메뉴 건너뛰기




Volumn 17, Issue 7, 2003, Pages 1315-1331

Specific ubiquitin-conjugating enzymes promote degradation of specific nuclear receptor coactivators

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; CELL NUCLEUS RECEPTOR COACTIVATOR; COGNATE LIGAND; LIGAND; PROTEASOME; REGULATOR PROTEIN; TRANSACTIVATOR PROTEIN; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UNCLASSIFIED DRUG;

EID: 0038648919     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2002-0209     Document Type: Article
Times cited : (54)

References (89)
  • 1
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • Aranda A, Pascual A 2001 Nuclear hormone receptors and gene expression. Physiol Rev 81:1269-1304
    • (2001) Physiol Rev , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 2
    • 0033630453 scopus 로고    scopus 로고
    • Steroid/nuclear receptor coactivators
    • Chen JD 2000 Steroid/nuclear receptor coactivators. Vitam Horm 58:391-448
    • (2000) Vitam Horm , vol.58 , pp. 391-448
    • Chen, J.D.1
  • 4
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Cellular and molecular biology
    • McKenna NJ, Lanz RB, O'Malley BW 1999 Nuclear receptor coregulators: cellular and molecular biology. Endocr Rev 20:321-344
    • (1999) Endocr Rev , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.2    O'Malley, B.W.3
  • 6
    • 0034735863 scopus 로고    scopus 로고
    • From ligand to response: Generating diversity in nuclear receptor coregulator function
    • McKenna NJ, O'Malley BW 2000 From ligand to response: generating diversity in nuclear receptor coregulator function. J Steroid Biochem Mol Biol 74:351-356
    • (2000) J Steroid Biochem Mol Biol , vol.74 , pp. 351-356
    • McKenna, N.J.1    O'Malley, B.W.2
  • 7
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna NJ, O'Malley BW 2002 Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108:465-474
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 8
    • 0034454583 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulators in action: Diversity for shared tasks
    • Robyr D, Wolffe AP, Wahli W 2000 Nuclear hormone receptor coregulators in action: diversity for shared tasks. Mol Endocrinol 14:329-347
    • (2000) Mol Endocrinol , vol.14 , pp. 329-347
    • Robyr, D.1    Wolffe, A.P.2    Wahli, W.3
  • 9
    • 0035099604 scopus 로고    scopus 로고
    • Transcriptional coregulators of the nuclear receptor superfamily: Coactivators and corepressors
    • Lee JW, Lee YC, Na SY, Jung DJ, Lee SK 2001 Transcriptional coregulators of the nuclear receptor superfamily: coactivators and corepressors. Cell Mol Life Sci 58:289-297
    • (2001) Cell Mol Life Sci , vol.58 , pp. 289-297
    • Lee, J.W.1    Lee, Y.C.2    Na, S.Y.3    Jung, D.J.4    Lee, S.K.5
  • 10
    • 0024524385 scopus 로고
    • The contribution of the N- and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific
    • Bocquel MT, Kumar V, Stricker C, Chambon P, Gronemeyer H 1989 The contribution of the N- and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific. Nucleic Acids Res 17:2581-2595
    • (1989) Nucleic Acids Res , vol.17 , pp. 2581-2595
    • Bocquel, M.T.1    Kumar, V.2    Stricker, C.3    Chambon, P.4    Gronemeyer, H.5
  • 11
    • 0024564101 scopus 로고
    • Steroid hormone receptors compete for factors that mediate their enhancer function
    • Meyer ME, Gronemeyer H, Turcotte B, Bocquel MT, Tasset D, Chambon P 1989 Steroid hormone receptors compete for factors that mediate their enhancer function. Cell 57:433-442
    • (1989) Cell , vol.57 , pp. 433-442
    • Meyer, M.E.1    Gronemeyer, H.2    Turcotte, B.3    Bocquel, M.T.4    Tasset, D.5    Chambon, P.6
  • 12
    • 0026500080 scopus 로고
    • In vitro activity of the transcription activation functions of the progesterone receptor. Evidence for intermediary factors
    • Shemshedini L, Ji JW, Brou C, Chambon P, Gronemeyer H 1992 In vitro activity of the transcription activation functions of the progesterone receptor. Evidence for intermediary factors. J Biol Chem 267:1834-1839
    • (1992) J Biol Chem , vol.267 , pp. 1834-1839
    • Shemshedini, L.1    Ji, J.W.2    Brou, C.3    Chambon, P.4    Gronemeyer, H.5
  • 13
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H, Lin RJ, Schlitz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM 1997 Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569-580
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schlitz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 14
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y 1996 The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953-959
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 16
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner DE, Berger SL 2000 Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64:435-459
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 18
    • 0030948085 scopus 로고    scopus 로고
    • SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase
    • Fraser RA, Rossignol M, Heard DJ, Egly JM, Chambon P 1997 SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase. J Biol Chem 272:7122-7126
    • (1997) J Biol Chem , vol.272 , pp. 7122-7126
    • Fraser, R.A.1    Rossignol, M.2    Heard, D.J.3    Egly, J.M.4    Chambon, P.5
  • 19
    • 0029953663 scopus 로고    scopus 로고
    • Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors
    • Imhof MO, McDonnell DP 1996 Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors. Mol Cell Biol 16:2594-2605
    • (1996) Mol Cell Biol , vol.16 , pp. 2594-2605
    • Imhof, M.O.1    McDonnell, D.P.2
  • 20
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities
    • Koh SS, Chen D, Lee YH, Stallcup MR 2001 Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. J Biol Chem 276:1089-1098
    • (2001) J Biol Chem , vol.276 , pp. 1089-1098
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 22
    • 0032404015 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR
    • Masuyama H, MacDonald PN 1998 Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR. J Cell Biochem 71:429-440
    • (1998) J Cell Biochem , vol.71 , pp. 429-440
    • Masuyama, H.1    MacDonald, P.N.2
  • 23
    • 0032907106 scopus 로고    scopus 로고
    • The Angelman syndrome associated gene, E6-AP, is also a coactivator for the nuclear hormone receptor superfamily
    • Nawaz Z, Lonard, DM, Smith CL, Lehman EL, Tsai SL, Tsai M-J, O'Malley BW 1999 The Angelman syndrome associated gene, E6-AP, is also a coactivator for the nuclear hormone receptor superfamily. Mol Cell Biol 19:1182-1189
    • (1999) Mol Cell Biol , vol.19 , pp. 1182-1189
    • Nawaz, Z.1    Lonard, D.M.2    Smith, C.L.3    Lehman, E.L.4    Tsai, S.L.5    Tsai, M.-J.6    O'Malley, B.W.7
  • 24
    • 0033516662 scopus 로고    scopus 로고
    • Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription
    • Poukka H, Aarnisalo P, Karvonen U, Palvimo JJ, Janne OA 1999 Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription. J Biol Chem 274:19441-19446
    • (1999) J Biol Chem , vol.274 , pp. 19441-19446
    • Poukka, H.1    Aarnisalo, P.2    Karvonen, U.3    Palvimo, J.J.4    Janne, O.A.5
  • 25
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka H, Karvonen U, Janne OA, Palvimo JJ 2000 Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc Natl Acad Sci USA 97:14145-14150
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 28
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate SA, Tsai SY, Tsai MJ, O'Malley BW 1995 Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354-1357
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3    O'Malley, B.W.4
  • 29
    • 0029978605 scopus 로고    scopus 로고
    • GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors
    • Hong H, Kohli K, Trivedi A, Johnson DL, Stallcup MR 1996 GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc Natl Acad Sci USA 93:4948-4952
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4948-4952
    • Hong, H.1    Kohli, K.2    Trivedi, A.3    Johnson, D.L.4    Stallcup, M.R.5
  • 30
    • 0030949836 scopus 로고    scopus 로고
    • GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors
    • Hong H, Kohli K, Garabedian MJ, Stallcup MR 1997 GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol Cell Biol 17:2735-2744
    • (1997) Mol Cell Biol , vol.17 , pp. 2735-2744
    • Hong, H.1    Kohli, K.2    Garabedian, M.J.3    Stallcup, M.R.4
  • 31
    • 0029954339 scopus 로고    scopus 로고
    • TIF-2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel JJ, Heine MJ, Zechel C, Chambon P, Gronemeyer H 1996 TIF-2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J 15:3667-3675
    • (1996) EMBO J , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 33
    • 0030872716 scopus 로고    scopus 로고
    • RAC-3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF-2
    • Li H, Gomes PJ, Chen JD 1997 RAC-3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF-2. Proc Natl Acad Sci USA 94:8479-8484
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8479-8484
    • Li, H.1    Gomes, P.J.2    Chen, J.D.3
  • 34
    • 0030786270 scopus 로고    scopus 로고
    • TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1
    • Takeshita A, Cardona GR, Koibuchi N, Suen CS, Chin WW 1997 TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J Biol Chem 272:27629-27634
    • (1997) J Biol Chem , vol.272 , pp. 27629-27634
    • Takeshita, A.1    Cardona, G.R.2    Koibuchi, N.3    Suen, C.S.4    Chin, W.W.5
  • 36
    • 0033400343 scopus 로고    scopus 로고
    • Nuclear receptors: Coactivators, corepressors and chromatin remodeling in the control of transcription
    • Collingwood TN, Urnov FD, Wolffe AP 1999 Nuclear receptors: coactivators, corepressors and chromatin remodeling in the control of transcription. J Mol Endocrinol 23:255-275
    • (1999) J Mol Endocrinol , vol.23 , pp. 255-275
    • Collingwood, T.N.1    Urnov, F.D.2    Wolffe, A.P.3
  • 38
    • 0030054665 scopus 로고    scopus 로고
    • The hbrm and BRG-1 proteins, components of the human SNF/SWI complex, are phosphorylated and excluded from the condensed chromosomes during mitosis
    • Muchardt C, Reyes JC, Bourachot B, Leguoy E, Yaniv M 1996 The hbrm and BRG-1 proteins, components of the human SNF/SWI complex, are phosphorylated and excluded from the condensed chromosomes during mitosis. EMBO J 15:3394-3402
    • (1996) EMBO J , vol.15 , pp. 3394-3402
    • Muchardt, C.1    Reyes, J.C.2    Bourachot, B.3    Leguoy, E.4    Yaniv, M.5
  • 39
    • 0030971868 scopus 로고    scopus 로고
    • Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix
    • Reyes JC, Muchardt C, Yaniv M 1997 Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix. J Cell Biol 137:263-274
    • (1997) J Cell Biol , vol.137 , pp. 263-274
    • Reyes, J.C.1    Muchardt, C.2    Yaniv, M.3
  • 40
    • 0000279559 scopus 로고    scopus 로고
    • Importance of the regulation of nuclear receptor degradation
    • Dennis AP, Haq RU, Nawaz Z 2001 Importance of the regulation of nuclear receptor degradation. Front Biosci 6:D954-D959
    • (2001) Front Biosci , vol.6
    • Dennis, A.P.1    Haq, R.U.2    Nawaz, Z.3
  • 41
    • 0028890361 scopus 로고
    • Interaction of thyroid-hormone receptor with a conserved transcriptional mediator
    • Lee JW, Ryan F, Swaffield JC, Johnston SA, Moore DD 1995 Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. Nature 374:91-94
    • (1995) Nature , vol.374 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, J.C.3    Johnston, S.A.4    Moore, D.D.5
  • 42
    • 0032526024 scopus 로고    scopus 로고
    • Proteasomal regulation of nuclear receptor corepressor-mediated transcription
    • Zhang J, Guenther MG, Carthew RW, Lazar MA 1998 Proteasomal regulation of nuclear receptor corepressor-mediated transcription. Genes Dev 12:1775-1780
    • (1998) Genes Dev , vol.12 , pp. 1775-1780
    • Zhang, J.1    Guenther, M.G.2    Carthew, R.W.3    Lazar, M.A.4
  • 43
    • 0033304776 scopus 로고    scopus 로고
    • Proteasome-mediated proteolysis of estrogen receptor: A novel component in autologous down-regulation
    • Alarid ET, Bakopoulos N, Solodin N 1999 Proteasome-mediated proteolysis of estrogen receptor: a novel component in autologous down-regulation. Mol Endocrinol 13:1522-1534
    • (1999) Mol Endocrinol , vol.13 , pp. 1522-1534
    • Alarid, E.T.1    Bakopoulos, N.2    Solodin, N.3
  • 44
    • 0033060824 scopus 로고    scopus 로고
    • Implication of proteasome in estrogen receptor degradation
    • El Khissiin A, Leclercq G 1999 Implication of proteasome in estrogen receptor degradation. FEBS Lett 448:160-166
    • (1999) FEBS Lett , vol.448 , pp. 160-166
    • El Khissiin, A.1    Leclercq, G.2
  • 45
    • 0033967491 scopus 로고    scopus 로고
    • Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome
    • Lange CA, Shen T, Horwitz KB 2000 Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome. Proc Natl Acad Sci USA 97:1032-1037
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1032-1037
    • Lange, C.A.1    Shen, T.2    Horwitz, K.B.3
  • 47
    • 0029100143 scopus 로고
    • Ubiquitination of the rat uterine estrogen receptor: Dependence on estradiol
    • Nirmala PB, Thampan RV 1995 Ubiquitination of the rat uterine estrogen receptor: dependence on estradiol. Biochem Biophys Res Commun 213:24-31
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 24-31
    • Nirmala, P.B.1    Thampan, R.V.2
  • 48
    • 0033554012 scopus 로고    scopus 로고
    • 9-cis-Retinoic acid decreases the level of its cognate receptor, retinoid X receptor, through acceleration of the turnover
    • Nomura Y, Nagaya T, Hayashi Y, Kambe F, Seo H 1999 9-cis-Retinoic acid decreases the level of its cognate receptor, retinoid X receptor, through acceleration of the turnover. Biochem Biophys Res Commun 260:729-733
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 729-733
    • Nomura, Y.1    Nagaya, T.2    Hayashi, Y.3    Kambe, F.4    Seo, H.5
  • 49
    • 0032544474 scopus 로고    scopus 로고
    • Evidence for enhanced ubiquitin-mediated proteolysis of the chicken progesterone receptor by progesterone
    • Syvala H, Vienonen A, Zhuang YH, Kivineva M, Ylikomi T, Tuohimaa P 1998 Evidence for enhanced ubiquitin-mediated proteolysis of the chicken progesterone receptor by progesterone. Life Sci 63:1505-1512
    • (1998) Life Sci , vol.63 , pp. 1505-1512
    • Syvala, H.1    Vienonen, A.2    Zhuang, Y.H.3    Kivineva, M.4    Ylikomi, T.5    Tuohimaa, P.6
  • 51
    • 0033638393 scopus 로고    scopus 로고
    • The 26S proteasome is required for estrogen receptor-α and coactivator turnover and for efficient estrogen receptor-α transactivation
    • Lonard DM, Nawaz Z, Smith CL, O'Malley BW 2000 The 26S proteasome is required for estrogen receptor-α and coactivator turnover and for efficient estrogen receptor-α transactivation. Mol Cell 5:939-948
    • (2000) Mol Cell , vol.5 , pp. 939-948
    • Lonard, D.M.1    Nawaz, Z.2    Smith, C.L.3    O'Malley, B.W.4
  • 52
    • 0035900780 scopus 로고    scopus 로고
    • Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids
    • Wallace AD, Cidlowski JA 2001 Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J Biol Chem 276:42714-42721
    • (2001) J Biol Chem , vol.276 , pp. 42714-42721
    • Wallace, A.D.1    Cidlowski, J.A.2
  • 53
    • 0036132133 scopus 로고    scopus 로고
    • Molecular perspectives on selective estrogen receptor modulators (SERMs): Progress in understanding their tissue-specific agonist and antagonist actions
    • Lonard DM, Smith CL 2002 Molecular perspectives on selective estrogen receptor modulators (SERMs): progress in understanding their tissue-specific agonist and antagonist actions. Steroids 67:15-24
    • (2002) Steroids , vol.67 , pp. 15-24
    • Lonard, D.M.1    Smith, C.L.2
  • 54
    • 0000413462 scopus 로고    scopus 로고
    • Regulation of interferon-γ-activated STAT1 by the ubiquitin-proteasome pathway
    • Kim TK, Maniatis T 1996 Regulation of interferon-γ-activated STAT1 by the ubiquitin-proteasome pathway. Science 273:1717-1719
    • (1996) Science , vol.273 , pp. 1717-1719
    • Kim, T.K.1    Maniatis, T.2
  • 55
    • 0030790796 scopus 로고    scopus 로고
    • Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack
    • Li S, Li Y, Carthew RW, Lai ZC 1997 Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack. Cell 90:469-478
    • (1997) Cell , vol.90 , pp. 469-478
    • Li, S.1    Li, Y.2    Carthew, R.W.3    Lai, Z.C.4
  • 57
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κ B1 precursor protein and the activation of NF-κB
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T 1994 The ubiquitin-proteasome pathway is required for processing the NF-κ B1 precursor protein and the activation of NF-κB. Cell 78:773-785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 58
    • 0030888109 scopus 로고    scopus 로고
    • The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase
    • Huibregtse JM, Yang JC, Beaudenon SL 1997 The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc Natl Acad Sci USA 94:3656-3661
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3656-3661
    • Huibregtse, J.M.1    Yang, J.C.2    Beaudenon, S.L.3
  • 59
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien DL, Cummings CJ, Adams HP, Mancini MG, Patel K, DeMartino GN, Marcelli M, Weigel NL, Mancini MA 1999 Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum Mol Genet 8:731-741
    • (1999) Hum Mol Genet , vol.8 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3    Mancini, M.G.4    Patel, K.5    DeMartino, G.N.6    Marcelli, M.7    Weigel, N.L.8    Mancini, M.A.9
  • 60
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman AM 2001 Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2:169-178
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 62
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM 2001 Mechanisms underlying ubiquitination. Annu Rev Biochem 70:503-533
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 63
    • 0029036701 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM 1995 A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci USA 92:2563-2567
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 64
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM 1995 A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci USA 92:5249
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5249
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 65
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • Finley D, Ciechanover A, Varshavsky A 1984 Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell 37:43-55
    • (1984) Cell , vol.37 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 66
    • 0035058061 scopus 로고    scopus 로고
    • The glucocorticoid receptor interacting protein 1 (GRIP1) localizes in discrete nuclear foci that associate with ND10 bodies and are enriched in components of the 26S proteasome
    • Baumann CT, Ma H, Wolford R, Reyes JC, Maruvada P, Lim C, Yen PM, Stallcup MR, Hager GL 2001 The glucocorticoid receptor interacting protein 1 (GRIP1) localizes in discrete nuclear foci that associate with ND10 bodies and are enriched in components of the 26S proteasome. Mol Endocrinol 15:485-500
    • (2001) Mol Endocrinol , vol.15 , pp. 485-500
    • Baumann, C.T.1    Ma, H.2    Wolford, R.3    Reyes, J.C.4    Maruvada, P.5    Lim, C.6    Yen, P.M.7    Stallcup, M.R.8    Hager, G.L.9
  • 69
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator
    • Perkins ND, Felzien LK, Betts JC, Leung K, Beach DH, Nabel GJ 1997 Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator. Science 275:523-527
    • (1997) Science , vol.275 , pp. 523-527
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 71
    • 0033610866 scopus 로고    scopus 로고
    • CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1
    • Fronsdal K, Engedal N, Slagsvold T, Saatcioglu F 1998 CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1. J Biol Chem 273:31853-31859
    • (1998) J Biol Chem , vol.273 , pp. 31853-31859
    • Fronsdal, K.1    Engedal, N.2    Slagsvold, T.3    Saatcioglu, F.4
  • 73
    • 0032491483 scopus 로고    scopus 로고
    • Nuclear integration of glucocorticoid receptor and nuclear factor-κB signaling by CREB-binding protein and steroid receptor coactivator-1
    • Sheppard KA, Phelps KM, Williams AJ, Thanos D, Glass CK, Rosenfeld MG, Gerritsen ME, Collins T 1998 Nuclear integration of glucocorticoid receptor and nuclear factor-κB signaling by CREB-binding protein and steroid receptor coactivator-1. J Biol Chem 273:29291-29294
    • (1998) J Biol Chem , vol.273 , pp. 29291-29294
    • Sheppard, K.A.1    Phelps, K.M.2    Williams, A.J.3    Thanos, D.4    Glass, C.K.5    Rosenfeld, M.G.6    Gerritsen, M.E.7    Collins, T.8
  • 75
    • 0032525905 scopus 로고    scopus 로고
    • The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate
    • Nuber U, Schwarz SE, Scheffner M 1998 The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate. Eur J Biochem 254:643-649
    • (1998) Eur J Biochem , vol.254 , pp. 643-649
    • Nuber, U.1    Schwarz, S.E.2    Scheffner, M.3
  • 76
    • 0036904663 scopus 로고    scopus 로고
    • UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis
    • Xie Y, Vashavsky A 2002 UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat Cell Biol 12:1003-1007
    • (2002) Nat Cell Biol , vol.12 , pp. 1003-1007
    • Xie, Y.1    Vashavsky, A.2
  • 77
    • 0024781014 scopus 로고
    • PEST regions, proteolysis and cell cycle progression
    • Rechsteiner M 1989 PEST regions, proteolysis and cell cycle progression. Rev Biol Celular 20:235-253
    • (1989) Rev Biol Celular , vol.20 , pp. 235-253
    • Rechsteiner, M.1
  • 78
    • 0025584623 scopus 로고
    • PEST sequences are signals for rapid intracellular proteolysis
    • Rechsteiner M 1990 PEST sequences are signals for rapid intracellular proteolysis. Semin Cell Biol 1:433-440
    • (1990) Semin Cell Biol , vol.1 , pp. 433-440
    • Rechsteiner, M.1
  • 79
    • 0034711290 scopus 로고    scopus 로고
    • Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-β signaling
    • Lin X, Liang M, Feng XH 2000 Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-β signaling. J Biol Chem 275:36818-36822
    • (2000) J Biol Chem , vol.275 , pp. 36818-36822
    • Lin, X.1    Liang, M.2    Feng, X.H.3
  • 80
    • 0033549789 scopus 로고    scopus 로고
    • A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
    • Zhu H, Kavsak P, Abdollah S, Wrana JL, Thomsen GH 1999 A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 400:687-693
    • (1999) Nature , vol.400 , pp. 687-693
    • Zhu, H.1    Kavsak, P.2    Abdollah, S.3    Wrana, J.L.4    Thomsen, G.H.5
  • 81
    • 0033119041 scopus 로고    scopus 로고
    • Degradation of MyoD by the ubiquitin pathway: Regulation by specific DNA-binding and identification of a novel site for ubiquitination
    • Ciechanover A, Breitschopf K, Hatoum OA, Bengal E 1999 Degradation of MyoD by the ubiquitin pathway: regulation by specific DNA-binding and identification of a novel site for ubiquitination. Mol Biol Rep 26:59-64
    • (1999) Mol Biol Rep , vol.26 , pp. 59-64
    • Ciechanover, A.1    Breitschopf, K.2    Hatoum, O.A.3    Bengal, E.4
  • 83
    • 0035929585 scopus 로고    scopus 로고
    • The human estrogen receptor-α is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators
    • Wijayaratne AL, McDonnell DP 2001 The human estrogen receptor-α is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators. J Biol Chem 276:35684-35692
    • (2001) J Biol Chem , vol.276 , pp. 35684-35692
    • Wijayaratne, A.L.1    McDonnell, D.P.2
  • 84
    • 0037036452 scopus 로고    scopus 로고
    • Proteasome inhibitors reduce luciferase and β-galactosidase activity in tissue culture cells
    • Deroo BJ, Archer TK 2002 Proteasome inhibitors reduce luciferase and β-galactosidase activity in tissue culture cells. J Biol Chem 277:20120-20123
    • (2002) J Biol Chem , vol.277 , pp. 20120-20123
    • Deroo, B.J.1    Archer, T.K.2
  • 85
    • 0033525687 scopus 로고    scopus 로고
    • Competition between thyroid hormone receptor-associated protein (TRAP) 220 and transcriptional intermediary factor (TIF) 2 for binding to nuclear receptors. Implications for the recruitment of TRAP and p160 coactivator complexes
    • Treuter E, Johansson L, Thomsen JS, Warnmark A, Leers J, Pelto-Huikko M, Sjoberg M, Wright AP, Spyrou G, Gustafsson JA 1999 Competition between thyroid hormone receptor-associated protein (TRAP) 220 and transcriptional intermediary factor (TIF) 2 for binding to nuclear receptors. Implications for the recruitment of TRAP and p160 coactivator complexes. J Biol Chem 274:6667-6677
    • (1999) J Biol Chem , vol.274 , pp. 6667-6677
    • Treuter, E.1    Johansson, L.2    Thomsen, J.S.3    Warnmark, A.4    Leers, J.5    Pelto-Huikko, M.6    Sjoberg, M.7    Wright, A.P.8    Spyrou, G.9    Gustafsson, J.A.10
  • 86
    • 0029131894 scopus 로고
    • The cellular content of Cdc25p, the Ras exchange factor in Saccharomyces cerevisiae, is regulated by destabilization through a cyclin destruction box
    • Kaplon T, Jacquet M 1995 The cellular content of Cdc25p, the Ras exchange factor in Saccharomyces cerevisiae, is regulated by destabilization through a cyclin destruction box. J Biol Chem 270:20742-20747
    • (1995) J Biol Chem , vol.270 , pp. 20742-20747
    • Kaplon, T.1    Jacquet, M.2
  • 87
    • 0028971506 scopus 로고
    • NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein C, Springael JY, Volland C, Haguenauer-Tsapis R, Andre B 1995 NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol Microbiol 18:77-87
    • (1995) Mol Microbiol , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    Andre, B.5
  • 88
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas AL, Siepmann TJ 1997 Pathways of ubiquitin conjugation. FASEB J 11:1257-1268
    • (1997) FASEB J , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 89
    • 0026769411 scopus 로고
    • Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis
    • Hatfield PM, Vierstra RD 1992 Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis. J Biol Chem 267:14799-14803
    • (1992) J Biol Chem , vol.267 , pp. 14799-14803
    • Hatfield, P.M.1    Vierstra, R.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.