The physiological role of the free 20S proteasome in protein degradation: A critical review
It has been almost three decades since the removal of oxidized proteins by the free 20S catalytic unit of the proteasome (20SPT) was proposed. Since then, experimental evidence suggesting a physiological role of proteolysis mediated by the free 20SPT has being gathered. Experimental data that favors...
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| Published in | Biochimica et biophysica acta. General subjects Vol. 1862; no. 12; pp. 2948 - 2954 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
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Elsevier B.V
01.12.2018
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| Abstract | It has been almost three decades since the removal of oxidized proteins by the free 20S catalytic unit of the proteasome (20SPT) was proposed. Since then, experimental evidence suggesting a physiological role of proteolysis mediated by the free 20SPT has being gathered.
Experimental data that favors the hypothesis of free 20SPT as playing a role in proteolysis are critically reviewed.
Protein degradation by the proteasome may proceed through multiple proteasome complexes with different requirements though the unequivocal role of the free 20SPT in cellular proteolysis towards native or oxidized proteins remains to be demonstrated.
The biological significance of proteolysis mediated by the free 20SPT has been elusive since its discovery. The present review critically analyzes the available experimental data supporting the proteolytic role of the free or single capped 20SPT. |
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| AbstractList | It has been almost three decades since the removal of oxidized proteins by the free 20S catalytic unit of the proteasome (20SPT) was proposed. Since then, experimental evidence suggesting a physiological role of proteolysis mediated by the free 20SPT has being gathered.
Experimental data that favors the hypothesis of free 20SPT as playing a role in proteolysis are critically reviewed.
Protein degradation by the proteasome may proceed through multiple proteasome complexes with different requirements though the unequivocal role of the free 20SPT in cellular proteolysis towards native or oxidized proteins remains to be demonstrated.
The biological significance of proteolysis mediated by the free 20SPT has been elusive since its discovery. The present review critically analyzes the available experimental data supporting the proteolytic role of the free or single capped 20SPT. It has been almost three decades since the removal of oxidized proteins by the free 20S catalytic unit of the proteasome (20SPT) was proposed. Since then, experimental evidence suggesting a physiological role of proteolysis mediated by the free 20SPT has being gathered.BACKGROUNDIt has been almost three decades since the removal of oxidized proteins by the free 20S catalytic unit of the proteasome (20SPT) was proposed. Since then, experimental evidence suggesting a physiological role of proteolysis mediated by the free 20SPT has being gathered.Experimental data that favors the hypothesis of free 20SPT as playing a role in proteolysis are critically reviewed.SCOPE OF REVIEWExperimental data that favors the hypothesis of free 20SPT as playing a role in proteolysis are critically reviewed.Protein degradation by the proteasome may proceed through multiple proteasome complexes with different requirements though the unequivocal role of the free 20SPT in cellular proteolysis towards native or oxidized proteins remains to be demonstrated.MAJOR CONCLUSIONSProtein degradation by the proteasome may proceed through multiple proteasome complexes with different requirements though the unequivocal role of the free 20SPT in cellular proteolysis towards native or oxidized proteins remains to be demonstrated.The biological significance of proteolysis mediated by the free 20SPT has been elusive since its discovery. The present review critically analyzes the available experimental data supporting the proteolytic role of the free or single capped 20SPT.GENERAL SIGNIFICANCEThe biological significance of proteolysis mediated by the free 20SPT has been elusive since its discovery. The present review critically analyzes the available experimental data supporting the proteolytic role of the free or single capped 20SPT. It has been almost three decades since the removal of oxidized proteins by the free 20S catalytic unit of the proteasome (20SPT) was proposed. Since then, experimental evidence suggesting a physiological role of proteolysis mediated by the free 20SPT has being gathered.Experimental data that favors the hypothesis of free 20SPT as playing a role in proteolysis are critically reviewed.Protein degradation by the proteasome may proceed through multiple proteasome complexes with different requirements though the unequivocal role of the free 20SPT in cellular proteolysis towards native or oxidized proteins remains to be demonstrated.The biological significance of proteolysis mediated by the free 20SPT has been elusive since its discovery. The present review critically analyzes the available experimental data supporting the proteolytic role of the free or single capped 20SPT. |
| Author | da Cunha, Fernanda Marques Demasi, Marilene |
| Author_xml | – sequence: 1 givenname: Marilene surname: Demasi fullname: Demasi, Marilene email: marilene.demasi@butantan.gov.br organization: Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo, SP, Brazil – sequence: 2 givenname: Fernanda Marques surname: da Cunha fullname: da Cunha, Fernanda Marques email: fmcunha@unifesp.br organization: Departamento de Bioquímica, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, SP, Brazil |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30297324$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1042/BCJ20160762 10.1074/jbc.C400111200 10.1016/j.jmb.2013.01.036 10.1016/j.abb.2014.05.002 10.1016/S0021-9258(17)38440-5 10.1096/fasebj.12.7.561 10.1083/jcb.200803022 10.1096/fj.05-4049fje 10.1074/jbc.271.26.15504 10.1038/nrclinonc.2016.206 10.1016/S0021-9258(18)71571-8 10.1016/j.bbamcr.2013.05.008 10.1073/pnas.202480499 10.1016/j.cell.2005.11.037 10.1016/j.molcel.2010.12.020 10.1016/S0021-9258(17)35950-1 10.1038/cdd.2009.67 10.1089/ars.2011.4210 10.1016/S0021-9258(19)50047-3 10.1016/j.celrep.2018.07.004 10.1016/S0021-9258(18)82272-4 10.1042/BCJ20160582 10.1042/bj3350637 10.1042/BJ20090528 10.1016/j.molcel.2006.08.025 10.1016/j.jmb.2008.12.081 10.1074/jbc.270.19.11623 10.1126/science.1261197 10.1016/j.cell.2017.04.023 10.1016/j.molcel.2007.06.033 10.1016/j.abb.2012.04.018 10.1074/jbc.270.5.2344 10.1038/srep34432 10.1091/mbc.e04-06-0477 10.1016/S1093-3263(00)00138-8 10.1073/pnas.74.1.54 10.1016/0891-5849(89)90028-2 10.1074/jbc.M111.277145 10.1016/S0003-9861(02)00336-3 10.1006/jsbi.1993.1050 10.1038/nsmb.3389 10.1038/80992 10.1016/S0092-8674(94)90482-0 10.1016/j.freeradbiomed.2013.11.017 10.1016/j.ceb.2009.11.002 10.1016/j.bbrc.2012.01.152 10.1016/j.tibs.2017.09.002 10.1016/j.molcel.2018.06.013 10.1126/scisignal.2001232 10.1074/jbc.M115.648659 10.1074/jbc.M206279200 10.1074/jbc.M001555200 10.1007/s00294-017-0708-5 10.1016/S1097-2765(00)80435-9 10.1093/emboj/cdg436 10.1042/BJ20101027 10.1016/j.celrep.2014.04.030 10.1080/15548627.2017.1356549 10.1016/j.celrep.2014.07.055 10.1016/S0021-9258(18)47552-7 10.1002/prot.21614 10.1016/j.bbamcr.2011.07.009 10.1083/jcb.96.6.1580 10.1016/S0092-8674(94)90462-6 10.1016/S0021-9258(18)61525-X 10.1073/pnas.071022298 10.1038/331192a0 10.1126/science.7732382 10.1111/j.1471-4159.1983.tb08056.x 10.1146/annurev.biochem.68.1.1015 10.1016/j.molcel.2007.05.028 10.1016/j.freeradbiomed.2016.08.002 10.1016/S0021-9258(18)47553-9 10.1016/j.mam.2009.04.001 10.1074/jbc.M116.727578 |
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| Keywords | Ubiquitin-proteasome system Ubiquitin- and ATP-independent protein degradation Proteasomal complexes |
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| References | Ramachandran, Fu, Schaffer, Na, Delannoy, Margolis (bb0135) 2018; 71 Stadtmueller, Hill (bb0140) 2011; 41 Waxman, Fagan, Goldberg (bb0060) 1987; 262 Voges, Zwickl, Baumeister (bb0010) 1999; 68 Yu, Singh Gautam, Wilmington, Wylie, Martinez-Fonts, Kago, Warburton, Chavali, Inobe, Finkelstein, Babu, Matouschek (bb0225) 2016; 291 Melo, Yoshida, Berger (bb0275) 2010; 432 Shringarpure, Grune, Mehlhase, Davies (bb0350) 2003; 278 Reeg, Jung, Castro, Davies, Henze, Grune (bb0365) 2016; 99 Collins, Goldberg (bb0210) 2017; 169 Livnat-Levanon, Kevei, Kleifeld, Krutauz, Segref, Rinaldi, Erpapazoglou, Cohen, Reis, Hoppe, Glickman (bb0315) 2014; 7 Song, Lee, Cho, Jeong, Shin, Lee (bb0390) 2016; 6 S. Fishbain, T. Inobe, E. Israeli, S. Chavali, H. Yu, G. Kago, M.M. Babu, A. Matouschek, Sequence composition of disordered regions fine-tunes protein half-life, Nat. Struct. Mol. Biol., 22 (2015) 214–221. Etlinger, Goldberg (bb0005) 1977; 74 Tarcsa, Szymanska, Lecker, O'Connor, Goldberg (bb0240) 2000; 275 Savulesku, Glickman (bb0180) 2011; 10 Demishtein, Fraiberg, Berko, Tirosh, Elazar, Navon (bb0340) 2017; 13 Palombella, Rando, Goldberg, Maniatis (bb0035) 1994; 78 Bercovich, Rosenberg-Hasson, Ciechanover, Kahana (bb0230) 1989; 264 Arrigo, Tanaka, Goldberg, Welch (bb0015) 1988; 331 Pickering, Davies (bb0325) 2012; 523 Rock, Gramm, Rothstein, Clark, Stein, Dick, Hwang, Goldberg (bb0030) 1994; 78 Grune, Reinheckel, Davies (bb0360) 1996; 271 Dudek, Shang, Valverde, Liu, Hobbs, Taylor (bb0385) 2005; 19 Ramachandran, Margolis (bb0130) 2017; 24 Xie, Varshavsky (bb0335) 2001; 98 Preston, Brodsky (bb0380) 2017; 474 Davies, Kj (bb0075) 1987; 262 Asano, Fukuda, Beck, Aufderheide, Förster, Danev, Baumeister (bb0105) 2015; 347 Dal Vechio, Cerqueira, Augusto, Lopes, Demasi (bb0205) 2014; 67 Ma, Slaughter, Demartino (bb0095) 1992; 267 Jung, Catalgol, Grune (bb0085) 2009; 30 Demasi, Hand, Ohara, Oliveira, Bicev, Bertoncini, Netto (bb0190) 2014; 557 Jariel-Encontre, Pariat, Martin, Carillo, Salvat, Piechaczyk (bb0235) 1995; 270 Pacifici, Konosll, Daviesll (bb0200) 1993; 268 Asher, Lotem, Sachs, Kahana, Shaul (bb0125) 2002; 99 Baugh, Viktorova, Pilipenko (bb0115) 2009; 386 Sledz, Förster, Baumeister (bb0160) 2013; 425 Wang, Yen, Kaiser, Huang (bb0310) 2010; 3 Kwon, Ciechanover (bb0020) 2017; 42 Silva, Netto, Simões, Santos, Gozzo, Demasi, Oliveira, Bicev, Klitzke, Sogayar, Demasi (bb0185) 2012; 16 Yoshimura, Kameyama, Takagi, Ikai, Tokunaga, Koide, Tanahashi, Tamura, Cejka, Baumeister (bb0090) 1993; 111 Tsvetkov, Reuven, Shaul (bb0245) 2010; 17 Kiffin, Christian, Knecht, Cuervo (bb0395) 2004; 15 Dunker, Lawson, Brown, Williams, Romero, Oh, Oldfield, Campen, Ratliff, Hipps (bb0280) 2001; 19 Li, Lonard, Jung, Malovannaya, Feng, Qin, Tsai, Tsai, O'Malley (bb0295) 2006; 124 Fagan, Waxman, Goldberg (bb0065) 1986; 261 Eisele, Reed, Rudack, Schweitzer, Beck, Nagy, Pfeifer, Plitzko, Baumeister, Tomko, Sakata (bb0175) 2018; 24 Lamark, Johansen (bb0345) 2010; 22 Smith, Chang, Park, Finley, Cheng, Goldberg (bb0165) 2007; 27 Bar-Nun, Glickman (bb0155) 2012; 1823 Pacifici, Salo, Davies (bb0080) 1989; 7 Davies, Goldberg (bb0070) 1987; 262 Pickering, Linder, Zhang, Forman, Davies (bb0100) 2012; 287 Foster, Whitby, Hill (bb0170) 2003; 22 Obin, Shang, Gong, Handelman, Blumberg, Taylor (bb0320) 1998; 12 Hough, Pratt, Rechsteiner (bb0055) 1987; 261 Collins, Wang, Caldwell, Chopra (bb0025) 2017; 474 Ju, Xie (bb0265) 2004; 279 Bajorek, Glickman (bb0195) 2004; 61 Erales, Coffino (bb0260) 2014; 1843 Grune, Reinheckel, Joshi, Davies (bb0355) 1995; 270 Li, Amazit, Long, Lonard, Monaco, O'Malley (bb0300) 2007; 26 Wilki, Orlowski (bb0050) 1983; 40 Groll, Bajorek, Köhler, Moroder, Rubin, Huber, Glickman, Finley (bb0145) 2000; 7 Hsieh, Su, Han, Carman (bb0255) 2015; 290 Myers, Olender, Savidor, Levin, Reuven, Shaul (bb0250) 2018 Sheaff, Singer, Swanger, Smitherman, Roberts, Clurman (bb0120) 2000; 5 Reinheckel, Sitte, Ullrich, Kuckelkorn, Davies, Grune (bb0305) 1998; 335 Manasanch, Orlowski (bb0045) 2017; 14 Tsvetkov, Asher, Paz, Reuven, Sussman, Silman, Shaul (bb0110) 2008; 70 Inai, Nishikimi (bb0330) 2002; 404 Fenteany, Standaert, Lane, Choi, Corey, Schreiber (bb0040) 1995; 268 Liu, Li, Thompson, Wooding, Chang, Tang, Yu, Thomas, Demartino (bb0290) 2006; 24 Tanaka, Waxman, Goldberg (bb0285) 1983; 96 Li, Demartino (bb0150) 2009; 421 van der Lee, Lang, Kruse, Gsponer, Sánchez De Groot, Huynen, Matouschek, Fuxreiter, Babu (bb0215) 2014; 8 Medicherla, Goldberg (bb0370) 2008; 182 Ha, Ju, Xie (bb0270) 2012; 419 Defenouillère, Fromont-Racine (bb0375) 2017; 63 Davies (10.1016/j.bbagen.2018.09.009_bb0070) 1987; 262 Myers (10.1016/j.bbagen.2018.09.009_bb0250) 2018 Lamark (10.1016/j.bbagen.2018.09.009_bb0345) 2010; 22 Li (10.1016/j.bbagen.2018.09.009_bb0295) 2006; 124 Waxman (10.1016/j.bbagen.2018.09.009_bb0060) 1987; 262 Reinheckel (10.1016/j.bbagen.2018.09.009_bb0305) 1998; 335 Yu (10.1016/j.bbagen.2018.09.009_bb0225) 2016; 291 Fagan (10.1016/j.bbagen.2018.09.009_bb0065) 1986; 261 Palombella (10.1016/j.bbagen.2018.09.009_bb0035) 1994; 78 Asano (10.1016/j.bbagen.2018.09.009_bb0105) 2015; 347 Pickering (10.1016/j.bbagen.2018.09.009_bb0325) 2012; 523 Silva (10.1016/j.bbagen.2018.09.009_bb0185) 2012; 16 Preston (10.1016/j.bbagen.2018.09.009_bb0380) 2017; 474 Sledz (10.1016/j.bbagen.2018.09.009_bb0160) 2013; 425 Reeg (10.1016/j.bbagen.2018.09.009_bb0365) 2016; 99 Jariel-Encontre (10.1016/j.bbagen.2018.09.009_bb0235) 1995; 270 Erales (10.1016/j.bbagen.2018.09.009_bb0260) 2014; 1843 Collins (10.1016/j.bbagen.2018.09.009_bb0210) 2017; 169 van der Lee (10.1016/j.bbagen.2018.09.009_bb0215) 2014; 8 Tsvetkov (10.1016/j.bbagen.2018.09.009_bb0110) 2008; 70 Savulesku (10.1016/j.bbagen.2018.09.009_bb0180) 2011; 10 Wang (10.1016/j.bbagen.2018.09.009_bb0310) 2010; 3 Tanaka (10.1016/j.bbagen.2018.09.009_bb0285) 1983; 96 Melo (10.1016/j.bbagen.2018.09.009_bb0275) 2010; 432 Voges (10.1016/j.bbagen.2018.09.009_bb0010) 1999; 68 Ramachandran (10.1016/j.bbagen.2018.09.009_bb0135) 2018; 71 Dudek (10.1016/j.bbagen.2018.09.009_bb0385) 2005; 19 Baugh (10.1016/j.bbagen.2018.09.009_bb0115) 2009; 386 Rock (10.1016/j.bbagen.2018.09.009_bb0030) 1994; 78 Tsvetkov (10.1016/j.bbagen.2018.09.009_bb0245) 2010; 17 Pickering (10.1016/j.bbagen.2018.09.009_bb0100) 2012; 287 Livnat-Levanon (10.1016/j.bbagen.2018.09.009_bb0315) 2014; 7 Etlinger (10.1016/j.bbagen.2018.09.009_bb0005) 1977; 74 Dunker (10.1016/j.bbagen.2018.09.009_bb0280) 2001; 19 Shringarpure (10.1016/j.bbagen.2018.09.009_bb0350) 2003; 278 Wilki (10.1016/j.bbagen.2018.09.009_bb0050) 1983; 40 Hough (10.1016/j.bbagen.2018.09.009_bb0055) 1987; 261 Ramachandran (10.1016/j.bbagen.2018.09.009_bb0130) 2017; 24 Stadtmueller (10.1016/j.bbagen.2018.09.009_bb0140) 2011; 41 Medicherla (10.1016/j.bbagen.2018.09.009_bb0370) 2008; 182 10.1016/j.bbagen.2018.09.009_bb0220 Kwon (10.1016/j.bbagen.2018.09.009_bb0020) 2017; 42 Eisele (10.1016/j.bbagen.2018.09.009_bb0175) 2018; 24 Smith (10.1016/j.bbagen.2018.09.009_bb0165) 2007; 27 Ju (10.1016/j.bbagen.2018.09.009_bb0265) 2004; 279 Obin (10.1016/j.bbagen.2018.09.009_bb0320) 1998; 12 Pacifici (10.1016/j.bbagen.2018.09.009_bb0200) 1993; 268 Dal Vechio (10.1016/j.bbagen.2018.09.009_bb0205) 2014; 67 Bar-Nun (10.1016/j.bbagen.2018.09.009_bb0155) 2012; 1823 Bajorek (10.1016/j.bbagen.2018.09.009_bb0195) 2004; 61 Collins (10.1016/j.bbagen.2018.09.009_bb0025) 2017; 474 Asher (10.1016/j.bbagen.2018.09.009_bb0125) 2002; 99 Xie (10.1016/j.bbagen.2018.09.009_bb0335) 2001; 98 Jung (10.1016/j.bbagen.2018.09.009_bb0085) 2009; 30 Fenteany (10.1016/j.bbagen.2018.09.009_bb0040) 1995; 268 Grune (10.1016/j.bbagen.2018.09.009_bb0360) 1996; 271 Hsieh (10.1016/j.bbagen.2018.09.009_bb0255) 2015; 290 Groll (10.1016/j.bbagen.2018.09.009_bb0145) 2000; 7 Grune (10.1016/j.bbagen.2018.09.009_bb0355) 1995; 270 Li (10.1016/j.bbagen.2018.09.009_bb0300) 2007; 26 Liu (10.1016/j.bbagen.2018.09.009_bb0290) 2006; 24 Tarcsa (10.1016/j.bbagen.2018.09.009_bb0240) 2000; 275 Li (10.1016/j.bbagen.2018.09.009_bb0150) 2009; 421 Foster (10.1016/j.bbagen.2018.09.009_bb0170) 2003; 22 Bercovich (10.1016/j.bbagen.2018.09.009_bb0230) 1989; 264 Inai (10.1016/j.bbagen.2018.09.009_bb0330) 2002; 404 Manasanch (10.1016/j.bbagen.2018.09.009_bb0045) 2017; 14 Ha (10.1016/j.bbagen.2018.09.009_bb0270) 2012; 419 Pacifici (10.1016/j.bbagen.2018.09.009_bb0080) 1989; 7 Defenouillère (10.1016/j.bbagen.2018.09.009_bb0375) 2017; 63 Arrigo (10.1016/j.bbagen.2018.09.009_bb0015) 1988; 331 Demasi (10.1016/j.bbagen.2018.09.009_bb0190) 2014; 557 Song (10.1016/j.bbagen.2018.09.009_bb0390) 2016; 6 Demishtein (10.1016/j.bbagen.2018.09.009_bb0340) 2017; 13 Kiffin (10.1016/j.bbagen.2018.09.009_bb0395) 2004; 15 Yoshimura (10.1016/j.bbagen.2018.09.009_bb0090) 1993; 111 Ma (10.1016/j.bbagen.2018.09.009_bb0095) 1992; 267 Sheaff (10.1016/j.bbagen.2018.09.009_bb0120) 2000; 5 Davies (10.1016/j.bbagen.2018.09.009_bb0075) 1987; 262 |
| References_xml | – volume: 261 start-page: 2400 year: 1987 end-page: 2408 ident: bb0055 article-title: Ubiquitin-lysozyme conjugates Identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates publication-title: J. Biol. Chem. – volume: 262 start-page: 2451 year: 1987 end-page: 2457 ident: bb0060 article-title: Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates publication-title: J. Biol. Chem. – volume: 8 start-page: 1832 year: 2014 end-page: 1844 ident: bb0215 article-title: Intrinsically disordered segments affect protein half-life in the cell and during evolution publication-title: Cell Rep. – volume: 335 start-page: 637 year: 1998 end-page: 642 ident: bb0305 article-title: Comparative resistance of the 20S and 26S proteasome to oxidative stress publication-title: Biochem. J. – volume: 40 start-page: 842 year: 1983 end-page: 849 ident: bb0050 article-title: Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex publication-title: J. Neurochem. – volume: 432 start-page: 217 year: 2010 end-page: 226 ident: bb0275 article-title: Functional dissection of the N-terminal degron of human thymidylate synthase publication-title: Biochem. J. – volume: 19 start-page: 26 year: 2001 end-page: 59 ident: bb0280 article-title: Intrinsically disordered protein publication-title: J. Mol. Graph. Model – volume: 264 start-page: 15949 year: 1989 end-page: 15952 ident: bb0230 article-title: Degradation of ornithine decarboxylase in reticulocyte lysate is ATP-dependent but ubiquitin-independent publication-title: J. Biol. Chem. – volume: 6 start-page: 34432 year: 2016 end-page: 34446 ident: bb0390 article-title: Degradation of redox-sensitive proteins including peroxiredoxins and DJ-1 is promoted by oxidation-induced conformational changes and ubiquitination publication-title: Sci. Rep. – volume: 262 start-page: 8227 year: 1987 end-page: 8234 ident: bb0075 article-title: Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells publication-title: J. Biol. Chem. – volume: 474 start-page: 1127 year: 2017 end-page: 1147 ident: bb0025 article-title: Chemical approaches to targeted protein degradation through modulation of the ubiquitin–proteasome pathway publication-title: Biochem. J. – volume: 16 start-page: 1183 year: 2012 end-page: 1194 ident: bb0185 article-title: Redox control of 20S proteasome gating publication-title: Antioxid. Redox Signal. – volume: 290 start-page: 11467 year: 2015 end-page: 11478 ident: bb0255 article-title: Phosphorylation regulates the ubiquitin-independent degradation of yeast Pah1 phosphatidate phosphatase by the 20S proteasome publication-title: J. Biol. Chem. – volume: 3 start-page: ra88 year: 2010 ident: bb0310 article-title: Regulation of the 26S proteasome complex during oxidative stress publication-title: Sci. Signal. – volume: 63 start-page: 997 year: 2017 end-page: 1005 ident: bb0375 article-title: The ribosome-bound quality control complex: from aberrant peptide clearance to proteostasis maintenance publication-title: Curr. Genet. – volume: 24 start-page: 39 year: 2006 end-page: 50 ident: bb0290 article-title: ATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome publication-title: Mol. Cell – year: 2018 ident: bb0250 article-title: The disordered landscape of the 20S proteasome substrates reveals tight association with phase separated granules publication-title: Proteomics – volume: 278 start-page: 311 year: 2003 end-page: 318 ident: bb0350 article-title: Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome publication-title: J. Biol. Chem. – volume: 74 start-page: 54 year: 1977 end-page: 58 ident: bb0005 article-title: A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 267 start-page: 10515 year: 1992 end-page: 10523 ident: bb0095 article-title: Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain) publication-title: J. Biol. Chem. – volume: 169 start-page: 792 year: 2017 end-page: 806 ident: bb0210 article-title: The logic of the 26S proteasome publication-title: Cell – volume: 270 start-page: 11623 year: 1995 end-page: 11627 ident: bb0235 article-title: Ubiquitylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome publication-title: J. Biol. Chem. – volume: 70 start-page: 1357 year: 2008 end-page: 1366 ident: bb0110 article-title: Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome publication-title: Proteins Struct. Funct. Bioinforma. – volume: 14 start-page: 417 year: 2017 end-page: 433 ident: bb0045 article-title: Proteasome inhibitors in cancer therapy publication-title: Nat. Rev. Clin. Oncol. – volume: 287 start-page: 10021 year: 2012 end-page: 10031 ident: bb0100 article-title: Nrf2-dependent induction of proteasome and Pa28αβ regulator are required for adaptation to oxidative stress publication-title: J. Biol. Chem. – volume: 523 start-page: 181 year: 2012 end-page: 190 ident: bb0325 article-title: Differential roles of proteasome and immunoproteasome regulators Pa28αβ, Pa28γ and Pa200 in the degradation of oxidized proteins publication-title: Arch. Biochem. Biophys. – volume: 15 start-page: 4829 year: 2004 end-page: 4840 ident: bb0395 article-title: Activation of chaperone-mediated autophagy during oxidative stress publication-title: Mol. Biol. Cell – volume: 331 start-page: 192 year: 1988 end-page: 194 ident: bb0015 article-title: Identity of the 19S “prosome” particle with the large multifunctional protease complex of mammalian cells (the proteasome) publication-title: Nature – volume: 275 start-page: 20295 year: 2000 end-page: 20301 ident: bb0240 article-title: Ca2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26 S proteasomes without ubiquitination publication-title: J. Biol. Chem. – volume: 291 start-page: 14526 year: 2016 end-page: 14539 ident: bb0225 article-title: Conserved sequence preferences contribute to substrate recognition by the proteasome publication-title: J. Biol. Chem. – volume: 7 start-page: 1 year: 2014 end-page: 10 ident: bb0315 article-title: Reversible 26S proteasome disassembly upon mitochondrial stress publication-title: Cell Rep. – volume: 98 start-page: 3056 year: 2001 end-page: 3061 ident: bb0335 article-title: RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 22 start-page: 192 year: 2010 end-page: 198 ident: bb0345 article-title: Autophagy: links with the proteasome publication-title: Curr. Opin. Cell Biol. – volume: 182 start-page: 663 year: 2008 end-page: 673 ident: bb0370 article-title: Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins publication-title: J. Cell Biol. – volume: 10 year: 2011 ident: bb0180 article-title: Proteasome Activator 200: the Heat is on… publication-title: Mol. Cell. Proteomics – volume: 5 start-page: 403 year: 2000 end-page: 410 ident: bb0120 article-title: Proteasomal turnover of p21Cip1 does not require p21Cip1 ubiquitination publication-title: Mol. Cell – volume: 42 start-page: 873 year: 2017 end-page: 886 ident: bb0020 article-title: The ubiquitin code in the ubiquitin-proteasome system and autophagy publication-title: Trends Biochem. Sci. – volume: 96 start-page: 1580 year: 1983 end-page: 1585 ident: bb0285 article-title: ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin publication-title: J. Cell Biol. – volume: 347 start-page: 439 year: 2015 end-page: 442 ident: bb0105 article-title: A molecular census of 26S proteasomes in intact neurons publication-title: Science – volume: 474 start-page: 445 year: 2017 end-page: 469 ident: bb0380 article-title: The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation publication-title: Biochem. J. – volume: 68 start-page: 1015 year: 1999 end-page: 1068 ident: bb0010 article-title: The 26S proteasome: a molecular machine designed for controlled proteolysis publication-title: Annu. Rev. Biochem. – volume: 279 start-page: 23851 year: 2004 end-page: 23854 ident: bb0265 article-title: Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and-independent publication-title: J. Biol. Chem. – volume: 1843 start-page: 216 year: 2014 end-page: 221 ident: bb0260 article-title: Ubiquitin-independent proteasomal degradation publication-title: Biochim. Biophys. Acta (BBA) Mol. Cell Res. – volume: 13 start-page: 1697 year: 2017 end-page: 1708 ident: bb0340 article-title: SQSTM1/p62-mediated autophagy compensates for loss of proteasome polyubiquitin recruiting capacity publication-title: Autophagy – volume: 67 start-page: 304 year: 2014 end-page: 313 ident: bb0205 article-title: Peptides that activate the 20S proteasome by gate opening increased oxidized protein removal and reduced protein aggregation publication-title: Free Radic. Biol. Med. – volume: 419 start-page: 226 year: 2012 end-page: 231 ident: bb0270 article-title: The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits publication-title: Biochem. Biophys. Res. Commun. – volume: 78 start-page: 773 year: 1994 end-page: 785 ident: bb0035 article-title: The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B publication-title: Cell – reference: S. Fishbain, T. Inobe, E. Israeli, S. Chavali, H. Yu, G. Kago, M.M. Babu, A. Matouschek, Sequence composition of disordered regions fine-tunes protein half-life, Nat. Struct. Mol. Biol., 22 (2015) 214–221. – volume: 425 start-page: 1415 year: 2013 end-page: 1423 ident: bb0160 article-title: Allosteric effects in the regulation of 26S proteasome activities publication-title: Mol. Biol. – volume: 61 start-page: 1579 year: 2004 end-page: 1588 ident: bb0195 article-title: Keepers at the final gates: regulatory complexes and gating of the proteasome channel publication-title: Cell. Mol. Life Sci. – volume: 41 start-page: 8 year: 2011 end-page: 19 ident: bb0140 article-title: Proteasome activators publication-title: Mol. Cell – volume: 71 start-page: 169 year: 2018 end-page: 177 ident: bb0135 article-title: Activity-dependent degradation of the nascentome by the neuronal membrane proteasome publication-title: Mol. Cell – volume: 270 start-page: 2344 year: 1995 end-page: 2351 ident: bb0355 article-title: Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome publication-title: J. Biol. Chem. – volume: 262 start-page: 8220 year: 1987 end-page: 8226 ident: bb0070 article-title: Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes publication-title: J. Biol. Chem. – volume: 421 start-page: 397 year: 2009 end-page: 404 ident: bb0150 article-title: Variably modulated gating of the 26S proteasome by ATP and polyubiquitin publication-title: Biochem. J. – volume: 7 start-page: 1062 year: 2000 end-page: 1067 ident: bb0145 article-title: A gated channel into the proteasome core particle publication-title: Nat. Struct. Biol. – volume: 22 start-page: 4356 year: 2003 end-page: 4364 ident: bb0170 article-title: The pore of activated 20S proteasome has an ordered 7-fold symmetric conformation publication-title: EMBO J. – volume: 1823 start-page: 67 year: 2012 end-page: 82 ident: bb0155 article-title: Proteasomal AAA-ATPases: structure and function publication-title: Biochim. Biophys. Acta – volume: 271 start-page: 15504 year: 1996 end-page: 15509 ident: bb0360 article-title: Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome publication-title: J. Biol. Chem. – volume: 268 start-page: 15405 year: 1993 end-page: 15411 ident: bb0200 article-title: Hydrophobicity as the signal for radical-modified hemoglobin by selective degradation of hydroxyl the multicatalytic proteinase publication-title: J. Biol. Chem. – volume: 386 start-page: 814 year: 2009 end-page: 827 ident: bb0115 article-title: Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination publication-title: J. Mol. Biol. – volume: 27 start-page: 731 year: 2007 end-page: 744 ident: bb0165 article-title: Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry publication-title: Mol. Cell – volume: 268 start-page: 726 year: 1995 end-page: 731 ident: bb0040 article-title: Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin publication-title: Science – volume: 111 start-page: 200 year: 1993 end-page: 211 ident: bb0090 article-title: Molecular characterization of the“ 26S” proteasome complex from rat liver publication-title: J. Struct. Biol. – volume: 78 start-page: 761 year: 1994 end-page: 771 ident: bb0030 article-title: Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules publication-title: Cell – volume: 17 start-page: 103 year: 2010 end-page: 108 ident: bb0245 article-title: Ubiquitin-independent p53 proteasomal degradation publication-title: Cell Death Differ. – volume: 261 start-page: 5705 year: 1986 end-page: 5713 ident: bb0065 article-title: Red blood cells contain a pathway for the degradation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin publication-title: J. Biol. Chem. – volume: 99 start-page: 153 year: 2016 end-page: 166 ident: bb0365 article-title: The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome publication-title: Free Radic. Biol. Med. – volume: 30 start-page: 191 year: 2009 end-page: 296 ident: bb0085 article-title: The proteasomal system publication-title: Mol. Aspects Med. – volume: 24 start-page: 419 year: 2017 end-page: 430 ident: bb0130 article-title: A mammalian nervous-system-specific plasma membrane proteasome complex that modulates neuronal function publication-title: Nat. Struct. Mol. Biol. – volume: 124 start-page: 381 year: 2006 end-page: 392 ident: bb0295 article-title: The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGγ proteasome publication-title: Cell – volume: 99 start-page: 13125 year: 2002 end-page: 13130 ident: bb0125 article-title: Mdm-2 and ubiquitin-independent p53 proteasomal degradation regulated by NQO1 publication-title: Proc. Natl. Acad. Sci. – volume: 404 start-page: 279 year: 2002 end-page: 284 ident: bb0330 article-title: Increased degradation of oxidized proteins in yeast defective in 26 S proteasome assembly publication-title: Arch. Biochem. Biophys. – volume: 19 start-page: 1707 year: 2005 end-page: 1709 ident: bb0385 article-title: Selectivity of the ubiquitin pathway for oxidatively modified proteins: relevance to protein precipitation diseases publication-title: FASEB J. – volume: 557 start-page: 65 year: 2014 end-page: 71 ident: bb0190 article-title: 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins publication-title: Arch. Biochem. Biophys. – volume: 26 start-page: 831 year: 2007 end-page: 842 ident: bb0300 article-title: Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGγ-proteasome pathway publication-title: Mol. Cell – volume: 24 start-page: 1301 year: 2018 end-page: 1315.e5 ident: bb0175 article-title: Expanded coverage of the 26 proteasome conformational landscape reveals mechanisms of peptidase gating publication-title: Cell Rep. – volume: 12 start-page: 561 year: 1998 end-page: 569 ident: bb0320 article-title: Redox regulation of ubiquitin-conjugating enzymes: mechanistic insights using the thiol-specific oxidant diamide publication-title: FASEB J. – volume: 7 start-page: 521 year: 1989 end-page: 536 ident: bb0080 article-title: Macroxyproteinase (MOP): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells publication-title: Free Radic. Biol. Med. – volume: 474 start-page: 1127 year: 2017 ident: 10.1016/j.bbagen.2018.09.009_bb0025 article-title: Chemical approaches to targeted protein degradation through modulation of the ubiquitin–proteasome pathway publication-title: Biochem. J. doi: 10.1042/BCJ20160762 – volume: 279 start-page: 23851 year: 2004 ident: 10.1016/j.bbagen.2018.09.009_bb0265 article-title: Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and-independent publication-title: J. Biol. Chem. doi: 10.1074/jbc.C400111200 – volume: 425 start-page: 1415 year: 2013 ident: 10.1016/j.bbagen.2018.09.009_bb0160 article-title: Allosteric effects in the regulation of 26S proteasome activities publication-title: Mol. Biol. doi: 10.1016/j.jmb.2013.01.036 – volume: 61 start-page: 1579 year: 2004 ident: 10.1016/j.bbagen.2018.09.009_bb0195 article-title: Keepers at the final gates: regulatory complexes and gating of the proteasome channel publication-title: Cell. Mol. Life Sci. – volume: 557 start-page: 65 year: 2014 ident: 10.1016/j.bbagen.2018.09.009_bb0190 article-title: 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2014.05.002 – volume: 261 start-page: 5705 year: 1986 ident: 10.1016/j.bbagen.2018.09.009_bb0065 article-title: Red blood cells contain a pathway for the degradation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)38440-5 – volume: 12 start-page: 561 year: 1998 ident: 10.1016/j.bbagen.2018.09.009_bb0320 article-title: Redox regulation of ubiquitin-conjugating enzymes: mechanistic insights using the thiol-specific oxidant diamide publication-title: FASEB J. doi: 10.1096/fasebj.12.7.561 – volume: 182 start-page: 663 year: 2008 ident: 10.1016/j.bbagen.2018.09.009_bb0370 article-title: Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins publication-title: J. Cell Biol. doi: 10.1083/jcb.200803022 – volume: 19 start-page: 1707 year: 2005 ident: 10.1016/j.bbagen.2018.09.009_bb0385 article-title: Selectivity of the ubiquitin pathway for oxidatively modified proteins: relevance to protein precipitation diseases publication-title: FASEB J. doi: 10.1096/fj.05-4049fje – volume: 271 start-page: 15504 year: 1996 ident: 10.1016/j.bbagen.2018.09.009_bb0360 article-title: Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.26.15504 – volume: 14 start-page: 417 year: 2017 ident: 10.1016/j.bbagen.2018.09.009_bb0045 article-title: Proteasome inhibitors in cancer therapy publication-title: Nat. Rev. Clin. Oncol. doi: 10.1038/nrclinonc.2016.206 – volume: 264 start-page: 15949 year: 1989 ident: 10.1016/j.bbagen.2018.09.009_bb0230 article-title: Degradation of ornithine decarboxylase in reticulocyte lysate is ATP-dependent but ubiquitin-independent publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)71571-8 – volume: 1843 start-page: 216 year: 2014 ident: 10.1016/j.bbagen.2018.09.009_bb0260 article-title: Ubiquitin-independent proteasomal degradation publication-title: Biochim. Biophys. Acta (BBA) Mol. Cell Res. doi: 10.1016/j.bbamcr.2013.05.008 – volume: 99 start-page: 13125 year: 2002 ident: 10.1016/j.bbagen.2018.09.009_bb0125 article-title: Mdm-2 and ubiquitin-independent p53 proteasomal degradation regulated by NQO1 publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.202480499 – volume: 124 start-page: 381 year: 2006 ident: 10.1016/j.bbagen.2018.09.009_bb0295 article-title: The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGγ proteasome publication-title: Cell doi: 10.1016/j.cell.2005.11.037 – volume: 41 start-page: 8 year: 2011 ident: 10.1016/j.bbagen.2018.09.009_bb0140 article-title: Proteasome activators publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.12.020 – volume: 261 start-page: 2400 year: 1987 ident: 10.1016/j.bbagen.2018.09.009_bb0055 article-title: Ubiquitin-lysozyme conjugates Identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)35950-1 – volume: 17 start-page: 103 year: 2010 ident: 10.1016/j.bbagen.2018.09.009_bb0245 article-title: Ubiquitin-independent p53 proteasomal degradation publication-title: Cell Death Differ. doi: 10.1038/cdd.2009.67 – volume: 16 start-page: 1183 year: 2012 ident: 10.1016/j.bbagen.2018.09.009_bb0185 article-title: Redox control of 20S proteasome gating publication-title: Antioxid. Redox Signal. doi: 10.1089/ars.2011.4210 – volume: 267 start-page: 10515 year: 1992 ident: 10.1016/j.bbagen.2018.09.009_bb0095 article-title: Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain) publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)50047-3 – volume: 24 start-page: 1301 year: 2018 ident: 10.1016/j.bbagen.2018.09.009_bb0175 article-title: Expanded coverage of the 26 proteasome conformational landscape reveals mechanisms of peptidase gating publication-title: Cell Rep. doi: 10.1016/j.celrep.2018.07.004 – volume: 268 start-page: 15405 year: 1993 ident: 10.1016/j.bbagen.2018.09.009_bb0200 article-title: Hydrophobicity as the signal for radical-modified hemoglobin by selective degradation of hydroxyl the multicatalytic proteinase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)82272-4 – volume: 474 start-page: 445 year: 2017 ident: 10.1016/j.bbagen.2018.09.009_bb0380 article-title: The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation publication-title: Biochem. J. doi: 10.1042/BCJ20160582 – volume: 335 start-page: 637 year: 1998 ident: 10.1016/j.bbagen.2018.09.009_bb0305 article-title: Comparative resistance of the 20S and 26S proteasome to oxidative stress publication-title: Biochem. J. doi: 10.1042/bj3350637 – volume: 421 start-page: 397 year: 2009 ident: 10.1016/j.bbagen.2018.09.009_bb0150 article-title: Variably modulated gating of the 26S proteasome by ATP and polyubiquitin publication-title: Biochem. J. doi: 10.1042/BJ20090528 – volume: 24 start-page: 39 year: 2006 ident: 10.1016/j.bbagen.2018.09.009_bb0290 article-title: ATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome publication-title: Mol. Cell doi: 10.1016/j.molcel.2006.08.025 – volume: 386 start-page: 814 year: 2009 ident: 10.1016/j.bbagen.2018.09.009_bb0115 article-title: Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2008.12.081 – volume: 270 start-page: 11623 year: 1995 ident: 10.1016/j.bbagen.2018.09.009_bb0235 article-title: Ubiquitylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.19.11623 – volume: 347 start-page: 439 year: 2015 ident: 10.1016/j.bbagen.2018.09.009_bb0105 article-title: A molecular census of 26S proteasomes in intact neurons publication-title: Science doi: 10.1126/science.1261197 – volume: 169 start-page: 792 year: 2017 ident: 10.1016/j.bbagen.2018.09.009_bb0210 article-title: The logic of the 26S proteasome publication-title: Cell doi: 10.1016/j.cell.2017.04.023 – volume: 27 start-page: 731 year: 2007 ident: 10.1016/j.bbagen.2018.09.009_bb0165 article-title: Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry publication-title: Mol. Cell doi: 10.1016/j.molcel.2007.06.033 – volume: 523 start-page: 181 year: 2012 ident: 10.1016/j.bbagen.2018.09.009_bb0325 article-title: Differential roles of proteasome and immunoproteasome regulators Pa28αβ, Pa28γ and Pa200 in the degradation of oxidized proteins publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2012.04.018 – volume: 270 start-page: 2344 year: 1995 ident: 10.1016/j.bbagen.2018.09.009_bb0355 article-title: Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.5.2344 – volume: 6 start-page: 34432 year: 2016 ident: 10.1016/j.bbagen.2018.09.009_bb0390 article-title: Degradation of redox-sensitive proteins including peroxiredoxins and DJ-1 is promoted by oxidation-induced conformational changes and ubiquitination publication-title: Sci. Rep. doi: 10.1038/srep34432 – volume: 15 start-page: 4829 year: 2004 ident: 10.1016/j.bbagen.2018.09.009_bb0395 article-title: Activation of chaperone-mediated autophagy during oxidative stress publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e04-06-0477 – volume: 19 start-page: 26 year: 2001 ident: 10.1016/j.bbagen.2018.09.009_bb0280 article-title: Intrinsically disordered protein publication-title: J. Mol. Graph. Model doi: 10.1016/S1093-3263(00)00138-8 – volume: 74 start-page: 54 year: 1977 ident: 10.1016/j.bbagen.2018.09.009_bb0005 article-title: A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.74.1.54 – volume: 7 start-page: 521 year: 1989 ident: 10.1016/j.bbagen.2018.09.009_bb0080 article-title: Macroxyproteinase (MOP): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells publication-title: Free Radic. Biol. Med. doi: 10.1016/0891-5849(89)90028-2 – volume: 287 start-page: 10021 year: 2012 ident: 10.1016/j.bbagen.2018.09.009_bb0100 article-title: Nrf2-dependent induction of proteasome and Pa28αβ regulator are required for adaptation to oxidative stress publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.277145 – volume: 404 start-page: 279 year: 2002 ident: 10.1016/j.bbagen.2018.09.009_bb0330 article-title: Increased degradation of oxidized proteins in yeast defective in 26 S proteasome assembly publication-title: Arch. Biochem. Biophys. doi: 10.1016/S0003-9861(02)00336-3 – volume: 111 start-page: 200 year: 1993 ident: 10.1016/j.bbagen.2018.09.009_bb0090 article-title: Molecular characterization of the“ 26S” proteasome complex from rat liver publication-title: J. Struct. Biol. doi: 10.1006/jsbi.1993.1050 – volume: 24 start-page: 419 year: 2017 ident: 10.1016/j.bbagen.2018.09.009_bb0130 article-title: A mammalian nervous-system-specific plasma membrane proteasome complex that modulates neuronal function publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.3389 – volume: 7 start-page: 1062 year: 2000 ident: 10.1016/j.bbagen.2018.09.009_bb0145 article-title: A gated channel into the proteasome core particle publication-title: Nat. Struct. Biol. doi: 10.1038/80992 – ident: 10.1016/j.bbagen.2018.09.009_bb0220 – volume: 78 start-page: 773 year: 1994 ident: 10.1016/j.bbagen.2018.09.009_bb0035 article-title: The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B publication-title: Cell doi: 10.1016/S0092-8674(94)90482-0 – volume: 67 start-page: 304 year: 2014 ident: 10.1016/j.bbagen.2018.09.009_bb0205 article-title: Peptides that activate the 20S proteasome by gate opening increased oxidized protein removal and reduced protein aggregation publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2013.11.017 – volume: 22 start-page: 192 year: 2010 ident: 10.1016/j.bbagen.2018.09.009_bb0345 article-title: Autophagy: links with the proteasome publication-title: Curr. Opin. Cell Biol. doi: 10.1016/j.ceb.2009.11.002 – volume: 419 start-page: 226 year: 2012 ident: 10.1016/j.bbagen.2018.09.009_bb0270 article-title: The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2012.01.152 – volume: 42 start-page: 873 year: 2017 ident: 10.1016/j.bbagen.2018.09.009_bb0020 article-title: The ubiquitin code in the ubiquitin-proteasome system and autophagy publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2017.09.002 – volume: 71 start-page: 169 year: 2018 ident: 10.1016/j.bbagen.2018.09.009_bb0135 article-title: Activity-dependent degradation of the nascentome by the neuronal membrane proteasome publication-title: Mol. Cell doi: 10.1016/j.molcel.2018.06.013 – volume: 3 start-page: ra88 year: 2010 ident: 10.1016/j.bbagen.2018.09.009_bb0310 article-title: Regulation of the 26S proteasome complex during oxidative stress publication-title: Sci. Signal. doi: 10.1126/scisignal.2001232 – volume: 290 start-page: 11467 year: 2015 ident: 10.1016/j.bbagen.2018.09.009_bb0255 article-title: Phosphorylation regulates the ubiquitin-independent degradation of yeast Pah1 phosphatidate phosphatase by the 20S proteasome publication-title: J. Biol. Chem. doi: 10.1074/jbc.M115.648659 – volume: 278 start-page: 311 year: 2003 ident: 10.1016/j.bbagen.2018.09.009_bb0350 article-title: Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome publication-title: J. Biol. Chem. doi: 10.1074/jbc.M206279200 – volume: 275 start-page: 20295 year: 2000 ident: 10.1016/j.bbagen.2018.09.009_bb0240 article-title: Ca2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26 S proteasomes without ubiquitination publication-title: J. Biol. Chem. doi: 10.1074/jbc.M001555200 – volume: 63 start-page: 997 year: 2017 ident: 10.1016/j.bbagen.2018.09.009_bb0375 article-title: The ribosome-bound quality control complex: from aberrant peptide clearance to proteostasis maintenance publication-title: Curr. Genet. doi: 10.1007/s00294-017-0708-5 – volume: 5 start-page: 403 year: 2000 ident: 10.1016/j.bbagen.2018.09.009_bb0120 article-title: Proteasomal turnover of p21Cip1 does not require p21Cip1 ubiquitination publication-title: Mol. Cell doi: 10.1016/S1097-2765(00)80435-9 – volume: 22 start-page: 4356 year: 2003 ident: 10.1016/j.bbagen.2018.09.009_bb0170 article-title: The pore of activated 20S proteasome has an ordered 7-fold symmetric conformation publication-title: EMBO J. doi: 10.1093/emboj/cdg436 – volume: 432 start-page: 217 year: 2010 ident: 10.1016/j.bbagen.2018.09.009_bb0275 article-title: Functional dissection of the N-terminal degron of human thymidylate synthase publication-title: Biochem. J. doi: 10.1042/BJ20101027 – volume: 10 year: 2011 ident: 10.1016/j.bbagen.2018.09.009_bb0180 article-title: Proteasome Activator 200: the Heat is on… publication-title: Mol. Cell. Proteomics – volume: 7 start-page: 1 year: 2014 ident: 10.1016/j.bbagen.2018.09.009_bb0315 article-title: Reversible 26S proteasome disassembly upon mitochondrial stress publication-title: Cell Rep. doi: 10.1016/j.celrep.2014.04.030 – volume: 13 start-page: 1697 year: 2017 ident: 10.1016/j.bbagen.2018.09.009_bb0340 article-title: SQSTM1/p62-mediated autophagy compensates for loss of proteasome polyubiquitin recruiting capacity publication-title: Autophagy doi: 10.1080/15548627.2017.1356549 – volume: 8 start-page: 1832 year: 2014 ident: 10.1016/j.bbagen.2018.09.009_bb0215 article-title: Intrinsically disordered segments affect protein half-life in the cell and during evolution publication-title: Cell Rep. doi: 10.1016/j.celrep.2014.07.055 – volume: 262 start-page: 8220 year: 1987 ident: 10.1016/j.bbagen.2018.09.009_bb0070 article-title: Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)47552-7 – volume: 70 start-page: 1357 year: 2008 ident: 10.1016/j.bbagen.2018.09.009_bb0110 article-title: Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome publication-title: Proteins Struct. Funct. Bioinforma. doi: 10.1002/prot.21614 – volume: 1823 start-page: 67 year: 2012 ident: 10.1016/j.bbagen.2018.09.009_bb0155 article-title: Proteasomal AAA-ATPases: structure and function publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2011.07.009 – volume: 96 start-page: 1580 year: 1983 ident: 10.1016/j.bbagen.2018.09.009_bb0285 article-title: ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin publication-title: J. Cell Biol. doi: 10.1083/jcb.96.6.1580 – volume: 78 start-page: 761 year: 1994 ident: 10.1016/j.bbagen.2018.09.009_bb0030 article-title: Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules publication-title: Cell doi: 10.1016/S0092-8674(94)90462-6 – volume: 262 start-page: 2451 year: 1987 ident: 10.1016/j.bbagen.2018.09.009_bb0060 article-title: Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)61525-X – volume: 98 start-page: 3056 year: 2001 ident: 10.1016/j.bbagen.2018.09.009_bb0335 article-title: RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.071022298 – volume: 331 start-page: 192 year: 1988 ident: 10.1016/j.bbagen.2018.09.009_bb0015 article-title: Identity of the 19S “prosome” particle with the large multifunctional protease complex of mammalian cells (the proteasome) publication-title: Nature doi: 10.1038/331192a0 – volume: 268 start-page: 726 year: 1995 ident: 10.1016/j.bbagen.2018.09.009_bb0040 article-title: Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin publication-title: Science doi: 10.1126/science.7732382 – volume: 40 start-page: 842 year: 1983 ident: 10.1016/j.bbagen.2018.09.009_bb0050 article-title: Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex publication-title: J. Neurochem. doi: 10.1111/j.1471-4159.1983.tb08056.x – volume: 68 start-page: 1015 year: 1999 ident: 10.1016/j.bbagen.2018.09.009_bb0010 article-title: The 26S proteasome: a molecular machine designed for controlled proteolysis publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.68.1.1015 – volume: 26 start-page: 831 year: 2007 ident: 10.1016/j.bbagen.2018.09.009_bb0300 article-title: Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGγ-proteasome pathway publication-title: Mol. Cell doi: 10.1016/j.molcel.2007.05.028 – year: 2018 ident: 10.1016/j.bbagen.2018.09.009_bb0250 article-title: The disordered landscape of the 20S proteasome substrates reveals tight association with phase separated granules publication-title: Proteomics – volume: 99 start-page: 153 year: 2016 ident: 10.1016/j.bbagen.2018.09.009_bb0365 article-title: The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2016.08.002 – volume: 262 start-page: 8227 year: 1987 ident: 10.1016/j.bbagen.2018.09.009_bb0075 article-title: Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)47553-9 – volume: 30 start-page: 191 year: 2009 ident: 10.1016/j.bbagen.2018.09.009_bb0085 article-title: The proteasomal system publication-title: Mol. Aspects Med. doi: 10.1016/j.mam.2009.04.001 – volume: 291 start-page: 14526 year: 2016 ident: 10.1016/j.bbagen.2018.09.009_bb0225 article-title: Conserved sequence preferences contribute to substrate recognition by the proteasome publication-title: J. Biol. Chem. doi: 10.1074/jbc.M116.727578 |
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| SubjectTerms | Adenosine Triphosphate - metabolism Catalysis Hydrophobic and Hydrophilic Interactions oxidation Oxidation-Reduction Proteasomal complexes proteasome endopeptidase complex Proteasome Endopeptidase Complex - physiology protein degradation proteins Proteolysis Ubiquitin - metabolism Ubiquitin- and ATP-independent protein degradation Ubiquitin-proteasome system |
| Title | The physiological role of the free 20S proteasome in protein degradation: A critical review |
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