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Volumn 21, Issue 10, 2007, Pages 2427-2439

Glycogen synthase kinase-3 protects estrogen receptor α from proteasomal degradation and is required for full transcriptional activity of the receptor

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXIMIDE; ESTROGEN RECEPTOR ALPHA; GLYCOGEN SYNTHASE KINASE 3; PROTEASOME;

EID: 34948886577     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2007-0129     Document Type: Article
Times cited : (52)

References (44)
  • 1
    • 0030728930 scopus 로고    scopus 로고
    • Tissue distribution and quantitative analysis of estrogen receptor α and estrogen receptor β messenger ribonucleic acid in the wild-type and ERα-knockout mouse
    • Couse JF, Lindzey J, Grandien K, Gustafsson JA, Korach KS 1997 Tissue distribution and quantitative analysis of estrogen receptor α and estrogen receptor β messenger ribonucleic acid in the wild-type and ERα-knockout mouse. Endocrinology 138:4613-4621
    • (1997) Endocrinology , vol.138 , pp. 4613-4621
    • Couse, J.F.1    Lindzey, J.2    Grandien, K.3    Gustafsson, J.A.4    Korach, K.S.5
  • 2
    • 0035813112 scopus 로고    scopus 로고
    • The multifaceted mechanisms of estradiol and estrogen receptor signalling
    • Hall JM, Couse JF, Korach KS 2001 The multifaceted mechanisms of estradiol and estrogen receptor signalling. J Biol Chem 276:36869-36872
    • (2001) J Biol Chem , vol.276 , pp. 36869-36872
    • Hall, J.M.1    Couse, J.F.2    Korach, K.S.3
  • 3
    • 0033305438 scopus 로고    scopus 로고
    • Estrogen receptor null mice: What have we learned and where will they lead us?
    • Couse JF, Korach KS 1999 Estrogen receptor null mice: what have we learned and where will they lead us? Endocr Rev 20:358-417
    • (1999) Endocr Rev , vol.20 , pp. 358-417
    • Couse, J.F.1    Korach, K.S.2
  • 5
    • 0034468021 scopus 로고    scopus 로고
    • Estrogen receptor transcription and transactivation. Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors
    • Ruff M, Gangloff M, Wurtz JM, Moras D 2000 Estrogen receptor transcription and transactivation. Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors. Breast Cancer Res 2:353-359
    • (2000) Breast Cancer Res , vol.2 , pp. 353-359
    • Ruff, M.1    Gangloff, M.2    Wurtz, J.M.3    Moras, D.4
  • 6
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • Tora L, White JH, Brou C, Tasset DM, Webster NJG, Scheer E, Chambon P 1989 The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 59:477-487
    • (1989) Cell , vol.59 , pp. 477-487
    • Tora, L.1    White, J.H.2    Brou, C.3    Tasset, D.M.4    Webster, N.J.G.5    Scheer, E.6    Chambon, P.7
  • 7
    • 84995870933 scopus 로고
    • Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions
    • Tzukerman MT, Esty A, Santiso-Mere D, Danielan P, Parker MG, Stein RB, Pike JW, McDonnell DP 1994 Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol Endocrinol 8:21-30
    • (1994) Mol Endocrinol , vol.8 , pp. 21-30
    • Tzukerman, M.T.1    Esty, A.2    Santiso-Mere, D.3    Danielan, P.4    Parker, M.G.5    Stein, R.B.6    Pike, J.W.7    McDonnell, D.P.8
  • 9
    • 33751552134 scopus 로고    scopus 로고
    • Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, DNA, and coregulators associated with alterations in estrogen and tamoxifen activity
    • Likhite VS, Stossi F, Kim K, Katzenellenbogen BS, Katzenellenbogen JA 2006 Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, DNA, and coregulators associated with alterations in estrogen and tamoxifen activity. Mol Endocrinol 20:3120-3132
    • (2006) Mol Endocrinol , vol.20 , pp. 3120-3132
    • Likhite, V.S.1    Stossi, F.2    Kim, K.3    Katzenellenbogen, B.S.4    Katzenellenbogen, J.A.5
  • 10
    • 0028111526 scopus 로고
    • Phosphorylation of the human estrogen receptor: Identification of hormone-regulated sites and examination of their influence on transcriptional activity
    • Le Goff P, Montano MM, Schodin DJ, Katzenellenbogen BS 1994 Phosphorylation of the human estrogen receptor: identification of hormone-regulated sites and examination of their influence on transcriptional activity. J Biol Chem 269:4458-4466
    • (1994) J Biol Chem , vol.269 , pp. 4458-4466
    • Le Goff, P.1    Montano, M.M.2    Schodin, D.J.3    Katzenellenbogen, B.S.4
  • 11
    • 0037211754 scopus 로고    scopus 로고
    • Estrogen receptor phosphorylation
    • Lannigan DA 2003 Estrogen receptor phosphorylation. Steroids 68:1-9
    • (2003) Steroids , vol.68 , pp. 1-9
    • Lannigan, D.A.1
  • 12
    • 25444468111 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 interacts with and phosphorylates estrogen receptor α and is involved in the regulation of receptor activity
    • Medunjanin S, Hermani A, De Servi B, Grisouard J, Rincke G, Mayer D 2005 Glycogen synthase kinase-3 interacts with and phosphorylates estrogen receptor α and is involved in the regulation of receptor activity. J Biol Chem 280:33006-33014
    • (2005) J Biol Chem , vol.280 , pp. 33006-33014
    • Medunjanin, S.1    Hermani, A.2    De Servi, B.3    Grisouard, J.4    Rincke, G.5    Mayer, D.6
  • 13
    • 0033529557 scopus 로고    scopus 로고
    • Potentiation of human estrogen receptor α transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex
    • Rogatsky I, Towbridge JM, Garabedian MJ 1999 Potentiation of human estrogen receptor α transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex. J Biol Chem 274:22296-22302
    • (1999) J Biol Chem , vol.274 , pp. 22296-22302
    • Rogatsky, I.1    Towbridge, J.M.2    Garabedian, M.J.3
  • 14
    • 0033636597 scopus 로고    scopus 로고
    • Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7
    • Chen D, Riedl T, Washbrook E, Pace PE, Coombes RC, Egly JM, Ali S 2000 Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7. Mol Cell 6:127-137
    • (2000) Mol Cell , vol.6 , pp. 127-137
    • Chen, D.1    Riedl, T.2    Washbrook, E.3    Pace, P.E.4    Coombes, R.C.5    Egly, J.M.6    Ali, S.7
  • 15
    • 0032557452 scopus 로고    scopus 로고
    • Estradiol-induced phosphorylation of serine 118 in the estrogen receptor is independent of p42/p44 mitogen-activated protein kinase
    • Joel PB, Traish AM, Lannigan DA 1998 Estradiol-induced phosphorylation of serine 118 in the estrogen receptor is independent of p42/p44 mitogen-activated protein kinase. J Biol Chem 273:13317-13323
    • (1998) J Biol Chem , vol.273 , pp. 13317-13323
    • Joel, P.B.1    Traish, A.M.2    Lannigan, D.A.3
  • 16
    • 0029163578 scopus 로고
    • Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor
    • Joel PB, Traish AM, Lannigan DA 1995 Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Mol Endocrinol 9:1041-1052
    • (1995) Mol Endocrinol , vol.9 , pp. 1041-1052
    • Joel, P.B.1    Traish, A.M.2    Lannigan, D.A.3
  • 17
    • 46649091672 scopus 로고    scopus 로고
    • The cell-specific activity of the estrogen receptor α may be fine-tuned by phosphorylation-induced structural gymnastics
    • Gburcik V, Picard D 2006 The cell-specific activity of the estrogen receptor α may be fine-tuned by phosphorylation-induced structural gymnastics. Nucl Recept Signal 4:1-4
    • (2006) Nucl Recept Signal , vol.4 , pp. 1-4
    • Gburcik, V.1    Picard, D.2
  • 18
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factor A
    • Woodgett JR 1990 Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J 9:2431-2438
    • (1990) EMBO J , vol.9 , pp. 2431-2438
    • Woodgett, J.R.1
  • 19
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation
    • Hoeflich KP, Luo J, Rubie EA, Tsao MS, Jin O, Woodgett JR 2000 Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation. Nature 406:86-90
    • (2000) Nature , vol.406 , pp. 86-90
    • Hoeflich, K.P.1    Luo, J.2    Rubie, E.A.3    Tsao, M.S.4    Jin, O.5    Woodgett, J.R.6
  • 20
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase-3β in cellular signalling
    • Grimes CA, Jope RS 2001 The multifaceted roles of glycogen synthase kinase-3β in cellular signalling. Prog Neurobiol 65:391-426
    • (2001) Prog Neurobiol , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 21
    • 0442276554 scopus 로고    scopus 로고
    • The glamour and gloom of glycogen synthase kinase-3
    • Jope RS, Johnson GVW 2004 The glamour and gloom of glycogen synthase kinase-3. Trends Biochem Sci 29:95-102
    • (2004) Trends Biochem Sci , vol.29 , pp. 95-102
    • Jope, R.S.1    Johnson, G.V.W.2
  • 22
    • 1642375658 scopus 로고    scopus 로고
    • Estradiol inhibits GSK-3 and regulates interaction of estrogen receptors, and β-catenin in the hippocampus
    • Cardonna-Gomez P, Perez M, Avila J, Garcia-Segura LM, Wandosell F 2004 Estradiol inhibits GSK-3 and regulates interaction of estrogen receptors, and β-catenin in the hippocampus. Mol Cell Neurosci 25:363-373
    • (2004) Mol Cell Neurosci , vol.25 , pp. 363-373
    • Cardonna-Gomez, P.1    Perez, M.2    Avila, J.3    Garcia-Segura, L.M.4    Wandosell, F.5
  • 23
    • 33646791491 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and glycogen synthase kinase 3 regulate estrogen receptor-mediated transcription in neuronal cells
    • Mendez P, Garcia-Segura LM 2006 Phosphatidylinositol 3-kinase and glycogen synthase kinase 3 regulate estrogen receptor-mediated transcription in neuronal cells. Endocrinology 147:3027-3039
    • (2006) Endocrinology , vol.147 , pp. 3027-3039
    • Mendez, P.1    Garcia-Segura, L.M.2
  • 24
    • 23744476859 scopus 로고    scopus 로고
    • Impact of PKCδ on estrogen receptor localisation and activity in breast cancer cells
    • De Servi B, Hermani A, Medunjanin S, Mayer D 2005 Impact of PKCδ on estrogen receptor localisation and activity in breast cancer cells. Oncogene 24:4946-4955
    • (2005) Oncogene , vol.24 , pp. 4946-4955
    • De Servi, B.1    Hermani, A.2    Medunjanin, S.3    Mayer, D.4
  • 27
    • 0024549892 scopus 로고
    • Regulation of estrogen receptor messenger ribonucleic acid and protein levels in human breast cancer cell lines by sex steroid hormones, their antagonists, and growth factors
    • Read LD, Greene GL, Katzenellenbogen BS 1989 Regulation of estrogen receptor messenger ribonucleic acid and protein levels in human breast cancer cell lines by sex steroid hormones, their antagonists, and growth factors. Mol Endocrinol 3:295-304
    • (1989) Mol Endocrinol , vol.3 , pp. 295-304
    • Read, L.D.1    Greene, G.L.2    Katzenellenbogen, B.S.3
  • 28
    • 0029883292 scopus 로고    scopus 로고
    • Models of estrogen receptor regulation by estrogens and antiestrogens in breast cancer cell lines
    • Pink JJ, Jordan CV 1996 Models of estrogen receptor regulation by estrogens and antiestrogens in breast cancer cell lines. Cancer Res 56:2321-2330
    • (1996) Cancer Res , vol.56 , pp. 2321-2330
    • Pink, J.J.1    Jordan, C.V.2
  • 29
    • 0025133474 scopus 로고
    • Expression of estrogen receptor and its messenger ribonucleic acid in the MCF-7 cell line: Multiparametric analysis of its processing and regulation by estrogen
    • Berthois Y, Dong XF, Roux-Dossetto M, Martin PM 1990 Expression of estrogen receptor and its messenger ribonucleic acid in the MCF-7 cell line: multiparametric analysis of its processing and regulation by estrogen. Mol Cell Endocrinol 74:11-20
    • (1990) Mol Cell Endocrinol , vol.74 , pp. 11-20
    • Berthois, Y.1    Dong, X.F.2    Roux-Dossetto, M.3    Martin, P.M.4
  • 31
    • 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
  • 33
    • 0018254898 scopus 로고
    • Nuclear mechanisms of estrogen action
    • Horwitz KB, McGuire WL 1978 Nuclear mechanisms of estrogen action. J Biol Chem 253:8185-8191
    • (1978) J Biol Chem , vol.253 , pp. 8185-8191
    • Horwitz, K.B.1    McGuire, W.L.2
  • 34
    • 0035878743 scopus 로고    scopus 로고
    • Estrogen receptor interaction with estrogen response elements
    • Klinge CM 2001 Estrogen receptor interaction with estrogen response elements. Nucleic Acids Res 29:2905-2919
    • (2001) Nucleic Acids Res , vol.29 , pp. 2905-2919
    • Klinge, C.M.1
  • 35
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • Phiel CJ, Wilson CA, Lee VMY, Klein PS 2003 GSK-3α regulates production of Alzheimer's disease amyloid-β peptides. Nature 423:435-439
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.Y.3    Klein, P.S.4
  • 36
    • 34948895733 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded estrogen receptor α 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 estrogen receptor α on responsive promoters is an integral feature of estrogen signaling. Mol Cell 23:4813-4823
    • (2003) Mol Cell , vol.23 , pp. 4813-4823
    • 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
  • 37
    • 0027185315 scopus 로고
    • Involvement of the coding sequence for the estrogen receptor gene in autologous ligand-dependent down-regulation
    • Kaneko KJ, Furlow JD, Gorski J 1993 Involvement of the coding sequence for the estrogen receptor gene in autologous ligand-dependent down-regulation. Mol Endocrinol 7:879-888
    • (1993) Mol Endocrinol , vol.7 , pp. 879-888
    • Kaneko, K.J.1    Furlow, J.D.2    Gorski, J.3
  • 38
    • 0032839041 scopus 로고    scopus 로고
    • Ligand structure influences autologous downregulation of estrogen receptor-α messenger RNA
    • Davis MD, Vanderkuur JA, Brooks SC 1999 Ligand structure influences autologous downregulation of estrogen receptor-α messenger RNA. J Steroid Biochem Mol Biol 70:27-37
    • (1999) J Steroid Biochem Mol Biol , vol.70 , pp. 27-37
    • Davis, M.D.1    Vanderkuur, J.A.2    Brooks, S.C.3
  • 39
    • 0035477020 scopus 로고    scopus 로고
    • GSK-3 takes centre stage more than 20 years after its discovery
    • Frame S, Cohen P 2001 GSK-3 takes centre stage more than 20 years after its discovery. Biochem J 359:1-16
    • (2001) Biochem J , vol.359 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 40
    • 0033574527 scopus 로고    scopus 로고
    • Phosphorylation of axin, a Wnt signal negative regulator, by glycogen synthase kinase-3β regulates its stability
    • Yamamoto H, Kishida S, Kishida M, Ikeda S, Takada S, Kikuchi A 1999 Phosphorylation of axin, a Wnt signal negative regulator, by glycogen synthase kinase-3β regulates its stability. J Biol Chem 274:10681-10684
    • (1999) J Biol Chem , vol.274 , pp. 10681-10684
    • Yamamoto, H.1    Kishida, S.2    Kishida, M.3    Ikeda, S.4    Takada, S.5    Kikuchi, A.6
  • 41
    • 20844453021 scopus 로고    scopus 로고
    • Differential regulation of estrogen-inducible proteolysis and transcription by the estrogen receptor α N terminus
    • Valley CC, Métivier R, Solodin NM, Fowler AM, Mashek MT, Hill L, Alarid ET 2005 Differential regulation of estrogen-inducible proteolysis and transcription by the estrogen receptor α N terminus. Mol Cell Biol 13:5417-5428
    • (2005) Mol Cell Biol , vol.13 , pp. 5417-5428
    • Valley, C.C.1    Métivier, R.2    Solodin, N.M.3    Fowler, A.M.4    Mashek, M.T.5    Hill, L.6    Alarid, E.T.7
  • 42
    • 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
  • 43
    • 0031947016 scopus 로고    scopus 로고
    • Dehydroepiandrosterone sulfate estrogenic action at its physiological plasma concentration in human breast cancer cell lines
    • Le Bail JC, Allen K, Nicolas JC, Habrioux G 1998 Dehydroepiandrosterone sulfate estrogenic action at its physiological plasma concentration in human breast cancer cell lines. Anticancer Res 18:1683-1688
    • (1998) Anticancer Res , vol.18 , pp. 1683-1688
    • Le Bail, J.C.1    Allen, K.2    Nicolas, J.C.3    Habrioux, G.4
  • 44
    • 0027171531 scopus 로고
    • Immediate and transient stimulation of protein tyrosine phosphorylation by estradiol in MCF-7 cells
    • Migliaccio A, Pagano M, Auricchio F 1993 Immediate and transient stimulation of protein tyrosine phosphorylation by estradiol in MCF-7 cells. Oncogene 8:2183-2191
    • (1993) Oncogene , vol.8 , pp. 2183-2191
    • Migliaccio, A.1    Pagano, M.2    Auricchio, F.3


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