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Volumn 146, Issue 5, 1999, Pages 929-940

A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity

Author keywords

BAG 1 isoforms; Cochaperone; Glucocorticoid receptor; Mineralocorticoid receptor; Transactivation

Indexed keywords

CHAPERONE; GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN 70; MINERALOCORTICOID RECEPTOR;

EID: 0344200100     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.146.5.929     Document Type: Article
Times cited : (85)

References (49)
  • 1
    • 0002339560 scopus 로고
    • Aldosterone action: Perspectives from the cloning of the mineralocorticoid receptor
    • J.P. Bonvalet. N. Farmann, M. Lombès, and M.-E. Rafestin-Oblin, editors. John Libbey Eurotext Ltd., Paris.
    • Arriza, J.L. 1991. Aldosterone action: perspectives from the cloning of the mineralocorticoid receptor. In Aldosterone. Fundamental Aspects. J.P. Bonvalet. N. Farmann, M. Lombès, and M.-E. Rafestin-Oblin, editors. John Libbey Eurotext Ltd., Paris. 13-21.
    • (1991) Aldosterone. Fundamental Aspects , pp. 13-21
    • Arriza, J.L.1
  • 2
    • 0023221667 scopus 로고
    • Cloning of human mineralocorticoid receptor complementary DNA: Structural and functional kinship with the glucocorticoid receptor
    • Arriza, J.L., C. Weinherger, G. Cerelli, T.M. Glaser, B.L. Hendelin, D.E. Housmann, and R.M. Evans. 1987. Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor. Science. 237:268-273.
    • (1987) Science , vol.237 , pp. 268-273
    • Arriza, J.L.1    Weinherger, C.2    Cerelli, G.3    Glaser, T.M.4    Hendelin, B.L.5    Housmann, D.E.6    Evans, R.M.7
  • 4
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • Beato, M., P. Herrlich, and G. Schütz. 1995. Steroid hormone receptors: many actors in search of a plot. Cell. 83:851-857.
    • (1995) Cell , vol.83 , pp. 851-857
    • Beato, M.1    Herrlich, P.2    Schütz, G.3
  • 6
    • 0032489016 scopus 로고    scopus 로고
    • The hsp70 and hsp60 chaperone machines
    • Bukau, B., and A.L. Horwich. 1998. The hsp70 and hsp60 chaperone machines. Cell. 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 8
    • 0029899120 scopus 로고    scopus 로고
    • Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the RAN/TC4 GTPase mediates an essential function independent of nuclear protein import
    • Carey, K.L., S.A. Richards, K.M. Lounsbury, and I.G. Macara. 1996. Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the RAN/TC4 GTPase mediates an essential function independent of nuclear protein import. J. Cell Biol. 133:985-996.
    • (1996) J. Cell Biol. , vol.133 , pp. 985-996
    • Carey, K.L.1    Richards, S.A.2    Lounsbury, K.M.3    Macara, I.G.4
  • 9
    • 0030138947 scopus 로고    scopus 로고
    • Molecular mechanisms of anti-inflammatory action of glucocorticoids
    • Cato, A.C.B., and E. Wade. 1996. Molecular mechanisms of anti-inflammatory action of glucocorticoids. BioEssays. 18:371-378.
    • (1996) BioEssays , vol.18 , pp. 371-378
    • Cato, A.C.B.1    Wade, E.2
  • 12
    • 0027743317 scopus 로고
    • Heat shock protein 70 is associated in substoichiometric amounts with the rat hepatic glucocorticoid receptor
    • Diehl, E.E., and T.J. Schmidt. 1993. Heat shock protein 70 is associated in substoichiometric amounts with the rat hepatic glucocorticoid receptor. Biochemistry. 32:13510-13515.
    • (1993) Biochemistry , vol.32 , pp. 13510-13515
    • Diehl, E.E.1    Schmidt, T.J.2
  • 13
    • 0030989277 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery
    • Dittmar, K.D., and W.B. Pratt. 1997. Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery. J. Biol. Chem. 272: 13047-13054.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13047-13054
    • Dittmar, K.D.1    Pratt, W.B.2
  • 14
    • 0032571320 scopus 로고    scopus 로고
    • The role of Dna-J-like proteins in glucocorticoid receptor-hsp90 heterocomplex assembly by the reconstituted hsp90.P60.Hsp70 foldosome complex
    • Dittmar, K.D., M. Banach, M.D. Galigniana, and W.B. Pratt. 1998. The role of Dna-J-like proteins in glucocorticoid receptor-hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex. J. Biol. Chem. 273:7358-7366.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7358-7366
    • Dittmar, K.D.1    Banach, M.2    Galigniana, M.D.3    Pratt, W.B.4
  • 15
    • 0032539721 scopus 로고    scopus 로고
    • Subcellular localization of mineralocorticoid receptor in living cells: Effects of receptor agonists and antagonists
    • Fejes-Tóth, G., D. Pearce, and A. Náray-Fejes-Tóth. 1998. Subcellular localization of mineralocorticoid receptor in living cells: effects of receptor agonists and antagonists. Proc. Natl. Acad. Sci. USA. 95:2973-2978.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2973-2978
    • Fejes-Tóth, G.1    Pearce, D.2    Náray-Fejes-Tóth, A.3
  • 16
    • 0032496242 scopus 로고    scopus 로고
    • BAG-1L protein enhances androgen receptor function
    • Froesch, B.A., S. Takayama, and J.C. Reed. 1998. BAG-1L protein enhances androgen receptor function. J. Biol. Chem. 273:11660-11666.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11660-11666
    • Froesch, B.A.1    Takayama, S.2    Reed, J.C.3
  • 17
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The hip-hop connection
    • Frydman, J., and J. Höhfeld. 1997. Chaperones get in touch: the hip-hop connection. Trends Biochem. Sci. 22:87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Höhfeld, J.2
  • 18
    • 0029025826 scopus 로고
    • A single amino acid exchange abolishes dimerization of androgen receptor and causes Reifenstein syndrome
    • Gast, A., F. Neuschmid-Kaspar, H. Klocker, and A.C.B. Cato. 1995. A single amino acid exchange abolishes dimerization of androgen receptor and causes Reifenstein syndrome. Mol. Cell. Endocrinol. 111:93-98.
    • (1995) Mol. Cell. Endocrinol. , vol.111 , pp. 93-98
    • Gast, A.1    Neuschmid-Kaspar, F.2    Klocker, H.3    Cato, A.C.B.4
  • 19
    • 0030671388 scopus 로고    scopus 로고
    • Proteins interacting with the molecular chaperone hsp70/hsc70: Physical associations and effects on refolding activity
    • Gebauer, M., M. Zeiner, and U. Gehring. 1997. Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity. FEBS Lett. 417:109-113.
    • (1997) FEBS Lett. , vol.417 , pp. 109-113
    • Gebauer, M.1    Zeiner, M.2    Gehring, U.3
  • 20
    • 0031770820 scopus 로고    scopus 로고
    • Interference between proteins Hap46 and Hop/p60, which bind to different domains of the molecular chaperone hsp70/hsc70
    • Gebauer, M., M. Zeiner, and U. Gehring. 1998. Interference between proteins Hap46 and Hop/p60, which bind to different domains of the molecular chaperone hsp70/hsc70. Mol. Cell. Biol. 18:6238-6244.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6238-6244
    • Gebauer, M.1    Zeiner, M.2    Gehring, U.3
  • 21
    • 0022453518 scopus 로고
    • Functional domains of the human glucocorticoid receptor
    • Giguère, V., S.M. Hollenberg, M.G. Rosenfeld, and R.M. Evans. 1986. Functional domains of the human glucocorticoid receptor. Cell. 46:645-652.
    • (1986) Cell , vol.46 , pp. 645-652
    • Giguère, V.1    Hollenberg, S.M.2    Rosenfeld, M.G.3    Evans, R.M.4
  • 22
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. 1996. Molecular chaperones in cellular protein folding. Nature. 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 23
  • 25
    • 0028200803 scopus 로고
    • Isolation of a mouse Golgi mannosidase cDNA, member of a gene family conserved from yeast to mammals
    • Herscovics, A., J. Schneikert, A. Athanassiadis, and K. Moremen. 1994. Isolation of a mouse Golgi mannosidase cDNA, member of a gene family conserved from yeast to mammals. J. Biol. Chem. 269:9864-9871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9864-9871
    • Herscovics, A.1    Schneikert, J.2    Athanassiadis, A.3    Moremen, K.4
  • 26
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Höhfeld, J., and S. Jentsch. 1997. GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO (Eur. Mol. Biol. Organ.) J. 16: 6209-6216.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 6209-6216
    • Höhfeld, J.1    Jentsch, S.2
  • 27
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle
    • Höhfeld, J., Y. Minami, and F.-U. Hartl. 1995. Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle. Cell. 83:589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    Hartl, F.-U.3
  • 28
    • 0023649571 scopus 로고
    • Colocalization of DNA-binding and transactivation functions in the human glucocorticoid receptor
    • Hollenberg, S.M., V. Giguère, P. Segui, and R.M. Evans. 1987. Colocalization of DNA-binding and transactivation functions in the human glucocorticoid receptor. Cell. 49:39-46.
    • (1987) Cell , vol.49 , pp. 39-46
    • Hollenberg, S.M.1    Giguère, V.2    Segui, P.3    Evans, R.M.4
  • 29
    • 0027969323 scopus 로고
    • Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90.1
    • Hutchison, K.A., K.D. Dittmar, M.J. Czar, and W.B. Pratt. 1994. Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90.1. Biol. Chem. 269:5043-5049.
    • (1994) Biol. Chem. , vol.269 , pp. 5043-5049
    • Hutchison, K.A.1    Dittmar, K.D.2    Czar, M.J.3    Pratt, W.B.4
  • 30
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates hsp70/hsp90 interactions in protein folding
    • Johnson, B.D., R.J. Schumacher, E.D. Ross, and D.O. Toft. 1998. Hop modulates hsp70/hsp90 interactions in protein folding. J. Biol. Chem. 273:3679-3686.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3679-3686
    • Johnson, B.D.1    Schumacher, R.J.2    Ross, E.D.3    Toft, D.O.4
  • 31
    • 0027363415 scopus 로고
    • A mutant androgen receptor from patients with reifenstein syndrome: Identification of the function of a conserved alanine residue in the D box of steroid receptors
    • Kaspar, F., H. Klocker, A. Denninger, and A.C.B. Cato. 1993. A mutant androgen receptor from patients with Reifenstein syndrome: identification of the function of a conserved alanine residue in the D box of steroid receptors. Mol Cell. Biol. 13:7850-7858.
    • (1993) Mol Cell. Biol. , vol.13 , pp. 7850-7858
    • Kaspar, F.1    Klocker, H.2    Denninger, A.3    Cato, A.C.B.4
  • 32
    • 0026643338 scopus 로고
    • Point mutation in the DNA binding domain of the androgen receptor in two families with reifenstein syndrome
    • Klocker, H., F. Kaspar, J. Eberle, S. Überreiter, C. Radmayr, and G. Bartsch. 1992. Point mutation in the DNA binding domain of the androgen receptor in two families with Reifenstein syndrome. Am. J. Hum. Genet. 50:1318-1327.
    • (1992) Am. J. Hum. Genet , vol.50 , pp. 1318-1327
    • Klocker, H.1    Kaspar, F.2    Eberle, J.3    Überreiter, S.4    Radmayr, C.5    Bartsch, G.6
  • 33
    • 0032486380 scopus 로고    scopus 로고
    • RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis
    • Kullmann, M., J. Schneikert, J. Moll, S. Heck, M. Zeiner, U. Gehring, and A.C.B. Cato. 1998. RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis. J. Biol. Chem. 273:14620-14625.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14620-14625
    • Kullmann, M.1    Schneikert, J.2    Moll, J.3    Heck, S.4    Zeiner, M.5    Gehring, U.6    Cato, A.C.B.7
  • 34
    • 0032479430 scopus 로고    scopus 로고
    • Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells
    • Liu, R., S. Takayama, Y. Zheng, B. Froesch, G.-Q Chen, X. Xhang, J.C. Reed, and X.-K. Zhang. 1998. Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells. J. Biol. Chem. 273:16985-16992.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16985-16992
    • Liu, R.1    Takayama, S.2    Zheng, Y.3    Froesch, B.4    Chen, G.-Q.5    Xhang, X.6    Reed, J.C.7    Zhang, X.-K.8
  • 35
    • 0031081426 scopus 로고    scopus 로고
    • Mechanism of gene expression by the glucocorticoid receptor: Role of protein-protein interactions
    • McEwan, J.I., A.P.H. Wright, and J.-Å. Gustafsson. 1997. Mechanism of gene expression by the glucocorticoid receptor: role of protein-protein interactions. BioEssays. 19:153-160.
    • (1997) BioEssays , vol.19 , pp. 153-160
    • McEwan, J.I.1    Wright, A.P.H.2    Gustafsson, J.-Å.3
  • 36
    • 0031466639 scopus 로고    scopus 로고
    • Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation
    • Packham, G., M. Brimmell, and J.L. Cleveland. 1997. Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation. Biochem. J. 328:807-813.
    • (1997) Biochem. J. , vol.328 , pp. 807-813
    • Packham, G.1    Brimmell, M.2    Cleveland, J.L.3
  • 37
    • 0031871101 scopus 로고    scopus 로고
    • Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor-hsp90 heterocomplex assembly
    • Pratt, W.B., and K.D. Dittmar. 1998. Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor-hsp90 heterocomplex assembly. Trends Endocrinol. Metab. 5:244-252.
    • (1998) Trends Endocrinol. Metab. , vol.5 , pp. 244-252
    • Pratt, W.B.1    Dittmar, K.D.2
  • 38
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
    • Rassow, J., O. von Ahsen, U. Borner, and N. Pfanner. 1997. Molecular chaperones: towards a characterization of the heat-shock protein 70 family. Trends Cell Biol. 7:129-133.
    • (1997) Trends Cell Biol. , vol.7 , pp. 129-133
    • Rassow, J.1    Von Ahsen, O.2    Borner, U.3    Pfanner, N.4
  • 39
    • 0029793329 scopus 로고    scopus 로고
    • Androgen receptor-Ets protein interaction is a novel mechanism for steroid hormone-mediated down-regulation of matrix metalloproteinase expression
    • Schneikert, J., H. Peterziel, P.-A. Defossez, H. Klocker, Y. de Launoit, and A.C.B. Cato. 1996. Androgen receptor-Ets protein interaction is a novel mechanism for steroid hormone-mediated down-regulation of matrix metalloproteinase expression. J. Biol. Chem. 271:23907-23913.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23907-23913
    • Schneikert, J.1    Peterziel, H.2    Defossez, P.-A.3    Klocker, H.4    De Launoit, Y.5    Cato, A.C.B.6
  • 40
    • 0027957428 scopus 로고
    • Heat shock protein is tightly associated with the recombinant human glucocorticoid receptor: Glucocorticoid response element complex
    • Srinivasan, G., N.T. Patel, E.B. Thompson. 1994. Heat shock protein is tightly associated with the recombinant human glucocorticoid receptor: glucocorticoid response element complex. Mol. Endocrinol. 8:189-196.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 189-196
    • Srinivasan, G.1    Patel, N.T.2    Thompson, E.B.3
  • 42
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity
    • Takayama, S., T. Sato, S. Krajewski, K. Kochel, S. Irie, J.A. Millan, and J.C. Reed. 1995. Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity. Cell. 80:279-284.
    • (1995) Cell. , vol.80 , pp. 279-284
    • Takayama, S.1    Sato, T.2    Krajewski, S.3    Kochel, K.4    Irie, S.5    Millan, J.A.6    Reed, J.C.7
  • 45
    • 0029937303 scopus 로고    scopus 로고
    • Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1
    • Wang, H.-G., S. Takayama, U.R. Rapp, and J.C. Reed. 1996. Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1. Proc. Natl. Acad. Sci. USA. 93:7063-7068.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7063-7068
    • Wang, H.-G.1    Takayama, S.2    Rapp, U.R.3    Reed, J.C.4
  • 47
    • 0032572715 scopus 로고    scopus 로고
    • Human BAG-1/RAP46 protein is generated as four isoforms by alternative translation initiation and overexpressed in cancer cells
    • Yang, X., G. Chernenko, Y. Hao, Z. Ding, M.M. Pater, A. Pater, and S.-C. Tang. 1998. Human BAG-1/RAP46 protein is generated as four isoforms by alternative translation initiation and overexpressed in cancer cells. Oncogens. 17:981-989.
    • (1998) Oncogens , vol.17 , pp. 981-989
    • Yang, X.1    Chernenko, G.2    Hao, Y.3    Ding, Z.4    Pater, M.M.5    Pater, A.6    Tang, S.-C.7
  • 48
    • 0029614713 scopus 로고
    • A protein that interacts with members of the nuclear hormone receptor family: Identification and cDNA cloning
    • Zeiner, M., and U. Gehring. 1995. A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning. Proc. Natl. Acad. Sci. USA. 92:11465-11469.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11465-11469
    • Zeiner, M.1    Gehring, U.2
  • 49
    • 0030766734 scopus 로고    scopus 로고
    • Mammalian protein RAP46: An interaction partner and modulator of 70 kDa heat shock proteins
    • Zeiner, M., M. Gebauer, and U. Gehring. 1997. Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins. EMBO (Eur. Mol. Biol. Organ.) J. 16:5483-5490.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 5483-5490
    • Zeiner, M.1    Gebauer, M.2    Gehring, U.3


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