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Volumn 25, Issue 12, 2014, Pages 1824-1835

Autoregulation of the 26S proteasome by in situ ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

26S PROTEASOME; ADRM1 PROTEIN; DEUBIQUITINASE; POLYUBIQUITIN; PROTEASOME; PROTEIN; RPT5 PROTEIN; S5A PROTEIN; SMALL INTERFERING RNA; UBIQUITINATED PROTEIN; UCH37 PROTEIN; UNCLASSIFIED DRUG; ADRM1 PROTEIN, HUMAN; ATP DEPENDENT 26S PROTEASE; MEMBRANE PROTEIN; PROTEIN SUBUNIT; PSMD4 PROTEIN, HUMAN; UBE2D1 PROTEIN, HUMAN; UBE3A PROTEIN, HUMAN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE; UBIQUITIN THIOLESTERASE; UCHL5 PROTEIN, HUMAN;

EID: 84902668478     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-10-0585     Document Type: Article
Times cited : (64)

References (60)
  • 1
    • 84866269021 scopus 로고    scopus 로고
    • Near-atomic resolution structural model of the yeast 26S proteasome
    • Beck F et al. (2012). Near-atomic resolution structural model of the yeast 26S proteasome. Proc Natl Acad Sci USA 109, 14870-14875.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 14870-14875
    • Beck, F.1
  • 2
    • 64849084080 scopus 로고    scopus 로고
    • Isolation of mammalian 26S proteasomes and p97/VCP complexes using the ubiquitin-like domain from HHR23B reveals novel proteasome-associated proteins
    • Besche HC, Haas W, Gygi SP, Goldberg AL (2009). Isolation of mammalian 26S proteasomes and p97/VCP complexes using the ubiquitin-like domain from HHR23B reveals novel proteasome-associated proteins. Biochemistry 48, 2538-2549.
    • (2009) Biochemistry , vol.48 , pp. 2538-2549
    • Besche, H.C.1    Haas, W.2    Gygi, S.P.3    Goldberg, A.L.4
  • 3
    • 84876935501 scopus 로고    scopus 로고
    • Proteasome regulation by ADP-ribosylation
    • Cho-Park PF, Steller H (2013). Proteasome regulation by ADP-ribosylation. Cell 153, 614-627.
    • (2013) Cell , vol.153 , pp. 614-627
    • Cho-Park, P.F.1    Steller, H.2
  • 4
    • 0026506729 scopus 로고
    • Purification and characterization of a protein inhibitor of the 20S proteasome (macropain)
    • Chu-Ping M, Slaughter CA, DeMartino GN (1992). Purification and characterization of a protein inhibitor of the 20S proteasome (macropain). Biochim Biophys Acta 1119, 303-311.
    • (1992) Biochim Biophys Acta , vol.1119 , pp. 303-311
    • Chu-Ping, M.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 5
    • 0028025326 scopus 로고
    • Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20 S proteasome
    • Chu-Ping M, Vu JH, Proske RJ, Slaughter CA, DeMartino GN (1994). Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20 S proteasome. J Biol Chem 269, 3539-3547. (Pubitemid 24237678)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.5 , pp. 3539-3547
    • Chu-Ping, M.1    Vu, J.H.2    Proske, R.J.3    Slaughter, C.A.4    DeMartino, G.N.5
  • 7
    • 84859702750 scopus 로고    scopus 로고
    • Molecular model of the human 26S proteasome
    • da Fonseca PC, He J, Morris EP (2012). Molecular model of the human 26S proteasome. Mol Cell 46, 54-66.
    • (2012) Mol Cell , vol.46 , pp. 54-66
    • Da Fonseca, P.C.1    He, J.2    Morris, E.P.3
  • 9
    • 84856085129 scopus 로고    scopus 로고
    • Inhibition of proteasome deubiquitinating activity as a new cancer therapy
    • D'Arcy P et al. (2011). Inhibition of proteasome deubiquitinating activity as a new cancer therapy. Nat Med 17, 1636-1640.
    • (2011) Nat Med , vol.17 , pp. 1636-1640
    • D'Arcy, P.1
  • 12
    • 27144495057 scopus 로고    scopus 로고
    • E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer
    • DOI 10.1038/nsmb984, PII N984
    • Eletr ZM, Huang DT, Duda DM, Schulman BA, Kuhlman B (2005). E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer. Nat Struct Mol Biol 12, 933-934. (Pubitemid 41486719)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 933-934
    • Eletr, Z.M.1    Huang, D.T.2    Duda, D.M.3    Schulman, B.A.4    Kuhlman, B.5
  • 14
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D (2009). Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78, 477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 15
    • 84863872261 scopus 로고    scopus 로고
    • Protein degradation and the stress response
    • Flick K, Kaiser P (2012). Protein degradation and the stress response. Semin Cell Dev Biol 23, 515-522.
    • (2012) Semin Cell Dev Biol , vol.23 , pp. 515-522
    • Flick, K.1    Kaiser, P.2
  • 16
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • DOI 10.1042/BJ20030282
    • Fuertes G, Martin de Llano JJ, Villarroya A, Rivett AJ, Knecht E (2003). Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem J 375, 75-86. (Pubitemid 37255383)
    • (2003) Biochemical Journal , vol.375 , Issue.1 , pp. 75-86
    • Fuertes, G.1    Martin, D.L.J.J.2    Villarroya, A.3    Rivett, A.J.4    Knecht, E.5
  • 17
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A (2002). The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82, 373-428. (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 18
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 A resolution
    • DOI 10.1038/386463a0
    • Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber R (1997). Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386, 463-471. (Pubitemid 27164066)
    • (1997) Nature , vol.386 , Issue.6624 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3    Stock, D.4    Bochtler, M.5    Bartunik, H.D.6    Huber, R.7
  • 20
    • 33749348820 scopus 로고    scopus 로고
    • A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
    • DOI 10.1038/sj.emboj.7601338, PII 7601338
    • Hamazaki J, Iemura S, Natsume T, Yashiroda H, Tanaka K, Murata S (2006). A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J 25, 4524-4536. (Pubitemid 44498126)
    • (2006) EMBO Journal , vol.25 , Issue.19 , pp. 4524-4536
    • Hamazaki, J.1    Iemura, S.-I.2    Natsume, T.3    Yashiroda, H.4    Tanaka, K.5    Murata, S.6
  • 22
    • 34249007126 scopus 로고    scopus 로고
    • A Ubiquitin Stress Response Induces Altered Proteasome Composition
    • DOI 10.1016/j.cell.2007.03.042, PII S009286740700459X
    • Hanna J, Meides A, Zhang DP, Finley D (2007). A ubiquitin stress response induces altered proteasome composition. Cell 129, 747-759. (Pubitemid 46802382)
    • (2007) Cell , vol.129 , Issue.4 , pp. 747-759
    • Hanna, J.1    Meides, A.2    Zhang, D.P.3    Finley, D.4
  • 23
    • 34250375116 scopus 로고    scopus 로고
    • E3-Independent Monoubiquitination of Ubiquitin-Binding Proteins
    • DOI 10.1016/j.molcel.2007.05.014, PII S1097276507003152
    • Hoeller D, Hecker CM, Wagner S, Rogov V, Dotsch V, Dikic I (2007). E3-independent monoubiquitination of ubiquitin-binding proteins. Mol Cell 26, 891-898. (Pubitemid 46921003)
    • (2007) Molecular Cell , vol.26 , Issue.6 , pp. 891-898
    • Hoeller, D.1    Hecker, C.-M.2    Wagner, S.3    Rogov, V.4    Dotsch, V.5    Dikic, I.6
  • 26
    • 72149130935 scopus 로고    scopus 로고
    • The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome
    • Jacobson AD, Zhang NY, Xu P, Han KJ, Noone S, Peng J, Liu CW (2009). The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome. J Biol Chem 284, 35485-35494.
    • (2009) J Biol Chem , vol.284 , pp. 35485-35494
    • Jacobson, A.D.1    Zhang, N.Y.2    Xu, P.3    Han, K.J.4    Noone, S.5    Peng, J.6    Liu, C.W.7
  • 27
    • 0029588670 scopus 로고
    • Identification of a family of closely related human ubiquitin conjugating enzymes
    • DOI 10.1074/jbc.270.51.30408
    • Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM (1995). Identification of a family of closely related human ubiquitin conjugating enzymes. J Biol Chem 270, 30408-30414. (Pubitemid 26005094)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.51 , pp. 30408-30414
    • Jensen, J.P.1    Bates, P.W.2    Yang, M.3    Vierstra, R.D.4    Weissman, A.M.5
  • 29
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • Kim W et al. (2011). Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell 44, 325-340.
    • (2011) Mol Cell , vol.44 , pp. 325-340
    • Kim, W.1
  • 30
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • DOI 10.1038/416763a
    • Lam YA, Lawson TG, Velayutham M, Zweier JL, Pickart CM (2002). A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 416, 763-767. (Pubitemid 34429155)
    • (2002) Nature , vol.416 , Issue.6882 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweler, J.L.4    Pickart, C.M.5
  • 31
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • DOI 10.1038/385737a0
    • Lam YA, Xu W, DeMartino GN, Cohen RE (1997). Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385, 737-740. (Pubitemid 27098096)
    • (1997) Nature , vol.385 , Issue.6618 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    DeMartino, G.N.3    Cohen, R.E.4
  • 34
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • Lee BH et al. (2010). Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467, 179-184.
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1
  • 35
    • 84859184764 scopus 로고    scopus 로고
    • Ubiquitylation of Drosophila p54/Rpn10/S5a regulates its interaction with the UBA-UBL polyubiquitin receptors
    • Lipinszki Z, Kovacs L, Deak P, Udvardy A (2012). Ubiquitylation of Drosophila p54/Rpn10/S5a regulates its interaction with the UBA-UBL polyubiquitin receptors. Biochemistry 51, 2461-2470.
    • (2012) Biochemistry , vol.51 , pp. 2461-2470
    • Lipinszki, Z.1    Kovacs, L.2    Deak, P.3    Udvardy, A.4
  • 36
    • 84872773589 scopus 로고    scopus 로고
    • Functions of the 19S complex in proteasomal degradation
    • Liu CW, Jacobson AD (2013). Functions of the 19S complex in proteasomal degradation. Trends Biochem Sci 38, 103-110.
    • (2013) Trends Biochem Sci , vol.38 , pp. 103-110
    • Liu, C.W.1    Jacobson, A.D.2
  • 37
  • 39
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger MB, Hristova VA, Weissman AM (2012). HECT and RING finger families of E3 ubiquitin ligases at a glance. J. Cell Sci 125, 531-537.
    • (2012) J. Cell Sci , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 40
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • DOI 10.1038/nrm1336
    • Pickart CM, Cohen RE (2004). Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 5, 177-187. (Pubitemid 38325799)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.3 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 41
    • 33845713194 scopus 로고    scopus 로고
    • hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
    • DOI 10.1038/sj.emboj.7601450, PII 7601450
    • Qiu XB, Ouyang SY, Li CJ, Miao S, Wang L, Goldberg AL (2006). hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. EMBO J 25, 5742-5753. (Pubitemid 44967758)
    • (2006) EMBO Journal , vol.25 , Issue.24 , pp. 5742-5753
    • Qiu, X.-B.1    Ouyang, S.-Y.2    Li, C.-J.3    Miao, S.4    Wang, L.5    Goldberg, A.L.6
  • 43
    • 84859175458 scopus 로고    scopus 로고
    • FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis
    • Rani N, Aichem A, Schmidtke G, Kreft SG, Groettrup M (2012). FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis. Nat Commun 3, 749.
    • (2012) Nat Commun , vol.3 , pp. 749
    • Rani, N.1    Aichem, A.2    Schmidtke, G.3    Kreft, S.G.4    Groettrup, M.5
  • 44
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu FE, Ventii KH, Wilkinson KD (2009). Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem 78, 363-397.
    • (2009) Annu Rev Biochem , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 45
  • 46
    • 79957933700 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway and cellular responses to oxidative stress
    • Shang F, Taylor A (2011). Ubiquitin-proteasome pathway and cellular responses to oxidative stress. Free Radic Biol Med 51, 5-16.
    • (2011) Free Radic Biol Med , vol.51 , pp. 5-16
    • Shang, F.1    Taylor, A.2
  • 47
    • 77953467032 scopus 로고    scopus 로고
    • Characterization of the brain 26S proteasome and its interacting proteins
    • Tai HC, Besche H, Goldberg AL, Schuman EM (2010). Characterization of the brain 26S proteasome and its interacting proteins. Front Mol Neurosci 3, 12.
    • (2010) Front Mol Neurosci , vol.3 , pp. 12
    • Tai, H.C.1    Besche, H.2    Goldberg, A.L.3    Schuman, E.M.4
  • 49
  • 50
    • 77951945222 scopus 로고    scopus 로고
    • Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: Implications for proteasome structure and assembly
    • Tomko RJJr, Funakoshi M, Schneider K, Wang J, Hochstrasser M (2010). Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly. Mol Cell 38, 393-403.
    • (2010) Mol Cell , vol.38 , pp. 393-403
    • Tomko Jr., R.J.1    Funakoshi, M.2    Schneider, K.3    Wang, J.4    Hochstrasser, M.5
  • 51
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • DOI 10.1126/science.1075898
    • Verma R, Aravind L, Oania R, McDonald WH, Yates JRIII, Koonin EV, Deshaies RJ (2002). Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611-615. (Pubitemid 35215317)
    • (2002) Science , vol.298 , Issue.5593 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates III, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 52
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • Verma R, Chen S, Feldman R, Schieltz D, Yates J, Dohmen J, Deshaies RJ (2000). Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol Biol Cell 11, 3425-3439.
    • (2000) Mol Biol Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 53
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • DOI 10.1016/j.cell.2004.06.014, PII S0092867404005835
    • Verma R, Oania R, Graumann J, Deshaies RJ (2004). Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99-110. (Pubitemid 38902817)
    • (2004) Cell , vol.118 , Issue.1 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 55
    • 29244447753 scopus 로고    scopus 로고
    • Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis
    • DOI 10.1038/sj.emboj.7600895
    • Wang M, Pickart CM (2005). Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis. EMBO J 24, 4324-4333. (Pubitemid 41828907)
    • (2005) EMBO Journal , vol.24 , Issue.24 , pp. 4324-4333
    • Wang, M.1    Pickart, C.M.2
  • 56
    • 33947380146 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the affinity-purified human 26S proteasome complex
    • DOI 10.1021/bi061994u
    • Wang X, Chen CF, Baker PR, Chen PL, Kaiser P, Huang L (2007). Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry 46, 3553-3565. (Pubitemid 46449172)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3553-3565
    • Wang, X.1    Chen, C.-F.2    Baker, P.R.3    Chen, P.-L.4    Kaiser, P.5    Huang, L.6
  • 57
    • 78649980437 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome complex during oxidative stress
    • Wang X, Yen J, Kaiser P, Huang L (2010). Regulation of the 26S proteasome complex during oxidative stress. Sci Signal 151, ra88.
    • (2010) Sci Signal , vol.151
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 58
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao T, Cohen RE (2002). A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 60
    • 67349242723 scopus 로고    scopus 로고
    • E2 interaction and dimerization in the crystal structure of TRAF6
    • Yin Q et al. (2009). E2 interaction and dimerization in the crystal structure of TRAF6. Nat Struct Mol Biol 16, 658-666.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 658-666
    • Yin, Q.1


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