  issue: 43
  year: 2011
  ident: pbio.3001474.ref035
  article-title: Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control.
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M111.284794
  contributor:
    fullname: EJ Klemm
– volume: 619
  start-page: 1
  year: 2019
  ident: pbio.3001474.ref058
  article-title: Assays for protein retrotranslocation in ERAD
  publication-title: Methods Enzymol
  doi: 10.1016/bs.mie.2019.01.002
  contributor:
    fullname: S Neal
– volume: 25
  start-page: 533
  issue: 3
  year: 2006
  ident: pbio.3001474.ref046
  article-title: Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
  publication-title: EMBO J
  doi: 10.1038/sj.emboj.7600946
  contributor:
    fullname: T Ravid
– volume: 77
  start-page: 1719
  issue: 7
  year: 2017
  ident: pbio.3001474.ref080
  article-title: Systematic In Vivo Inactivation of Chromatin-Regulating Enzymes Identifies Setd2 as a Potent Tumor Suppressor in Lung Adenocarcinoma
  publication-title: Cancer Res
  doi: 10.1158/0008-5472.CAN-16-2159
  contributor:
    fullname: DM Walter
– volume: 122
  start-page: 1374
  issue: Pt 9
  year: 2009
  ident: pbio.3001474.ref018
  article-title: A Ubc7p-binding domain in Cue1p activates ER-associated protein degradation
  publication-title: J Cell Sci
  doi: 10.1242/jcs.044255
  contributor:
    fullname: Z Kostova
– volume: 116
  start-page: 57
  issue: 1
  year: 1992
  ident: pbio.3001474.ref056
  article-title: Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process
  publication-title: J Cell Biol
  doi: 10.1083/jcb.116.1.57
  contributor:
    fullname: YS Tsao
– volume: 126
  start-page: 361
  issue: 2
  year: 2006
  ident: pbio.3001474.ref008
  article-title: Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
  publication-title: Cell
  doi: 10.1016/j.cell.2006.05.043
  contributor:
    fullname: P Carvalho
– volume: 66
  start-page: 213
  issue: Pt 2
  year: 2010
  ident: pbio.3001474.ref089
  article-title: PHENIX: a comprehensive Python-based system for macromolecular structure solution
  publication-title: Acta Crystallogr D Biol Crystallogr
  doi: 10.1107/S0907444909052925
  contributor:
    fullname: PD Adams
– volume: 448
  start-page: 435
  issue: 7152
  year: 2007
  ident: pbio.3001474.ref048
  article-title: A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum
  publication-title: Nature
  doi: 10.1038/nature06004
  contributor:
    fullname: HL Ploegh
– volume: 270
  start-page: 30408
  issue: 51
  year: 1995
  ident: pbio.3001474.ref065
  article-title: Identification of a family of closely related human ubiquitin conjugating enzymes
  publication-title: J Biol Chem
  doi: 10.1074/jbc.270.51.30408
  contributor:
    fullname: JP Jensen
– volume: 15
  start-page: 2660
  issue: 20
  year: 2001
  ident: pbio.3001474.ref007
  article-title: A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
  publication-title: Genes Dev
  doi: 10.1101/gad.933301
  contributor:
    fullname: R Swanson
– volume: 96
  start-page: 11364
  issue: 20
  year: 1999
  ident: pbio.3001474.ref086
  article-title: RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination.
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.96.20.11364
  contributor:
    fullname: KL Lorick
– volume: 175
  start-page: 261
  issue: 2
  year: 2006
  ident: pbio.3001474.ref057
  article-title: SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
  publication-title: J Cell Biol
  doi: 10.1083/jcb.200605196
  contributor:
    fullname: B Mueller
– volume: 108
  start-page: 2034
  issue: 5
  year: 2011
  ident: pbio.3001474.ref064
  article-title: HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1016229108
  contributor:
    fullname: ML Burr
– volume: 98
  start-page: 14422
  issue: 25
  year: 2001
  ident: pbio.3001474.ref025
  article-title: The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.251401598
  contributor:
    fullname: S Fang
– volume: 281
  start-page: 39308
  issue: 51
  year: 2006
  ident: pbio.3001474.ref047
  article-title: Sterol-regulated degradation of Insig-1 mediated by the membrane-bound ubiquitin ligase gp78
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M608999200
  contributor:
    fullname: JN Lee
– volume: 278
  start-page: 1806
  issue: 5344
  year: 1997
  ident: pbio.3001474.ref014
  article-title: Role of Cue1p in ubiquitination and degradation at the ER surface
  publication-title: Science
  doi: 10.1126/science.278.5344.1806
  contributor:
    fullname: T Biederer
– volume: 8
  year: 2019
  ident: pbio.3001474.ref067
  article-title: Cycles of autoubiquitination and deubiquitination regulate the ERAD ubiquitin ligase Hrd1.
  publication-title: Elife
  doi: 10.7554/eLife.50903
  contributor:
    fullname: BG Peterson
– volume: 108
  start-page: 20503
  issue: 51
  year: 2011
  ident: pbio.3001474.ref060
  article-title: Sterol-induced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1112831108
  contributor:
    fullname: Y Jo
– volume: 14
  start-page: 93
  issue: 1
  year: 2011
  ident: pbio.3001474.ref039
  article-title: Defining human ERAD networks through an integrative mapping strategy
  publication-title: Nat Cell Biol
  doi: 10.1038/ncb2383
  contributor:
    fullname: JC Christianson
– year: 2020
  ident: pbio.3001474.ref079
  article-title: dbGuide: a database of functionally validated guide RNAs for genome editing in human and mouse cells
  publication-title: Nucleic Acids Res
  contributor:
    fullname: AA Gooden
– volume: 93
  start-page: 111
  year: 2019
  ident: pbio.3001474.ref004
  article-title: Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope
  publication-title: Semin Cell Dev Biol
  doi: 10.1016/j.semcdb.2018.09.013
  contributor:
    fullname: AB Mehrtash
– volume: 54
  start-page: 503
  issue: 2
  year: 2013
  ident: pbio.3001474.ref038
  article-title: Monotopic topology is required for lipid droplet targeting of ancient ubiquitous protein 1
  publication-title: J Lipid Res
  doi: 10.1194/jlr.M033852
  contributor:
    fullname: A Stevanovic
– volume: 79
  start-page: 768
  issue: 5
  year: 2020
  ident: pbio.3001474.ref021
  article-title: Quality Control of ER Membrane Proteins by the RNF185/Membralin Ubiquitin Ligase Complex
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2020.07.009
  contributor:
    fullname: ML van de Weijer
– volume: 532
  start-page: 147
  issue: 1–2
  year: 2002
  ident: pbio.3001474.ref033
  article-title: Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
  publication-title: FEBS Lett
  doi: 10.1016/S0014-5793(02)03660-8
  contributor:
    fullname: M Kaneko
– volume: 74
  start-page: 146
  issue: 1–2
  year: 1996
  ident: pbio.3001474.ref063
  article-title: Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans
  publication-title: Cytogenet Cell Genet
  doi: 10.1159/000134403
  contributor:
    fullname: TK Watanabe
– volume: 290
  start-page: 30225
  issue: 51
  year: 2015
  ident: pbio.3001474.ref081
  article-title: Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M115.685867
  contributor:
    fullname: S Li
– volume: 17
  start-page: 2759
  issue: 10
  year: 1998
  ident: pbio.3001474.ref042
  article-title: Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
  publication-title: EMBO J
  doi: 10.1093/emboj/17.10.2759
  contributor:
    fullname: T Gilon
– volume: 165
  start-page: 41
  issue: 1
  year: 2004
  ident: pbio.3001474.ref009
  article-title: Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
  publication-title: J Cell Biol
  doi: 10.1083/jcb.200309132
  contributor:
    fullname: S Vashist
– volume: 293
  start-page: 4047
  issue: 11
  year: 2018
  ident: pbio.3001474.ref062
  article-title: Ring finger protein 145 (RNF145) is a ubiquitin ligase for sterol-induced degradation of HMG-CoA reductase.
  publication-title: J Biol Chem
  doi: 10.1074/jbc.RA117.001260
  contributor:
    fullname: LY Jiang
– volume: 6
  start-page: 30955
  year: 2016
  ident: pbio.3001474.ref020
  article-title: Genome-wide identification and gene expression profiling of ubiquitin ligases for endoplasmic reticulum protein degradation
  publication-title: Sci Rep
  doi: 10.1038/srep30955
  contributor:
    fullname: M Kaneko
– volume: 23
  start-page: 101493
  issue: 9
  year: 2020
  ident: pbio.3001474.ref011
  article-title: HRD Complex Self-Remodeling Enables a Novel Route of Membrane Protein Retrotranslocation.
  publication-title: iScience
  doi: 10.1016/j.isci.2020.101493
  contributor:
    fullname: S Neal
– volume: 263
  start-page: 7330
  issue: 15
  year: 1988
  ident: pbio.3001474.ref053
  article-title: A frameshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum
  publication-title: J Biol Chem
  doi: 10.1016/S0021-9258(18)68646-6
  contributor:
    fullname: RN Sifers
– volume: 10
  start-page: 272
  issue: 3
  year: 2008
  ident: pbio.3001474.ref051
  article-title: OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
  publication-title: Nat Cell Biol
  doi: 10.1038/ncb1689
  contributor:
    fullname: JC Christianson
– volume: 62
  start-page: 918
  issue: 6
  year: 2016
  ident: pbio.3001474.ref016
  article-title: The CUE Domain of Cue1 Aligns Growing Ubiquitin Chains with Ubc7 for
  publication-title: Rapid Elongation. Mol Cell
  doi: 10.1016/j.molcel.2016.04.031
  contributor:
    fullname: M von Delbrück
– volume: 32
  start-page: 2504
  issue: 18
  year: 2013
  ident: pbio.3001474.ref024
  article-title: Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine
  publication-title: EMBO J
  doi: 10.1038/emboj.2013.174
  contributor:
    fullname: R Das
– volume: 23
  start-page: 4484
  issue: 23
  year: 2012
  ident: pbio.3001474.ref055
  article-title: Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system
  publication-title: Mol Biol Cell
  doi: 10.1091/mbc.e12-08-0631
  contributor:
    fullname: YC Tsai
– volume: 132
  issue: 23
  year: 2019
  ident: pbio.3001474.ref003
  article-title: ER-associated degradation in health and disease—from substrate to organism
  publication-title: J Cell Sci
  doi: 10.1242/jcs.232850
  contributor:
    fullname: A Bhattacharya
– volume: 106
  start-page: 3722
  issue: 10
  year: 2009
  ident: pbio.3001474.ref030
  article-title: Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0808564106
  contributor:
    fullname: W Li
– volume: 20
  start-page: 2138
  issue: 12
  year: 2012
  ident: pbio.3001474.ref027
  article-title: Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains
  publication-title: Structure
  doi: 10.1016/j.str.2012.09.020
  contributor:
    fullname: S Liu
– volume: 73
  start-page: 377
  issue: 2
  year: 2019
  ident: pbio.3001474.ref040
  article-title: Genome-wide CRISPR Analysis Identifies Substrate-Specific Conjugation Modules in ER-Associated Degradation
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2018.11.015
  contributor:
    fullname: DE Leto
– volume: 19
  issue: 5)
  year: 2018
  ident: pbio.3001474.ref041
  article-title: MARCH6 and TRC8 facilitate the quality control of cytosolic and tail-anchored proteins
  publication-title: EMBO Rep
  contributor:
    fullname: S Stefanovic-Barrett
SSID ssj0022928
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Snippet Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple...
Endoplasmic reticulum–associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple...
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StartPage e3001474
SubjectTerms Amino Acid Sequence - genetics
Amino acids
Binding
Binding sites
Biology and Life Sciences
Bridges
Cell Line, Tumor
CRISPR
Degradation
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum-Associated Degradation - genetics
Endoplasmic Reticulum-Associated Degradation - physiology
Experiments
Homeostasis
Humans
Hydrogen bonding
Hydrogen bonds
Hydrophobicity
Lipids
Mammals
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membrane Proteins - physiology
Membrane Proteins - ultrastructure
Membranes
Mutagenesis
Mutation
Physical Sciences
Plasmids
Protein Binding - genetics
Protein Domains - genetics
Proteins
Quality control
Research and Analysis Methods
Substrates
Ubiquitin
Ubiquitin-conjugating enzyme
Ubiquitin-Conjugating Enzymes - genetics
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitin-Conjugating Enzymes - physiology
Ubiquitin-Conjugating Enzymes - ultrastructure
Ubiquitin-protein ligase
Ubiquitination
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Title A structurally conserved site in AUP1 binds the E2 enzyme UBE2G2 and is essential for ER-associated degradation
URI https://www.ncbi.nlm.nih.gov/pubmed/34879065
https://www.proquest.com/docview/2620104871/abstract/
https://www.proquest.com/docview/2608453302/abstract/
https://pubmed.ncbi.nlm.nih.gov/PMC8699718
https://doaj.org/article/1d1767c146ff4ca2be2d36cff2726f11
http://dx.doi.org/10.1371/journal.pbio.3001474
Volume 19
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