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Volumn 74, Issue 3, 1999, Pages 458-467

Only a small portion of the cytoplasmic progesterone receptor is associated with Hsp90 in vivo

Author keywords

Hsp90; Progesterone receptor

Indexed keywords

CYTOPLASMIC RECEPTOR; HEAT SHOCK PROTEIN 90; MUTANT PROTEIN; OLIGOMER; PROGESTERONE RECEPTOR; TRANSCRIPTION FACTOR;

EID: 0033198072     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(19990901)74:3<458::AID-JCB13>3.0.CO;2-M     Document Type: Article
Times cited : (5)

References (39)
  • 1
    • 0026511544 scopus 로고
    • Subunit composition of the untransformed glucocorticoid receptor in the cytosol and in the cell
    • Alexis MN, Mavridou I, Mitsiou DJ. 1992. Subunit composition of the untransformed glucocorticoid receptor in the cytosol and in the cell. Eur J Biochem 204:75-84.
    • (1992) Eur J Biochem , vol.204 , pp. 75-84
    • Alexis, M.N.1    Mavridou, I.2    Mitsiou, D.J.3
  • 2
    • 0027288627 scopus 로고
    • The steroid binding domain influences intracellular solubility of the baculovirus over-expressed glucocorticoid and mineralocorticoid receptors
    • Alnemri ES, Litwack G. 1993. The steroid binding domain influences intracellular solubility of the baculovirus over-expressed glucocorticoid and mineralocorticoid receptors. Biochemistry 32:5387-5393.
    • (1993) Biochemistry , vol.32 , pp. 5387-5393
    • Alnemri, E.S.1    Litwack, G.2
  • 3
    • 0024470651 scopus 로고
    • Contragestion and other clinical applications of RU 486, an antiprogesterone at the receptor
    • Baulieu EE. 1989. Contragestion and other clinical applications of RU 486, an antiprogesterone at the receptor. Science 245:1351-1357.
    • (1989) Science , vol.245 , pp. 1351-1357
    • Baulieu, E.E.1
  • 4
    • 0028999582 scopus 로고
    • Hold'em and fold'em: Chaperones and signal transduction
    • Bohen SP, Kralli A, Yamoto KR. 1995. Hold'em and fold'em: Chaperones and signal transduction. Science 268:1303-1304.
    • (1995) Science , vol.268 , pp. 1303-1304
    • Bohen, S.P.1    Kralli, A.2    Yamoto, K.R.3
  • 5
    • 0025128697 scopus 로고
    • Direct stoichiometric evidence that the untransformed Mr 300 000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex
    • Bresnick EH, Dalman FC, Pratt WB. 1990. Direct stoichiometric evidence that the untransformed Mr 300 000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex. Biochemistry 29:520-527.
    • (1990) Biochemistry , vol.29 , pp. 520-527
    • Bresnick, E.H.1    Dalman, F.C.2    Pratt, W.B.3
  • 7
    • 0025251798 scopus 로고
    • Several regions of human estrogen receptor are involved in the formation of receptor-heat shock protein-90 complexes
    • Chambraud B, Berry M, Redeuilh G, Chambon P and Baulieu EE. 1990. Several regions of human estrogen receptor are involved in the formation of receptor-heat shock protein-90 complexes. J Biol Chem 265:20686-20691.
    • (1990) J Biol Chem , vol.265 , pp. 20686-20691
    • Chambraud, B.1    Berry, M.2    Redeuilh, G.3    Chambon, P.4    Baulieu, E.E.5
  • 8
    • 0025260972 scopus 로고
    • In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90
    • Dalman FC, Koenig RJ, Perdew GH, Massa E, Pratt WB. 1990. In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90. J Biol Chem 265:3615-3618.
    • (1990) J Biol Chem , vol.265 , pp. 3615-3618
    • Dalman, F.C.1    Koenig, R.J.2    Perdew, G.H.3    Massa, E.4    Pratt, W.B.5
  • 10
    • 0021235161 scopus 로고
    • Polypeptide components of two 8S forms of chicken oviduct progesterone receptor
    • Dougherty JJ, Puri RK, Toft DO. 1984. Polypeptide components of two 8S forms of chicken oviduct progesterone receptor. J Biol Chem 259:8004-8009.
    • (1984) J Biol Chem , vol.259 , pp. 8004-8009
    • Dougherty, J.J.1    Puri, R.K.2    Toft, D.O.3
  • 11
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman BC, Toft DO, Morimoto RI. 1996. Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274:1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 12
    • 0020110357 scopus 로고
    • Activation, transformation and subunit structure of steroid hormone receptors
    • Grody WW, Schrader WT, O'Malley BW. 1982. Activation, transformation and subunit structure of steroid hormone receptors. Endocr Rev 3:141-162.
    • (1982) Endocr Rev , vol.3 , pp. 141-162
    • Grody, W.W.1    Schrader, W.T.2    O'Malley, B.W.3
  • 13
    • 0029440036 scopus 로고
    • Transcription factors 3: Nuclear receptors
    • New York: Academic Press
    • Gronemeyer H, Laudet V. 1995. Transcription factors 3: Nuclear receptors. Protein profile Volume 2. New York: Academic Press.
    • (1995) Protein Profile , vol.2
    • Gronemeyer, H.1    Laudet, V.2
  • 14
    • 0023186939 scopus 로고
    • Antiglucocorticosteroid effects suggest why steroid hormone is required for receptors to bind DNA in vivo but not in vitro
    • Groyer A, Schweizer-Groyer G, Cadepond F, Mariller M, Baulieu EE. 1987. Antiglucocorticosteroid effects suggest why steroid hormone is required for receptors to bind DNA in vivo but not in vitro. Nature 328:624.
    • (1987) Nature , vol.328 , pp. 624
    • Groyer, A.1    Schweizer-Groyer, G.2    Cadepond, F.3    Mariller, M.4    Baulieu, E.E.5
  • 16
    • 0022368612 scopus 로고
    • Conformational and eletrostatic propereties of unoccupied and liganded estrogen receptors determined by aquous two-phase partitioning
    • Hansen JC, Gorski J. 1985. Conformational and eletrostatic propereties of unoccupied and liganded estrogen receptors determined by aquous two-phase partitioning. Biochemistry 24:6078-6085.
    • (1985) Biochemistry , vol.24 , pp. 6078-6085
    • Hansen, J.C.1    Gorski, J.2
  • 17
    • 0028156864 scopus 로고
    • In vivo functional protein-protein interaction:Nuclear targeted hsp90 shifts sytoplasmic steroid receptor mutants into the nucleus
    • Kang KI, Devin J, Cadepond F, Jibard N, Guichon-Mantel A, Baulieu ET, Catelli AM. 1994. In vivo functional protein-protein interaction:nuclear targeted hsp90 shifts sytoplasmic steroid receptor mutants into the nucleus. Proc Natl Acad Sci USA 91:340-344.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 340-344
    • Kang, K.I.1    Devin, J.2    Cadepond, F.3    Jibard, N.4    Guichon-Mantel, A.5    Baulieu, E.T.6    Catelli, A.M.7
  • 18
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: Estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor
    • Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF. 1996. A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor. Cell Stress Chaperones 1:237-250.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 19
    • 0018855155 scopus 로고
    • Inhibition of progesterone receptor activation by sodium molybdate
    • Nishigori H, Toft D. 1980. Inhibition of progesterone receptor activation by sodium molybdate. Biochemistry 19: 77-83.
    • (1980) Biochemistry , vol.19 , pp. 77-83
    • Nishigori, H.1    Toft, D.2
  • 20
    • 0025915087 scopus 로고
    • Different immunoelectron microscopic locations of progesterone receptor and hsp90 in chick oviduct epithelial cells
    • Pekki AK. 1991. Different immunoelectron microscopic locations of progesterone receptor and hsp90 in chick oviduct epithelial cells. J Histochem Cytochem 39:1095-1101.
    • (1991) J Histochem Cytochem , vol.39 , pp. 1095-1101
    • Pekki, A.K.1
  • 21
    • 0029048456 scopus 로고
    • Progesterone receptor does not form oligomeric (8S), non-DNA-binding complex in intact cell nuclei
    • Pekki A, Ylikomi T, Syvälä H, Tuohimaa P. 1995. Progesterone receptor does not form oligomeric (8S), non-DNA-binding complex in intact cell nuclei. J Cell Biochem 58:1-10.
    • (1995) J Cell Biochem , vol.58 , pp. 1-10
    • Pekki, A.1    Ylikomi, T.2    Syvälä, H.3    Tuohimaa, P.4
  • 22
    • 0022351390 scopus 로고
    • Effects of molybdate on steroid receptors in intact GH1 cells
    • Raaka BM, Finnerty M, Sun E, Samuels HH. 1985. Effects of Molybdate on steroid receptors in intact GH1 cells. J Biol Chem 260:14009-14015.
    • (1985) J Biol Chem , vol.260 , pp. 14009-14015
    • Raaka, B.M.1    Finnerty, M.2    Sun, E.3    Samuels, H.H.4
  • 23
    • 0026343608 scopus 로고
    • Protein components of the nonactivated glucocorticoid receptor
    • Rexin M, Busch W, Gehring U. 1991. Protein components of the nonactivated glucocorticoid receptor. J Biol Chem 266:24601-24605.
    • (1991) J Biol Chem , vol.266 , pp. 24601-24605
    • Rexin, M.1    Busch, W.2    Gehring, U.3
  • 24
    • 0028136758 scopus 로고
    • Oligomeric structures of cytosoluble estrogen-receptor complexes as studied by antiestrogen receptor antibodies and chemical crosslinking of intact cells
    • Rossini GP, Camelli L. 1994. Oligomeric structures of cytosoluble estrogen-receptor complexes as studied by antiestrogen receptor antibodies and chemical crosslinking of intact cells. J Steroid Biochem Mol Biol 50:241-252.
    • (1994) J Steroid Biochem Mol Biol , vol.50 , pp. 241-252
    • Rossini, G.P.1    Camelli, L.2
  • 26
    • 0028911171 scopus 로고
    • Subunit structure of the nonactivated human estrogen receptor
    • Segnitz B, Gehring U. 1995. Subunit structure of the nonactivated human estrogen receptor. Proc Natl Acad Sci USA 92:2179-2183.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2179-2183
    • Segnitz, B.1    Gehring, U.2
  • 27
    • 0025640051 scopus 로고
    • Reconstitution of progesterone receptor with heat shock proteins
    • Smith DF, Schowalter DB, Kost SL, Toft DO. 1990. Reconstitution of progesterone receptor with heat shock proteins. Mol Endocrin 4:1704-1711.
    • (1990) Mol Endocrin , vol.4 , pp. 1704-1711
    • Smith, D.F.1    Schowalter, D.B.2    Kost, S.L.3    Toft, D.O.4
  • 28
    • 0027447541 scopus 로고
    • Steroid receptors and their associated proteins
    • Smith DF, Toft DO. 1993. Steroid receptors and their associated proteins. Mol Endocrinol 7:4-11.
    • (1993) Mol Endocrinol , vol.7 , pp. 4-11
    • Smith, D.F.1    Toft, D.O.2
  • 29
    • 0030054166 scopus 로고    scopus 로고
    • Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90
    • Stancato LF, Hutchison KA, Krishna P, Pratt WB. 1996. Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90. Biochemistry 35:554-461.
    • (1996) Biochemistry , vol.35 , pp. 554-1461
    • Stancato, L.F.1    Hutchison, K.A.2    Krishna, P.3    Pratt, W.B.4
  • 31
    • 0013913886 scopus 로고
    • A receptor molecule for estrogens: Isolation from the rat uterus and preliminary characterization
    • Toft D, Gorski J. 1966. A receptor molecule for estrogens: Isolation from the rat uterus and preliminary characterization. Proc Natl Acad Sci USA 55:1574-1581.
    • (1966) Proc Natl Acad Sci USA , vol.55 , pp. 1574-1581
    • Toft, D.1    Gorski, J.2
  • 33
    • 0024986273 scopus 로고
    • Repression of the alpha fetoprotein gene promoter by progesterone and chimeric receptors in the presence of hormones and anti-hormones
    • Turcotte B, Meyer ME, Bocquel MT, Belanger L, Chambon P. 1990. Repression of the alpha fetoprotein gene promoter by progesterone and chimeric receptors in the presence of hormones and anti-hormones. Mol Cell Biol 10:5002-5006.
    • (1990) Mol Cell Biol , vol.10 , pp. 5002-5006
    • Turcotte, B.1    Meyer, M.E.2    Bocquel, M.T.3    Belanger, L.4    Chambon, P.5
  • 34
    • 0029123088 scopus 로고
    • A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation
    • Whitfield GK, Hsieh JC, Nakajima S, MacDonald PN, Thompson PD, Jurutka PW, Haussler CA, Haussler MR. 1995. A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation. Mol Endocrinol 9:1166-1179.
    • (1995) Mol Endocrinol , vol.9 , pp. 1166-1179
    • Whitfield, G.K.1    Hsieh, J.C.2    Nakajima, S.3    Macdonald, P.N.4    Thompson, P.D.5    Jurutka, P.W.6    Haussler, C.A.7    Haussler, M.R.8
  • 35
    • 0023146969 scopus 로고
    • Intracellular localization of the glucocorticoid receptor evidence for cytoplasmic and nuclear localization
    • Wikstöm AC, Bakke O, Okret S, Brönnegård M, Gustafsson JÅ. 1987. Intracellular localization of the glucocorticoid receptor evidence for cytoplasmic and nuclear localization. Endocrinology 120:1232-1242.
    • (1987) Endocrinology , vol.120 , pp. 1232-1242
    • Wikstöm, A.C.1    Bakke, O.2    Okret, S.3    Brönnegård, M.4    Jå, G.5
  • 37
    • 0030046766 scopus 로고    scopus 로고
    • Assessment of glucocorticoid receptor-heat shock protein90 interactions in vivo during nucleocytoplasmic trafficking
    • Yang J, Defranco DB. 1996. Assessment of glucocorticoid receptor-heat shock protein90 interactions in vivo during nucleocytoplasmic trafficking. Mol Endocrin 10:3-13.
    • (1996) Mol Endocrin , vol.10 , pp. 3-13
    • Yang, J.1    Defranco, D.B.2
  • 38
    • 0026713869 scopus 로고
    • Cooperation of protosignals for nuclear accumulation of estrogen and progesterone receptors
    • Ylikomi T, Bocquel MT, Berry M, Gronemeyer H, Chambon P. 1992. Cooperation of protosignals for nuclear accumulation of estrogen and progesterone receptors. EMBO J 11:3681-3694.
    • (1992) EMBO J , vol.11 , pp. 3681-3694
    • Ylikomi, T.1    Bocquel, M.T.2    Berry, M.3    Gronemeyer, H.4    Chambon, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.