Base-CP proteasome can serve as a platform for stepwise lid formation

26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S RP is divisible into base and lid sub-complexes. Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rp...

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Published inBioscience reports Vol. 35; no. 3
Main Authors Yu, Zanlin, Livnat-Levanon, Nurit, Kleifeld, Oded, Mansour, Wissam, Nakasone, Mark A, Castaneda, Carlos A, Dixon, Emma K, Fushman, David, Reis, Noa, Pick, Elah, Glickman, Michael H
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Published England Portland Press Ltd 01.06.2015
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Abstract 26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S RP is divisible into base and lid sub-complexes. Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rpn8, Rpn9 and Rpn11), which interacts with both CP and base sub-complexes and module 2 (Rpn3, Rpn7, Rpn12 and Rpn15) that is attached mainly to module 1. We now show that suppression of RPN11 expression halted lid assembly yet enabled the base and 20S CP to pre-assemble and form a base-CP. A key role for Regulatory particle non-ATPase 11 (Rpn11) in bridging lid module 1 and module 2 subunits together is inferred from observing defective proteasomes in rpn11-m1, a mutant expressing a truncated form of Rpn11 and displaying mitochondrial phenotypes. An incomplete lid made up of five module 1 subunits attached to base-CP was identified in proteasomes isolated from this mutant. Re-introducing the C-terminal portion of Rpn11 enabled recruitment of missing module 2 subunits. In vitro, module 1 was reconstituted stepwise, initiated by Rpn11-Rpn8 heterodimerization. Upon recruitment of Rpn6, the module 1 intermediate was competent to lock into base-CP and reconstitute an incomplete 26S proteasome. Thus, base-CP can serve as a platform for gradual incorporation of lid, along a proteasome assembly pathway. Identification of proteasome intermediates and reconstitution of minimal functional units should clarify aspects of the inner workings of this machine and how multiple catalytic processes are synchronized within the 26S proteasome holoenzymes.
AbstractList 26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S RP is divisible into base and lid sub-complexes. Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rpn8, Rpn9 and Rpn11), which interacts with both CP and base sub-complexes and module 2 (Rpn3, Rpn7, Rpn12 and Rpn15) that is attached mainly to module 1. We now show that suppression of RPN11 expression halted lid assembly yet enabled the base and 20S CP to pre-assemble and form a base-CP. A key role for Regulatory particle non-ATPase 11 (Rpn11) in bridging lid module 1 and module 2 subunits together is inferred from observing defective proteasomes in rpn11-m1, a mutant expressing a truncated form of Rpn11 and displaying mitochondrial phenotypes. An incomplete lid made up of five module 1 subunits attached to base-CP was identified in proteasomes isolated from this mutant. Re-introducing the C-terminal portion of Rpn11 enabled recruitment of missing module 2 subunits. In vitro, module 1 was reconstituted stepwise, initiated by Rpn11-Rpn8 heterodimerization. Upon recruitment of Rpn6, the module 1 intermediate was competent to lock into base-CP and reconstitute an incomplete 26S proteasome. Thus, base-CP can serve as a platform for gradual incorporation of lid, along a proteasome assembly pathway. Identification of proteasome intermediates and reconstitution of minimal functional units should clarify aspects of the inner workings of this machine and how multiple catalytic processes are synchronized within the 26S proteasome holoenzymes.
26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S RP is divisible into base and lid sub-complexes. Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rpn8, Rpn9 and Rpn11), which interacts with both CP and base sub-complexes and module 2 (Rpn3, Rpn7, Rpn12 and Rpn15) that is attached mainly to module 1. We now show that suppression of RPN11 expression halted lid assembly yet enabled the base and 20S CP to pre-assemble and form a base-CP. A key role for Regulatory particle non-ATPase 11 (Rpn11) in bridging lid module 1 and module 2 subunits together is inferred from observing defective proteasomes in rpn11–m1 , a mutant expressing a truncated form of Rpn11 and displaying mitochondrial phenotypes. An incomplete lid made up of five module 1 subunits attached to base-CP was identified in proteasomes isolated from this mutant. Re-introducing the C-terminal portion of Rpn11 enabled recruitment of missing module 2 subunits. In vitro , module 1 was reconstituted stepwise, initiated by Rpn11–Rpn8 heterodimerization. Upon recruitment of Rpn6, the module 1 intermediate was competent to lock into base-CP and reconstitute an incomplete 26S proteasome. Thus, base-CP can serve as a platform for gradual incorporation of lid, along a proteasome assembly pathway. Identification of proteasome intermediates and reconstitution of minimal functional units should clarify aspects of the inner workings of this machine and how multiple catalytic processes are synchronized within the 26S proteasome holoenzymes. Defective proteasome 19S regulatory particles (RPs) were identified in rpn11f–m1 , a proteasomal mutant with mitochondrial phenotypes. The Rpn11 subunit initiates assembly of a five-subunit lid module competent to integrate into pre-assembled base-20S core particle (CP), with subsequent recruitment of remaining lid subunits.
Author Fushman, David
Mansour, Wissam
Nakasone, Mark A
Yu, Zanlin
Livnat-Levanon, Nurit
Kleifeld, Oded
Reis, Noa
Dixon, Emma K
Glickman, Michael H
Castaneda, Carlos A
Pick, Elah
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  surname: Glickman
  fullname: Glickman, Michael H
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Cites_doi 10.1016/j.cell.2009.04.061
10.1038/nature08065
10.1371/journal.pone.0105688
10.1016/j.molcel.2006.08.025
10.1038/nsmb.2659
10.1126/science.1075898
10.1007/s00294-010-0321-3
10.1016/j.bbrc.2010.05.061
10.1038/nature11468
10.1016/j.sbi.2014.02.002
10.1016/j.molcel.2012.03.026
10.1016/j.jmb.2011.05.005
10.1016/j.molcel.2013.12.009
10.1091/mbc.E06-07-0635
10.1016/j.molcel.2010.02.035
10.1016/j.str.2013.04.029
10.1128/MCB.18.6.3149
10.1016/j.celrep.2014.04.030
10.1073/pnas.1400546111
10.1042/BST0380029
10.1074/mcp.R110.003871
10.1074/jbc.M403165200
10.1042/BST0360807
10.1074/jbc.M109.076786
10.1016/j.bbamcr.2013.08.012
10.1186/1471-2091-3-28
10.1371/journal.pbio.0040267
10.1091/mbc.E07-07-0717
10.1016/j.febslet.2005.04.048
10.2174/1389203043379756
10.1073/pnas.1209345110
10.1038/nature01071
10.1016/j.jmb.2009.09.038
10.1042/BST0370937
10.1038/nsmb.1427
10.1016/S0378-1119(01)00799-5
10.1016/j.tcb.2010.03.007
10.1016/j.sbi.2007.12.014
10.1038/nrm2630
10.1016/j.cell.2005.03.028
10.1016/S0014-5793(97)00851-X
10.1038/nature13566
10.1515/hsz-2011-0285
10.1074/jbc.M111.316323
10.1093/emboj/20.24.7096
10.1091/mbc.9.10.2917
10.1042/BJ20040008
10.1038/nsmb.2616
10.1016/j.molcel.2011.11.020
10.1074/jbc.M113.482570
10.1038/nrm3741
10.1146/annurev.biochem.78.081507.101607
10.1016/j.molcel.2010.11.002
10.1016/j.str.2013.06.023
10.1074/jbc.M409364200
10.1016/j.bbrc.2013.04.069
10.1128/MCB.19.10.6575
10.1128/MCB.01227-08
10.1073/pnas.1120559109
10.1371/journal.pbio.0020002
10.1016/j.molcel.2008.10.011
10.1091/mbc.E10-08-0655
10.1128/MCB.19.10.6872
10.1016/S0968-0004(98)01217-1
10.1073/pnas.1403409111
10.1016/S0960-9822(03)00417-2
10.1105/tpc.111.086702
10.1016/j.str.2013.02.019
10.1093/emboj/17.17.4909
10.1038/nsmb.2771
10.1038/nature11848
10.1371/journal.pbio.0020013
10.1038/nature10774
10.1152/physrev.00027.2001
10.1016/j.yexcr.2009.08.018
10.1016/j.jmb.2007.04.084
10.1074/jbc.M314231200
10.1021/ja207220g
10.1074/jbc.M109.023218
10.1016/S0092-8674(00)81603-7
10.1242/jcs.01575
10.1093/embo-reports/kve184
10.1016/0378-1119(95)00212-O
10.1002/pmic.200700588
10.1038/nature11315
10.1016/j.molcel.2009.07.009
10.1073/pnas.1117648108
10.1038/msb4100024
10.1016/S0076-6879(05)99001-0
10.1016/j.cell.2004.06.013
10.1074/jbc.M307050200
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Issue 3
Keywords 26S proteasome
19S regulatory particle
lid
PCI
MPN
20S core particle
base
rpn11-m1
Language English
License 2015 The Author(s).
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References 9763452 - Mol Biol Cell. 1998 Oct;9(10):2917-31
18511945 - Nat Struct Mol Biol. 2008 Jun;15(6):573-80
10490597 - Mol Cell Biol. 1999 Oct;19(10):6575-84
15890341 - FEBS Lett. 2005 Jun 13;579(15):3214-23
16729052 - Mol Syst Biol. 2005;1:2005.0017
24013205 - Nat Struct Mol Biol. 2013 Oct;20(10):1164-72
21095592 - Mol Cell. 2010 Nov 24;40(4):671-81
22195964 - Mol Cell. 2011 Dec 23;44(6):907-17
14737182 - PLoS Biol. 2004 Jan;2(1):E2
12183636 - Science. 2002 Oct 18;298(5593):611-5
21962295 - J Am Chem Soc. 2011 Nov 9;133(44):17855-68
19075009 - Mol Cell Biol. 2009 Feb;29(4):1095-106
20823120 - Mol Cell Proteomics. 2011 May;10(5):R110.003871
19489727 - Annu Rev Biochem. 2009;78:477-513
15907469 - Cell. 2005 May 20;121(4):553-65
23911091 - Structure. 2013 Sep 3;21(9):1624-35
19412160 - Nature. 2009 Jun 11;459(7248):866-70
22187461 - Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):149-54
18172023 - Mol Biol Cell. 2008 Mar;19(3):1022-31
18186020 - Proteomics. 2008 Feb;8(3):508-20
25144743 - PLoS One. 2014;9(8):e105688
18276129 - Curr Opin Struct Biol. 2008 Feb;18(1):43-51
19589775 - J Biol Chem. 2009 Sep 11;284(37):24891-903
24463465 - Nat Struct Mol Biol. 2014 Mar;21(3):220-7
16338345 - Methods Enzymol. 2005;399:3-20
17559875 - J Mol Biol. 2007 Jul 27;370(5):846-55
22972301 - Nature. 2012 Sep 13;489(7415):304-8
9276459 - FEBS Lett. 1997 Aug 4;412(3):521-5
19732767 - Exp Cell Res. 2010 Jan 15;316(2):258-71
19683491 - Mol Cell. 2009 Aug 14;35(3):260-4
21619884 - J Mol Biol. 2011 Jul 15;410(3):383-99
7628709 - Gene. 1995 Jul 4;160(1):135-6
21289098 - Mol Biol Cell. 2011 Apr;22(7):911-20
15102831 - J Biol Chem. 2004 Jun 25;279(26):27168-76
15242642 - Cell. 2004 Jul 9;118(1):31-44
24516147 - Proc Natl Acad Sci U S A. 2014 Feb 25;111(8):2984-9
11943459 - Gene. 2002 Mar 6;286(1):43-51
12842014 - Curr Biol. 2003 Jul 1;13(13):1140-4
19754430 - Biochem Soc Trans. 2009 Oct;37(Pt 5):937-53
17135287 - Mol Biol Cell. 2007 Feb;18(2):569-80
18995839 - Mol Cell. 2008 Nov 7;32(3):415-25
20427185 - Trends Cell Biol. 2010 Jul;20(7):391-401
25389291 - J Biol Chem. 2015 Feb 20;290(8):4688-704
19446322 - Cell. 2009 May 29;137(5):887-99
23770819 - Nat Struct Mol Biol. 2013 Jul;20(7):781-8
21764993 - Plant Cell. 2011 Jul;23(7):2754-73
20074030 - Biochem Soc Trans. 2010 Feb;38(Pt 1):29-33
19165213 - Nat Rev Mol Cell Biol. 2009 Feb;10(2):104-15
23994620 - Biochim Biophys Acta. 2014 Jan;1843(1):13-25
11742986 - EMBO J. 2001 Dec 17;20(24):7096-107
22318722 - J Biol Chem. 2012 Apr 27;287(18):14659-71
20471955 - Biochem Biophys Res Commun. 2010 Jun 11;396(4):1048-53
24412063 - Mol Cell. 2014 Feb 6;53(3):433-43
23643786 - Biochem Biophys Res Commun. 2013 May 31;435(2):250-4
10490625 - Mol Cell Biol. 1999 Oct;19(10):6872-90
15018611 - Biochem J. 2004 Jul 1;381(Pt 1):275-85
17018291 - Mol Cell. 2006 Oct 6;24(1):39-50
22307589 - Proc Natl Acad Sci U S A. 2012 Jan 31;109(5):1380-7
16869714 - PLoS Biol. 2006 Aug;4(8):e267
25043011 - Nature. 2014 Aug 14;512(7513):161-5
14737189 - PLoS Biol. 2004 Jan;2(1):E13
19781552 - J Mol Biol. 2009 Nov 27;394(2):320-8
18429166 - Curr Protoc Protein Sci. 2001 Aug;Chapter 21:Unit 21.5
9584156 - Mol Cell Biol. 1998 Jun;18(6):3149-62
24857655 - Cell Rep. 2014 Jun 12;7(5):1371-80
15572408 - J Cell Sci. 2004 Dec 15;117(Pt 26):6447-54
22922647 - Nature. 2012 Sep 13;489(7415):263-8
20471945 - Mol Cell. 2010 May 14;38(3):393-403
9724628 - EMBO J. 1998 Sep 1;17(17):4909-19
9741626 - Cell. 1998 Sep 4;94(5):615-23
24452470 - Nat Rev Mol Cell Biol. 2014 Feb;15(2):122-33
22500737 - Mol Cell. 2012 Apr 13;46(1):54-66
22237024 - Nature. 2012 Feb 9;482(7384):186-91
23965995 - J Biol Chem. 2013 Oct 4;288(40):29215-22
12353037 - Nature. 2002 Sep 26;419(6905):403-7
20941496 - Curr Genet. 2010 Dec;56(6):543-57
15917626 - Methods Mol Biol. 2005;301:57-70
24706844 - Proc Natl Acad Sci U S A. 2014 Apr 15;111(15):5544-9
23823328 - Structure. 2013 Jul 2;21(7):1168-81
18793141 - Biochem Soc Trans. 2008 Oct;36(Pt 5):807-12
15188770 - Curr Protein Pept Sci. 2004 Jun;5(3):201-11
24632559 - Curr Opin Struct Biol. 2014 Feb;24:156-64
23288897 - Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1273-8
23562397 - Structure. 2013 May 7;21(5):727-40
23029643 - Biol Chem. 2012 Apr;393(4):217-34
14581483 - J Biol Chem. 2004 Jan 16;279(3):1729-38
9644972 - Trends Biochem Sci. 1998 Jun;23(6):204-5
15117943 - J Biol Chem. 2004 Jul 2;279(27):28807-16
11917093 - Physiol Rev. 2002 Apr;82(2):373-428
23407496 - Nature. 2013 Mar 7;495(7439):126-7
12370088 - BMC Biochem. 2002;3:28
20061387 - J Biol Chem. 2010 Mar 12;285(11):8330-9
15611133 - J Biol Chem. 2005 Feb 25;280(8):6537-47
11559592 - EMBO Rep. 2001 Sep;2(9):821-8
Inobe (2021111618442570500_B12) 2014; 24
Bailly (2021111618442570500_B65) 1999; 19
Bajorek (2021111618442570500_B53) 2003; 13
Sawada (2021111618442570500_B54) 1997; 412
Matiuhin (2021111618442570500_B57) 2008; 32
Isono (2021111618442570500_B66) 2005; 280
Rubin (2021111618442570500_B83) 1998; 17
Rosenzweig (2021111618442570500_B19) 2012; 287
Chandra (2021111618442570500_B79) 2010; 56
Castaneda (2021111618442570500_B76) 2013; 21
Pick (2021111618442570500_B36) 2009; 35
Matyskiela (2021111618442570500_B26) 2013; 20
Guterman (2021111618442570500_B14) 2004; 5
Pathare (2021111618442570500_B24) 2014; 111
Glickman (2021111618442570500_B80) 2005; 579
Ambroggio (2021111618442570500_B22) 2004; 2
Hofmann (2021111618442570500_B37) 1998; 23
Funakoshi (2021111618442570500_B48) 2009; 137
Beckwith (2021111618442570500_B56) 2013; 20
Fukunaga (2021111618442570500_B39) 2010; 396
Echalier (2021111618442570500_B87) 2013; 110
Murata (2021111618442570500_B47) 2009; 10
Maytal-Kivity (2021111618442570500_B20) 2002; 3
Mnaimneh (2021111618442570500_B77) 2004; 118
Vilchez (2021111618442570500_B94) 2012; 489
Lingaraju (2021111618442570500_B85) 2014; 512
Lasker (2021111618442570500_B18) 2012; 109
Birol (2021111618442570500_B86) 2014; 9
Babbitt (2021111618442570500_B91) 2005; 121
Byrne (2021111618442570500_B89) 2010; 316
Davy (2021111618442570500_B33) 2001; 2
Tomko (2021111618442570500_B50) 2010; 38
Joshi (2021111618442570500_B82) 2011; 410
Rosenzweig (2021111618442570500_B71) 2008; 15
Keller (2021111618442570500_B72) 2005; 1
Komander (2021111618442570500_B2) 2009; 37
Chandra (2021111618442570500_B78) 2010; 285
Peth (2021111618442570500_B9) 2013; 288
Finley (2021111618442570500_B3) 2009; 78
Tomko (2021111618442570500_B38) 2014; 53
Nakasone (2021111618442570500_B74) 2013; 21
Inobe (2021111618442570500_B7) 2008; 18
Rinaldi (2021111618442570500_B42) 2004; 381
Rinaldi (2021111618442570500_B63) 1998; 9
Rinaldi (2021111618442570500_B43) 2008; 19
Glickman (2021111618442570500_B5) 1998; 18
Glickman (2021111618442570500_B11) 2004; 2
Lin (2021111618442570500_B84) 2011; 23
Peth (2021111618442570500_B8) 2010; 40
Rinaldi (2021111618442570500_B62) 1995; 160
Schwanhausser (2021111618442570500_B1) 2013; 495
Schmidt (2021111618442570500_B81) 2014; 1843
Fu (2021111618442570500_B31) 2001; 20
Volk (2021111618442570500_B75) 2005; 399
Chen (2021111618442570500_B41) 2008; 8
Verma (2021111618442570500_B28) 2002; 298
Thompson (2021111618442570500_B92) 2009; 284
Yu (2021111618442570500_B35) 2011; 22
Funakoshi (2021111618442570500_B58) 2004; 117
Vilchez (2021111618442570500_B93) 2012; 489
Matias (2021111618442570500_B45) 2010; 38
Worden (2021111618442570500_B21) 2014; 21
da Fonseca (2021111618442570500_B30) 2012; 46
Pathare (2021111618442570500_B88) 2012; 109
Bhattacharyya (2021111618442570500_B25) 2014; 15
Unverdorben (2021111618442570500_B27) 2014; 111
Sone (2021111618442570500_B59) 2004; 279
Leggett (2021111618442570500_B69) 2005; 301
Bohn (2021111618442570500_B40) 2013; 435
Estrin (2021111618442570500_B61) 2013; 21
Yao (2021111618442570500_B29) 2002; 419
Sharon (2021111618442570500_B32) 2006; 4
Tomko (2021111618442570500_B60) 2011; 44
Glickman (2021111618442570500_B4) 2002; 82
Guterman (2021111618442570500_B10) 2004; 279
Sanches (2021111618442570500_B23) 2007; 370
Rosenzweig (2021111618442570500_B46) 2008; 36
Glickman (2021111618442570500_B70) 2001; Chapter 21
Glickman (2021111618442570500_B16) 1998; 94
Lee (2021111618442570500_B15) 2011; 10
Tanaka (2021111618442570500_B6) 2012; 393
Rinaldi (2021111618442570500_B64) 2002; 286
Liu (2021111618442570500_B52) 2006; 24
Tonoki (2021111618442570500_B90) 2009; 29
Bedford (2021111618442570500_B44) 2010; 20
Castaneda (2021111618442570500_B73) 2011; 133
Park (2021111618442570500_B49) 2009; 459
Isono (2021111618442570500_B34) 2007; 18
Isono (2021111618442570500_B67) 2004; 279
Lander (2021111618442570500_B17) 2012; 482
Takeuchi (2021111618442570500_B68) 1999; 19
Mansour (2021111618442570500_B13) 2014
Livnat-Levanon (2021111618442570500_B55) 2014; 7
Hendil (2021111618442570500_B51) 2009; 394
References_xml – volume: 137
  start-page: 887
  year: 2009
  ident: 2021111618442570500_B48
  article-title: Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base
  publication-title: Cell
  doi: 10.1016/j.cell.2009.04.061
  contributor:
    fullname: Funakoshi
– volume: 459
  start-page: 866
  year: 2009
  ident: 2021111618442570500_B49
  article-title: Hexameric assembly of the proteasomal ATPases is templated through their C termini
  publication-title: Nature
  doi: 10.1038/nature08065
  contributor:
    fullname: Park
– volume: 9
  start-page: e105688
  year: 2014
  ident: 2021111618442570500_B86
  article-title: Structural and biochemical characterization of the cop9 signalosome CSN5/CSN6 heterodimer
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0105688
  contributor:
    fullname: Birol
– volume: 24
  start-page: 39
  year: 2006
  ident: 2021111618442570500_B52
  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
  contributor:
    fullname: Liu
– volume: 20
  start-page: 1164
  year: 2013
  ident: 2021111618442570500_B56
  article-title: Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+unfoldase
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2659
  contributor:
    fullname: Beckwith
– volume: 298
  start-page: 611
  year: 2002
  ident: 2021111618442570500_B28
  article-title: Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
  publication-title: Science
  doi: 10.1126/science.1075898
  contributor:
    fullname: Verma
– volume: 56
  start-page: 543
  year: 2010
  ident: 2021111618442570500_B79
  article-title: Synthetic lethality of rpn11–1 rpn10Delta is linked to altered proteasome assembly and activity
  publication-title: Curr. Genet.
  doi: 10.1007/s00294-010-0321-3
  contributor:
    fullname: Chandra
– volume: 396
  start-page: 1048
  year: 2010
  ident: 2021111618442570500_B39
  article-title: Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2010.05.061
  contributor:
    fullname: Fukunaga
– volume: 489
  start-page: 304
  year: 2012
  ident: 2021111618442570500_B93
  article-title: Increased proteasome activity in human embryonic stem cells is regulated by PSMD11
  publication-title: Nature
  doi: 10.1038/nature11468
  contributor:
    fullname: Vilchez
– volume: 24
  start-page: 156
  year: 2014
  ident: 2021111618442570500_B12
  article-title: Paradigms of protein degradation by the proteasome
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2014.02.002
  contributor:
    fullname: Inobe
– volume: 46
  start-page: 54
  year: 2012
  ident: 2021111618442570500_B30
  article-title: Molecular model of the human 26S proteasome
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2012.03.026
  contributor:
    fullname: da Fonseca
– volume: 410
  start-page: 383
  year: 2011
  ident: 2021111618442570500_B82
  article-title: A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2011.05.005
  contributor:
    fullname: Joshi
– volume: 53
  start-page: 433
  year: 2014
  ident: 2021111618442570500_B38
  article-title: The intrinsically disordered Sem1 protein functions as a molecular tether during proteasome lid biogenesis
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2013.12.009
  contributor:
    fullname: Tomko
– volume: 18
  start-page: 569
  year: 2007
  ident: 2021111618442570500_B34
  article-title: The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.E06-07-0635
  contributor:
    fullname: Isono
– volume: 38
  start-page: 393
  year: 2010
  ident: 2021111618442570500_B50
  article-title: Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2010.02.035
  contributor:
    fullname: Tomko
– volume: 21
  start-page: 1168
  year: 2013
  ident: 2021111618442570500_B76
  article-title: Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains
  publication-title: Structure
  doi: 10.1016/j.str.2013.04.029
  contributor:
    fullname: Castaneda
– volume: 18
  start-page: 3149
  year: 1998
  ident: 2021111618442570500_B5
  article-title: The regulatory particle of the Saccharomyces cerevisiae proteasome
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.18.6.3149
  contributor:
    fullname: Glickman
– volume: 7
  start-page: 1371
  year: 2014
  ident: 2021111618442570500_B55
  article-title: Reversible 26S proteasome disassembly upon mitochondrial stress
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2014.04.030
  contributor:
    fullname: Livnat-Levanon
– volume: 111
  start-page: 2984
  year: 2014
  ident: 2021111618442570500_B24
  article-title: Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.1400546111
  contributor:
    fullname: Pathare
– volume: 38
  start-page: 29
  year: 2010
  ident: 2021111618442570500_B45
  article-title: Chaperone-assisted assembly of the proteasome core particle
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0380029
  contributor:
    fullname: Matias
– volume: 10
  start-page: R110.003871
  year: 2011
  ident: 2021111618442570500_B15
  article-title: Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
  publication-title: Mol. Cell. Proteomics
  doi: 10.1074/mcp.R110.003871
  contributor:
    fullname: Lee
– volume: 279
  start-page: 28807
  year: 2004
  ident: 2021111618442570500_B59
  article-title: Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M403165200
  contributor:
    fullname: Sone
– volume: 36
  start-page: 807
  year: 2008
  ident: 2021111618442570500_B46
  article-title: Chaperone-driven proteasome assembly
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0360807
  contributor:
    fullname: Rosenzweig
– volume: 285
  start-page: 8330
  year: 2010
  ident: 2021111618442570500_B78
  article-title: Proteasome assembly influences interaction with ubiquitinated proteins and shuttle factors
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M109.076786
  contributor:
    fullname: Chandra
– volume: 1843
  start-page: 13
  year: 2014
  ident: 2021111618442570500_B81
  article-title: Regulation of proteasome activity in health and disease
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbamcr.2013.08.012
  contributor:
    fullname: Schmidt
– volume: 3
  start-page: 28
  year: 2002
  ident: 2021111618442570500_B20
  article-title: MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
  publication-title: BMC Biochem.
  doi: 10.1186/1471-2091-3-28
  contributor:
    fullname: Maytal-Kivity
– volume: 4
  start-page: e267
  year: 2006
  ident: 2021111618442570500_B32
  article-title: Structural organization of the 19S proteasome lid: insights from MS of intact complexes
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.0040267
  contributor:
    fullname: Sharon
– volume: 19
  start-page: 1022
  year: 2008
  ident: 2021111618442570500_B43
  article-title: Dissection of the carboxyl-terminal domain of the proteasomal subunit Rpn11 in maintenance of mitochondrial structure and function
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.E07-07-0717
  contributor:
    fullname: Rinaldi
– volume: 579
  start-page: 3214
  year: 2005
  ident: 2021111618442570500_B80
  article-title: Proteasome plasticity
  publication-title: FEBS Lett.
  doi: 10.1016/j.febslet.2005.04.048
  contributor:
    fullname: Glickman
– volume: 5
  start-page: 201
  year: 2004
  ident: 2021111618442570500_B14
  article-title: Deubiquitinating enzymes are IN/(trinsic to proteasome function)
  publication-title: Curr. Protein Pept. Sci.
  doi: 10.2174/1389203043379756
  contributor:
    fullname: Guterman
– volume: 110
  start-page: 1273
  year: 2013
  ident: 2021111618442570500_B87
  article-title: Insights into the regulation of the human COP9 signalosome catalytic subunit, CSN5/Jab1
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.1209345110
  contributor:
    fullname: Echalier
– volume: 419
  start-page: 403
  year: 2002
  ident: 2021111618442570500_B29
  article-title: A cryptic protease couples deubiquitination and degradation by the proteasome
  publication-title: Nature
  doi: 10.1038/nature01071
  contributor:
    fullname: Yao
– volume: 394
  start-page: 320
  year: 2009
  ident: 2021111618442570500_B51
  article-title: The 20S proteasome as an assembly platform for the 19S regulatory complex
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.09.038
  contributor:
    fullname: Hendil
– volume: 37
  start-page: 937
  year: 2009
  ident: 2021111618442570500_B2
  article-title: The emerging complexity of protein ubiquitination
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0370937
  contributor:
    fullname: Komander
– volume: 15
  start-page: 573
  year: 2008
  ident: 2021111618442570500_B71
  article-title: The central unit within the 19S regulatory particle of the proteasome
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1427
  contributor:
    fullname: Rosenzweig
– volume: 286
  start-page: 43
  year: 2002
  ident: 2021111618442570500_B64
  article-title: Mitochondrial effects of the pleiotropic proteasomal mutation mpr1/rpn11: uncoupling from cell cycle defects in extragenic revertants
  publication-title: Gene
  doi: 10.1016/S0378-1119(01)00799-5
  contributor:
    fullname: Rinaldi
– volume: Chapter 21
  start-page: Unit 21.5
  year: 2001
  ident: 2021111618442570500_B70
  article-title: Purification and characterization of proteasomes from Saccharomyces cerevisiae
  publication-title: Curr. Protoc. Protein Sci.
  contributor:
    fullname: Glickman
– volume: 20
  start-page: 391
  year: 2010
  ident: 2021111618442570500_B44
  article-title: Assembly, structure, and function of the 26S proteasome
  publication-title: Trends Cell Biol.
  doi: 10.1016/j.tcb.2010.03.007
  contributor:
    fullname: Bedford
– volume: 18
  start-page: 43
  year: 2008
  ident: 2021111618442570500_B7
  article-title: Protein targeting to ATP-dependent proteases
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2007.12.014
  contributor:
    fullname: Inobe
– volume: 10
  start-page: 104
  year: 2009
  ident: 2021111618442570500_B47
  article-title: Molecular mechanisms of proteasome assembly
  publication-title: Nat. Rev. Mol. Cell. Biol.
  doi: 10.1038/nrm2630
  contributor:
    fullname: Murata
– volume: 121
  start-page: 553
  year: 2005
  ident: 2021111618442570500_B91
  article-title: ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle
  publication-title: Cell
  doi: 10.1016/j.cell.2005.03.028
  contributor:
    fullname: Babbitt
– volume: 412
  start-page: 521
  year: 1997
  ident: 2021111618442570500_B54
  article-title: Difference between PA700-like proteasome activator complex and the regulatory complex dissociated from the 26S proteasome implies the involvement of modulating factors in the 26S proteasome assembly
  publication-title: FEBS Lett.
  doi: 10.1016/S0014-5793(97)00851-X
  contributor:
    fullname: Sawada
– volume: 512
  start-page: 161
  year: 2014
  ident: 2021111618442570500_B85
  article-title: Crystal structure of the human COP9 signalosome
  publication-title: Nature
  doi: 10.1038/nature13566
  contributor:
    fullname: Lingaraju
– volume: 393
  start-page: 217
  year: 2012
  ident: 2021111618442570500_B6
  article-title: The proteasome: molecular machinery and pathophysiological roles
  publication-title: Biol. Chem.
  doi: 10.1515/hsz-2011-0285
  contributor:
    fullname: Tanaka
– volume: 287
  start-page: 14659
  year: 2012
  ident: 2021111618442570500_B19
  article-title: Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.316323
  contributor:
    fullname: Rosenzweig
– volume: 20
  start-page: 7096
  year: 2001
  ident: 2021111618442570500_B31
  article-title: Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
  publication-title: EMBO J.
  doi: 10.1093/emboj/20.24.7096
  contributor:
    fullname: Fu
– volume: 9
  start-page: 2917
  year: 1998
  ident: 2021111618442570500_B63
  article-title: A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.9.10.2917
  contributor:
    fullname: Rinaldi
– volume: 381
  start-page: 275
  year: 2004
  ident: 2021111618442570500_B42
  article-title: Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain
  publication-title: Biochem. J.
  doi: 10.1042/BJ20040008
  contributor:
    fullname: Rinaldi
– volume: 20
  start-page: 781
  year: 2013
  ident: 2021111618442570500_B26
  article-title: Conformational switching of the 26S proteasome enables substrate degradation
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2616
  contributor:
    fullname: Matyskiela
– volume: 44
  start-page: 907
  year: 2011
  ident: 2021111618442570500_B60
  article-title: Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2011.11.020
  contributor:
    fullname: Tomko
– volume: 288
  start-page: 29215
  year: 2013
  ident: 2021111618442570500_B9
  article-title: The ATP costs and time required to degrade ubiquitinated proteins by the 26 S proteasome
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.482570
  contributor:
    fullname: Peth
– volume: 15
  start-page: 122
  year: 2014
  ident: 2021111618442570500_B25
  article-title: Regulated protein turnover: snapshots of the proteasome in action
  publication-title: Nat. Rev. Mol. Cell. Biol.
  doi: 10.1038/nrm3741
  contributor:
    fullname: Bhattacharyya
– volume: 78
  start-page: 477
  year: 2009
  ident: 2021111618442570500_B3
  article-title: Recognition and processing of ubiquitin-protein conjugates by the proteasome
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.78.081507.101607
  contributor:
    fullname: Finley
– year: 2014
  ident: 2021111618442570500_B13
  article-title: Disassembly of Lys11- and mixed-linkage polyubiquitin conjugates provide insights into function of proteasomal deubiquitinases Rpn11 and Ubp6
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Mansour
– volume: 40
  start-page: 671
  year: 2010
  ident: 2021111618442570500_B8
  article-title: ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2010.11.002
  contributor:
    fullname: Peth
– volume: 21
  start-page: 1624
  year: 2013
  ident: 2021111618442570500_B61
  article-title: Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid
  publication-title: Structure
  doi: 10.1016/j.str.2013.06.023
  contributor:
    fullname: Estrin
– volume: 280
  start-page: 6537
  year: 2005
  ident: 2021111618442570500_B66
  article-title: Functional analysis of Rpn6p, a lid component of the 26 S proteasome, using temperature-sensitive rpn6 mutants of the yeast Saccharomyces cerevisiae
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M409364200
  contributor:
    fullname: Isono
– volume: 435
  start-page: 250
  year: 2013
  ident: 2021111618442570500_B40
  article-title: Localization of the regulatory particle subunit Sem1 in the 26S proteasome
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2013.04.069
  contributor:
    fullname: Bohn
– volume: 19
  start-page: 6575
  year: 1999
  ident: 2021111618442570500_B68
  article-title: Rpn9 is required for efficient assembly of the yeast 26S proteasome
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.19.10.6575
  contributor:
    fullname: Takeuchi
– volume: 29
  start-page: 1095
  year: 2009
  ident: 2021111618442570500_B90
  article-title: Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.01227-08
  contributor:
    fullname: Tonoki
– volume: 109
  start-page: 1380
  year: 2012
  ident: 2021111618442570500_B18
  article-title: Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.1120559109
  contributor:
    fullname: Lasker
– volume: 2
  start-page: E2
  year: 2004
  ident: 2021111618442570500_B22
  article-title: JAMM: a metalloprotease-like zinc site in the proteasome and signalosome
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.0020002
  contributor:
    fullname: Ambroggio
– volume: 32
  start-page: 415
  year: 2008
  ident: 2021111618442570500_B57
  article-title: Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2008.10.011
  contributor:
    fullname: Matiuhin
– volume: 22
  start-page: 911
  year: 2011
  ident: 2021111618442570500_B35
  article-title: Dual function of Rpn5 in two PCI complexes, the 26S proteasome and COP9 signalosome
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.E10-08-0655
  contributor:
    fullname: Yu
– volume: 19
  start-page: 6872
  year: 1999
  ident: 2021111618442570500_B65
  article-title: Functional characterization of rpn3 uncovers a distinct 19S proteasomal subunit requirement for ubiquitin-dependent proteolysis of cell cycle regulatory proteins in budding yeast
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.19.10.6872
  contributor:
    fullname: Bailly
– volume: 23
  start-page: 204
  year: 1998
  ident: 2021111618442570500_B37
  article-title: The PCI domain: a common theme in three multi-protein complexes
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/S0968-0004(98)01217-1
  contributor:
    fullname: Hofmann
– volume: 111
  start-page: 5544
  year: 2014
  ident: 2021111618442570500_B27
  article-title: Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.1403409111
  contributor:
    fullname: Unverdorben
– volume: 13
  start-page: 1140
  year: 2003
  ident: 2021111618442570500_B53
  article-title: Proteasome disassembly and downregulation is correlated with viability during stationary phase
  publication-title: Curr. Biol.
  doi: 10.1016/S0960-9822(03)00417-2
  contributor:
    fullname: Bajorek
– volume: 23
  start-page: 2754
  year: 2011
  ident: 2021111618442570500_B84
  article-title: The defective proteasome but not substrate recognition function is responsible for the null phenotypes of the Arabidopsis proteasome subunit RPN10
  publication-title: Plant Cell.
  doi: 10.1105/tpc.111.086702
  contributor:
    fullname: Lin
– volume: 21
  start-page: 727
  year: 2013
  ident: 2021111618442570500_B74
  article-title: Mixed-linkage ubiquitin chains send mixed messages
  publication-title: Structure
  doi: 10.1016/j.str.2013.02.019
  contributor:
    fullname: Nakasone
– volume: 17
  start-page: 4909
  year: 1998
  ident: 2021111618442570500_B83
  article-title: Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
  publication-title: EMBO J.
  doi: 10.1093/emboj/17.17.4909
  contributor:
    fullname: Rubin
– volume: 21
  start-page: 220
  year: 2014
  ident: 2021111618442570500_B21
  article-title: Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2771
  contributor:
    fullname: Worden
– volume: 495
  start-page: 126
  year: 2013
  ident: 2021111618442570500_B1
  article-title: Corrigendum: global quantification of mammalian gene expression control
  publication-title: Nature
  doi: 10.1038/nature11848
  contributor:
    fullname: Schwanhausser
– volume: 2
  start-page: E13
  year: 2004
  ident: 2021111618442570500_B11
  article-title: The proteasome and the delicate balance between destruction and rescue
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.0020013
  contributor:
    fullname: Glickman
– volume: 482
  start-page: 186
  year: 2012
  ident: 2021111618442570500_B17
  article-title: Complete subunit architecture of the proteasome regulatory particle
  publication-title: Nature
  doi: 10.1038/nature10774
  contributor:
    fullname: Lander
– volume: 82
  start-page: 373
  year: 2002
  ident: 2021111618442570500_B4
  article-title: The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
  publication-title: Physiol. Rev.
  doi: 10.1152/physrev.00027.2001
  contributor:
    fullname: Glickman
– volume: 316
  start-page: 258
  year: 2010
  ident: 2021111618442570500_B89
  article-title: Knockdown of human deubiquitinase PSMD14 induces cell cycle arrest and senescence
  publication-title: Exp. Cell. Res.
  doi: 10.1016/j.yexcr.2009.08.018
  contributor:
    fullname: Byrne
– volume: 370
  start-page: 846
  year: 2007
  ident: 2021111618442570500_B23
  article-title: The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2007.04.084
  contributor:
    fullname: Sanches
– volume: 279
  start-page: 27168
  year: 2004
  ident: 2021111618442570500_B67
  article-title: Rpn7 is required for the structural integrity of the 26 S proteasome of Saccharomyces cerevisiae
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M314231200
  contributor:
    fullname: Isono
– volume: 301
  start-page: 57
  year: 2005
  ident: 2021111618442570500_B69
  article-title: Purification of proteasomes, proteasome subcomplexes, and proteasome-associated proteins from budding yeast
  publication-title: Methods Mol. Biol.
  contributor:
    fullname: Leggett
– volume: 133
  start-page: 17855
  year: 2011
  ident: 2021111618442570500_B73
  article-title: Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja207220g
  contributor:
    fullname: Castaneda
– volume: 284
  start-page: 24891
  year: 2009
  ident: 2021111618442570500_B92
  article-title: Subcomplexes of PA700, the 19 S regulator of the 26 S proteasome, reveal relative roles of AAA subunits in 26 S proteasome assembly and activation and ATPase activity
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M109.023218
  contributor:
    fullname: Thompson
– volume: 94
  start-page: 615
  year: 1998
  ident: 2021111618442570500_B16
  article-title: A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81603-7
  contributor:
    fullname: Glickman
– volume: 117
  start-page: 6447
  year: 2004
  ident: 2021111618442570500_B58
  article-title: Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability
  publication-title: J. Cell. Sci.
  doi: 10.1242/jcs.01575
  contributor:
    fullname: Funakoshi
– volume: 2
  start-page: 821
  year: 2001
  ident: 2021111618442570500_B33
  article-title: A protein-protein interaction map of the Caenorhabditis elegans 26S proteasome
  publication-title: EMBO Rep.
  doi: 10.1093/embo-reports/kve184
  contributor:
    fullname: Davy
– volume: 160
  start-page: 135
  year: 1995
  ident: 2021111618442570500_B62
  article-title: A Saccharomyces cerevisiae gene essential for viability has been conserved in evolution
  publication-title: Gene
  doi: 10.1016/0378-1119(95)00212-O
  contributor:
    fullname: Rinaldi
– volume: 8
  start-page: 508
  year: 2008
  ident: 2021111618442570500_B41
  article-title: Subunit-subunit interactions in the human 26S proteasome
  publication-title: Proteomics
  doi: 10.1002/pmic.200700588
  contributor:
    fullname: Chen
– volume: 489
  start-page: 263
  year: 2012
  ident: 2021111618442570500_B94
  article-title: RPN-6 determines C. elegans longevity under proteotoxic stress conditions
  publication-title: Nature
  doi: 10.1038/nature11315
  contributor:
    fullname: Vilchez
– volume: 35
  start-page: 260
  year: 2009
  ident: 2021111618442570500_B36
  article-title: PCI complexes: beyond the proteasome, CSN, and eIF3 Troika
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2009.07.009
  contributor:
    fullname: Pick
– volume: 109
  start-page: 149
  year: 2012
  ident: 2021111618442570500_B88
  article-title: The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.1117648108
  contributor:
    fullname: Pathare
– volume: 1
  start-page: 2005 0017
  year: 2005
  ident: 2021111618442570500_B72
  article-title: A uniform proteomics MS/MS analysis platform utilizing open XML file formats
  publication-title: Mol. Syst. Biol.
  doi: 10.1038/msb4100024
  contributor:
    fullname: Keller
– volume: 399
  start-page: 3
  year: 2005
  ident: 2021111618442570500_B75
  article-title: Chemical and genetic strategies for manipulating polyubiquitin chain structure
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(05)99001-0
  contributor:
    fullname: Volk
– volume: 118
  start-page: 31
  year: 2004
  ident: 2021111618442570500_B77
  article-title: Exploration of essential gene functions via titratable promoter alleles
  publication-title: Cell
  doi: 10.1016/j.cell.2004.06.013
  contributor:
    fullname: Mnaimneh
– volume: 279
  start-page: 1729
  year: 2004
  ident: 2021111618442570500_B10
  article-title: Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M307050200
  contributor:
    fullname: Guterman
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Snippet 26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S...
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Aggregation Database
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SubjectTerms Endopeptidases - genetics
Endopeptidases - metabolism
Gene Silencing
Models, Molecular
Mutation
Original Paper
Proteasome Endopeptidase Complex - chemistry
Proteasome Endopeptidase Complex - genetics
Proteasome Endopeptidase Complex - metabolism
Protein Domains
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
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Title Base-CP proteasome can serve as a platform for stepwise lid formation
URI https://www.ncbi.nlm.nih.gov/pubmed/26182356
https://search.proquest.com/docview/1697214885
https://pubmed.ncbi.nlm.nih.gov/PMC4438304
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