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Volumn 25, Issue 1, 2011, Pages 58-71

Regulation of glucocorticoid receptor activity by a stress responsive transcriptional cofactor

Author keywords

[No Author keywords available]

Indexed keywords

ESTROGEN RECEPTOR; GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN; PROTEASOME; PROTEIN P300; TETRATRICOPEPTIDE REPEAT DOMAIN 5 PROTEIN; TETRATRICOPEPTIDE REPEAT PROTEIN; TRANSCRIPTION FACTOR; UBIQUITIN LIGASE MURINE DOUBLE MINUTE 2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 78650897180     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2010-0212     Document Type: Article
Times cited : (22)

References (53)
  • 2
    • 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
  • 3
    • 0030900729 scopus 로고    scopus 로고
    • Mouse glucocorticoid receptor phosphorylation status influences multiple functions of the receptor protein
    • Webster JC, Jewell CM, Bodwell JE, Munck A, Sar M, Cidlowski JA 1997 Mouse glucocorticoid receptor phosphorylation status influences multiple functions of the receptor protein. J Biol Chem 272: 9287-9293
    • (1997) J Biol Chem , vol.272 , pp. 9287-9293
    • Webster, J.C.1    Jewell, C.M.2    Bodwell, J.E.3    Munck, A.4    Sar, M.5    Cidlowski, J.A.6
  • 4
    • 0035883863 scopus 로고    scopus 로고
    • Ligand-dependent interaction of the glucocorticoid receptor with p53 enhances their degradation by Hdm2
    • Sengupta S, Wasylyk B 2001 Ligand-dependent interaction of the glucocorticoid receptor with p53 enhances their degradation by Hdm2. Genes Dev 15: 2367-2380
    • (2001) Genes Dev , vol.15 , pp. 2367-2380
    • Sengupta, S.1    Wasylyk, B.2
  • 5
    • 0041630956 scopus 로고    scopus 로고
    • Estrogen receptor-dependent proteasomal degradation of the glucocorticoid receptor is coupled to an increase in mdm2 protein expression
    • Kinyamu HK, Archer TK 2003 Estrogen receptor-dependent proteasomal degradation of the glucocorticoid receptor is coupled to an increase in mdm2 protein expression. Mol Cell Biol 23: 5867-5881
    • (2003) Mol Cell Biol , vol.23 , pp. 5867-5881
    • Kinyamu, H.K.1    Archer, T.K.2
  • 7
    • 1642392035 scopus 로고    scopus 로고
    • Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation
    • Galigniana MD, Harrell JM, Housley PR, Patterson C, Fisher SK, Pratt WB 2004 Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation. Brain Res Mol Brain Res 123: 27-36
    • (2004) Brain Res Mol Brain Res , vol.123 , pp. 27-36
    • Galigniana, M.D.1    Harrell, J.M.2    Housley, P.R.3    Patterson, C.4    Fisher, S.K.5    Pratt, W.B.6
  • 8
    • 22344452512 scopus 로고    scopus 로고
    • Alternative effects of the ubiquitinproteasome pathway on glucocorticoid receptor down-regulation and transactivation are mediated by CHIP, an E3 ligase
    • Wang X, DeFranco DB 2005 Alternative effects of the ubiquitinproteasome pathway on glucocorticoid receptor down-regulation and transactivation are mediated by CHIP, an E3 ligase. Mol Endocrinol 19: 1474-1482
    • (2005) Mol Endocrinol , vol.19 , pp. 1474-1482
    • Wang, X.1    DeFranco, D.B.2
  • 9
    • 0032907106 scopus 로고    scopus 로고
    • The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily
    • Nawaz Z, Lonard DM, Smith CL, Lev-Lehman E, Tsai SY, Tsai MJ, O'Malley BW 1999 The Angelman syndrome-associated protein, E6-AP, is 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    Lev-Lehman, E.4    Tsai, S.Y.5    Tsai, M.J.6    O'Malley, B.W.7
  • 10
    • 12144290835 scopus 로고    scopus 로고
    • Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes
    • Stavreva DA, Müller WG, Hager GL, Smith CL, McNally JG 2004 Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes. Mol Cell Biol 24: 2682-2697
    • (2004) Mol Cell Biol , vol.24 , pp. 2682-2697
    • Stavreva, D.A.1    Müller, W.G.2    Hager, G.L.3    Smith, C.L.4    McNally, J.G.5
  • 11
    • 55949117369 scopus 로고    scopus 로고
    • Genome wide transcriptional profiling in breast cancer cells reveals distinct changes in hormone receptor target genes and chromatin modifying enzymes after proteasome inhibition
    • Kinyamu HK, Collins JB, Grissom SF, Hebbar PB, Archer TK 2008 Genome wide transcriptional profiling in breast cancer cells reveals distinct changes in hormone receptor target genes and chromatin modifying enzymes after proteasome inhibition. Mol Carcinog 47: 845-885
    • (2008) Mol Carcinog , vol.47 , pp. 845-885
    • Kinyamu, H.K.1    Collins, J.B.2    Grissom, S.F.3    Hebbar, P.B.4    Archer, T.K.5
  • 12
    • 34347327136 scopus 로고    scopus 로고
    • Proteasome activity modulates chromatin modifications and RNA polymerase II phosphorylation to enhance glucocorticoid receptor-mediated transcription
    • Kinyamu HK, Archer TK 2007 Proteasome activity modulates chromatin modifications and RNA polymerase II phosphorylation to enhance glucocorticoid receptor-mediated transcription. Mol Cell Biol 27: 4891-4904
    • (2007) Mol Cell Biol , vol.27 , pp. 4891-4904
    • Kinyamu, H.K.1    Archer, T.K.2
  • 13
    • 0037135577 scopus 로고    scopus 로고
    • RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding
    • Schulz M, Eggert M, Baniahmad A, Dostert A, Heinzel T, Renkawitz R 2002 RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding. J Biol Chem 277: 26238-26243
    • (2002) J Biol Chem , vol.277 , pp. 26238-26243
    • Schulz, M.1    Eggert, M.2    Baniahmad, A.3    Dostert, A.4    Heinzel, T.5    Renkawitz, R.6
  • 14
    • 0033523917 scopus 로고    scopus 로고
    • The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors
    • Hu X, Lazar MA 1999 The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 402: 93-96
    • (1999) Nature , vol.402 , pp. 93-96
    • Hu, X.1    Lazar, M.A.2
  • 15
    • 0345650665 scopus 로고    scopus 로고
    • Activation functions 1 and 2 of nuclear receptors: Molecular strategies for transcriptional activation
    • Wärnmark A, Treuter E, Wright AP, Gustafsson JA 2003 Activation functions 1 and 2 of nuclear receptors: Molecular strategies for transcriptional activation. Mol Endocrinol 17: 1901-1909
    • (2003) Mol Endocrinol , vol.17 , pp. 1901-1909
    • Wärnmark, A.1    Treuter, E.2    Wright, A.P.3    Gustafsson, J.A.4
  • 17
    • 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
  • 19
    • 5644293177 scopus 로고    scopus 로고
    • Molecular interaction of retinoic acid receptors with coregulators PCAF and RIP140
    • Chen Y, Hu X, Wei LN 2004 Molecular interaction of retinoic acid receptors with coregulators PCAF and RIP140. Mol Cell Endocrinol 226: 43-50
    • (2004) Mol Cell Endocrinol , vol.226 , pp. 43-50
    • Chen, Y.1    Hu, X.2    Wei, L.N.3
  • 20
    • 0033214780 scopus 로고    scopus 로고
    • Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins
    • Hittelman AB, Burakov D, Iñiguez-Lluhí JA, Freedman LP, Garabedian MJ 1999 Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins. EMBO J 18: 5380-5388
    • (1999) EMBO J , vol.18 , pp. 5380-5388
    • Hittelman, A.B.1    Burakov, D.2    Iñiguez-Lluhí, J.A.3    Freedman, L.P.4    Garabedian, M.J.5
  • 21
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery DM, Kalkhoven E, Hoare S, Parker MG 1997 A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387: 733-736
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 23
    • 0032524634 scopus 로고    scopus 로고
    • The steroid receptor coactivator- 1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors
    • Onate SA, Boonyaratanakornkit V, Spencer TE, Tsai SY, Tsai MJ, Edwards DP, O'Malley BW 1998 The steroid receptor coactivator- 1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J Biol Chem 273: 12101-12108
    • (1998) J Biol Chem , vol.273 , pp. 12101-12108
    • Onate, S.A.1    Boonyaratanakornkit, V.2    Spencer, T.E.3    Tsai, S.Y.4    Tsai, M.J.5    Edwards, D.P.6    O'Malley, B.W.7
  • 24
    • 0032784653 scopus 로고    scopus 로고
    • The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription
    • Alen P, Claessens F, Verhoeven G, Rombauts W, Peeters B 1999 The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription. Mol Cell Biol 19: 6085-6097
    • (1999) Mol Cell Biol , vol.19 , pp. 6085-6097
    • Alen, P.1    Claessens, F.2    Verhoeven, G.3    Rombauts, W.4    Peeters, B.5
  • 25
    • 0033512783 scopus 로고    scopus 로고
    • The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1
    • Bevan CL, Hoare S, Claessens F, Heery DM, Parker MG 1999 The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1. Mol Cell Biol 19: 8383-8392
    • (1999) Mol Cell Biol , vol.19 , pp. 8383-8392
    • Bevan, C.L.1    Hoare, S.2    Claessens, F.3    Heery, D.M.4    Parker, M.G.5
  • 28
    • 0034892854 scopus 로고    scopus 로고
    • A TPR motif cofactor contributes to p300 activity in the p53 response
    • Demonacos C, Krstic-Demonacos M, La Thangue NB 2001 A TPR motif cofactor contributes to p300 activity in the p53 response. Mol Cell 8: 71-84
    • (2001) Mol Cell , vol.8 , pp. 71-84
    • Demonacos, C.1    Krstic-Demonacos, M.2    La Thangue, N.B.3
  • 32
    • 0025034814 scopus 로고
    • Snap helix with knob and hole: Essential repeats in S. pombe nuclear protein nuc2+
    • Hirano T, Kinoshita N, Morikawa K, YanagidaM1990 Snap helix with knob and hole: Essential repeats in S. pombe nuclear protein nuc2+. Cell 60: 319-328
    • (1990) Cell , vol.60 , pp. 319-328
    • Hirano, T.1    Kinoshita, N.2    Morikawa, K.3    Yanagida, M.4
  • 33
    • 0025159176 scopus 로고
    • A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
    • Sikorski RS, Boguski MS, Goebl M, Hieter P 1990 A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. Cell 60: 307-317
    • (1990) Cell , vol.60 , pp. 307-317
    • Sikorski, R.S.1    Boguski, M.S.2    Goebl, M.3    Hieter, P.4
  • 34
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch GL, Lässle M 1999 The tetratricopeptide repeat: A structural motif mediating protein-protein interactions. Bioessays 21: 932-939
    • (1999) Bioessays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lässle, M.2
  • 35
    • 3543037605 scopus 로고    scopus 로고
    • Tetratricopeptide repeat cochaperones in steroid receptor complexes
    • Smith DF 2004 Tetratricopeptide repeat cochaperones in steroid receptor complexes. Cell Stress Chaperone 9: 109-121
    • (2004) Cell Stress Chaperone , vol.9 , pp. 109-121
    • Smith, D.F.1
  • 36
    • 46449107665 scopus 로고    scopus 로고
    • A transcription cofactor required for the heat-shock response
    • Xu D, Zalmas LP, La Thangue NB 2008 A transcription cofactor required for the heat-shock response. EMBO Rep 9: 662-669
    • (2008) EMBO Rep , vol.9 , pp. 662-669
    • Xu, D.1    Zalmas, L.P.2    La Thangue, N.B.3
  • 37
    • 33644867538 scopus 로고    scopus 로고
    • The proteasome: A utility tool for transcription?
    • Collins GA, Tansey WP 2006 The proteasome: A utility tool for transcription? Curr Opin Genet Dev 16: 197-202
    • (2006) Curr Opin Genet Dev , vol.16 , pp. 197-202
    • Collins, G.A.1    Tansey, W.P.2
  • 38
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling
    • Reid G, Hübner MR, Métivier R, Brand H, Denger S, Manu D, Beaudouin J, Ellenberg J, Gannon F 2003 Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling. Mol Cell 11: 695-707
    • (2003) Mol Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hübner, M.R.2    Métivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6    Beaudouin, J.7    Ellenberg, J.8    Gannon, F.9
  • 40
    • 33750023437 scopus 로고    scopus 로고
    • Keeping transcriptional activators under control
    • Kodadek T, Sikder D, Nalley K 2006 Keeping transcriptional activators under control. Cell 127: 261-264
    • (2006) Cell , vol.127 , pp. 261-264
    • Kodadek, T.1    Sikder, D.2    Nalley, K.3
  • 42
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domainpeptide complexes: Critical elements in the assembly of the Hsp70- Hsp90 multichaperone machine
    • Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I 2000 Structure of TPR domainpeptide complexes: Critical elements in the assembly of the Hsp70- Hsp90 multichaperone machine. Cell 101: 199-210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 44
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell L, Cook P 1996 Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol Endocrinol 10: 705-712
    • (1996) Mol Endocrinol , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 45
    • 0020701027 scopus 로고
    • DNA damage as a basis for 4'-demethylepipodophyllotoxin- 9-(4,6-O-ethylidene-β-D-glucopyranoside) (etoposide) cytotoxicity
    • Wozniak AJ, Ross WE 1983 DNA damage as a basis for 4'- demethylepipodophyllotoxin- 9-(4,6-O-ethylidene-β-D-glucopyranoside) (etoposide) cytotoxicity. Cancer Res 43: 120-124
    • (1983) Cancer Res , vol.43 , pp. 120-124
    • Wozniak, A.J.1    Ross, W.E.2
  • 46
    • 0032478254 scopus 로고    scopus 로고
    • Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase
    • Rogatsky I, Logan SK, Garabedian MJ 1998 Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase. Proc Natl Acad Sci USA 95: 2050-2055
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2050-2055
    • Rogatsky, I.1    Logan, S.K.2    Garabedian, M.J.3
  • 48
    • 0036794281 scopus 로고    scopus 로고
    • Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation
    • Itoh M, Adachi M, Yasui H, Takekawa M, Tanaka H, Imai K 2002 Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation. Mol Endocrinol 16: 2382-2392
    • (2002) Mol Endocrinol , vol.16 , pp. 2382-2392
    • Itoh, M.1    Adachi, M.2    Yasui, H.3    Takekawa, M.4    Tanaka, H.5    Imai, K.6
  • 49
    • 0030796909 scopus 로고    scopus 로고
    • Induction of interleukin 6 by ionizing radiation in a human epithelial cell line: Control by corticosteroids
    • Beetz A, Messer G, Oppel T, van Beuningen D, Peter RU, Kind P 1997 Induction of interleukin 6 by ionizing radiation in a human epithelial cell line: Control by corticosteroids. Int J Radiat Biol 72: 33-43
    • (1997) Int J Radiat Biol , vol.72 , pp. 33-43
    • Beetz, A.1    Messer, G.2    Oppel, T.3    Van Beuningen, D.4    Peter, R.U.5    Kind, P.6
  • 50
    • 0031054252 scopus 로고    scopus 로고
    • Sequence-specific DNA binding and transcription factor phosphorylation by Ku Autoantigen/DNA-dependent protein kinase. Phosphorylation of Ser-527 of the rat glucocorticoid receptor
    • Giffin W, Kwast-Welfeld J, Rodda DJ, Préfontaine GG, Traykova- Andonova M, Zhang Y, Weigel NL, Lefebvre YA, Haché RJ 1997 Sequence-specific DNA binding and transcription factor phosphorylation by Ku Autoantigen/DNA-dependent protein kinase. Phosphorylation of Ser-527 of the rat glucocorticoid receptor. J Biol Chem 272: 5647-5658
    • (1997) J Biol Chem , vol.272 , pp. 5647-5658
    • Giffin, W.1    Kwast-Welfeld, J.2    Rodda, D.J.3    Préfontaine, G.G.4    Traykova- Andonova, M.5    Zhang, Y.6    Weigel, N.L.7    Lefebvre, Y.A.8    Haché, R.J.9
  • 51
    • 3042795223 scopus 로고    scopus 로고
    • Physiological and pathological consequences of the interactions of the p53 tumor suppressor with the glucocorticoid, androgen, and estrogen receptors
    • Sengupta S, Wasylyk B 2004 Physiological and pathological consequences of the interactions of the p53 tumor suppressor with the glucocorticoid, androgen, and estrogen receptors. AnnNYAcad Sci 1024: 54-71
    • (2004) AnnNYAcad Sci , vol.1024 , pp. 54-71
    • Sengupta, S.1    Wasylyk, B.2
  • 52
    • 0029982833 scopus 로고    scopus 로고
    • Glucocorticoid receptor structure and function in glucocorticoid- resistant small cell lung carcinoma cells
    • Ray DW, Davis JR, White A, Clark AJ 1996 Glucocorticoid receptor structure and function in glucocorticoid-resistant small cell lung carcinoma cells. Cancer Res 56: 3276-3280
    • (1996) Cancer Res , vol.56 , pp. 3276-3280
    • Ray, D.W.1    Davis, J.R.2    White, A.3    Clark, A.J.4
  • 53
    • 33847661809 scopus 로고    scopus 로고
    • Protocol for the fast chromatin immunoprecipitation (ChIP) method
    • Nelson JD, Denisenko O, Bomsztyk K 2006 Protocol for the fast chromatin immunoprecipitation (ChIP) method. Nat Protoc 1: 179-185
    • (2006) Nat Protoc , vol.1 , pp. 179-185
    • Nelson, J.D.1    Denisenko, O.2    Bomsztyk, K.3


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