메뉴 건너뛰기




Volumn 9, Issue 1, 2014, Pages

Hsp70 cochaperones HspBP1 and BAG-1M differentially regulate steroid hormone receptor function

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; BINDING PROTEIN; GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 70 BINDING PROTEIN 1; MINERALOCORTICOID RECEPTOR; PROTEIN BCL 2; PROTEIN BCL2 ASSOCIATED ATHANOGENE 1; STEROID RECEPTOR; UNCLASSIFIED DRUG;

EID: 84898015611     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0085415     Document Type: Article
Times cited : (24)

References (51)
  • 1
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, and Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475: 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 2
    • 52949139464 scopus 로고    scopus 로고
    • Minireview: The intersection of steroid receptors with molecular chaperones: Observations and questions
    • Smith DF, Toft DO (2008) Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions. Mol. Endocrinol. 22: 2229-2240.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 2229-2240
    • Smith, D.F.1    Toft, D.O.2
  • 3
    • 34547872322 scopus 로고    scopus 로고
    • The glucocorticoid responses are shaped by molecular chaperones
    • DOI 10.1016/j.mce.2007.05.018, PII S0303720707002146
    • Grad I, Picard D (2007) The glucocorticoid responses are shaped by molecular chaperones. Mol. Cell Endocrinol. 275: 2-12. (Pubitemid 47260713)
    • (2007) Molecular and Cellular Endocrinology , vol.275 , Issue.1-2 , pp. 2-12
    • Grad, I.1    Picard, D.2
  • 4
    • 20044395965 scopus 로고    scopus 로고
    • Stress and the brain: From adaptation to disease
    • DOI 10.1038/nrn1683
    • De Kloet ER, Joels M, Holsboer F (2005) Stress and the brain: from adaptation to disease. Nat. Rev. Neurosci 6: 463-475. (Pubitemid 40769171)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.6 , pp. 463-475
    • De Kloet, E.R.1    Joels, M.2    Holsboer, F.3
  • 5
    • 0033797445 scopus 로고    scopus 로고
    • The corticosteroid receptor hypothesis of depression
    • Holsboer F (2000) The corticosteroid receptor hypothesis of depression. Neuropsychopharmacology 23: 477-501.
    • (2000) Neuropsychopharmacology , vol.23 , pp. 477-501
    • Holsboer, F.1
  • 6
    • 77955400148 scopus 로고    scopus 로고
    • Differential impact of tetratricopeptide repeat proteins on the steroid hormone receptors
    • Schülke JP, Wochnik GM, Lang-Rollin I, Gassen NC, Knapp RT et al. (2010) Differential impact of tetratricopeptide repeat proteins on the steroid hormone receptors. PLoS. One. 5: e11717.
    • (2010) PLoS. One. , vol.5
    • Schülke, J.P.1    Wochnik, G.M.2    Lang-Rollin, I.3    Gassen, N.C.4    Knapp, R.T.5
  • 8
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
    • Smith DF (1993) Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7: 1418-1429.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 9
    • 0029681032 scopus 로고    scopus 로고
    • Molecular chaperoning of steroid hormone receptors
    • Pratt WB, Gehring U, Toft DO (1996) Molecular chaperoning of steroid hormone receptors. EXS. 77: 79-95.
    • (1996) EXS. , vol.77 , pp. 79-95
    • Pratt, W.B.1    Gehring, U.2    Toft, D.O.3
  • 11
    • 0037023732 scopus 로고    scopus 로고
    • HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor
    • DOI 10.1074/jbc.M111445200
    • Hernandez MP, Chadli A, Toft DO (2002) HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor. J. Biol. Chem. 277: 11873-11881. (Pubitemid 34952744)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 11873-11881
    • Patricia, H.M.1    Chadli, A.2    Toft, D.O.3
  • 12
    • 0033616741 scopus 로고    scopus 로고
    • DnaJ dramatically stimulates ATP hydrolysis by DnaK: Insight into targeting of Hsp70 proteins to polypeptide substrates
    • Russell R, Wali KA, Mehl AF, McMacken R (1999) DnaJ dramatically stimulates ATP hydrolysis by DnaK: insight into targeting of Hsp70 proteins to polypeptide substrates. Biochemistry 38: 4165-4176.
    • (1999) Biochemistry , vol.38 , pp. 4165-4176
    • Russell, R.1    Wali, K.A.2    Mehl, A.F.3    McMacken, R.4
  • 13
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Höhfeld J, Minami Y, Hartl FU (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
  • 14
    • 0034329452 scopus 로고    scopus 로고
    • Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
    • Young JC, Hartl FU (2000) Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J 19: 5930-5940.
    • (2000) EMBO J , vol.19 , pp. 5930-5940
    • Young, J.C.1    Hartl, F.U.2
  • 15
    • 0032483996 scopus 로고    scopus 로고
    • Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein
    • DOI 10.1074/jbc.273.49.32883
    • Raynes DA, Guerriero V Jr (1998) Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein. J. Biol. Chem. 273: 32883-32888. (Pubitemid 28557679)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.49 , pp. 32883-32888
    • Raynes, D.A.1    Guerriero Jr., V.2
  • 16
    • 13244278043 scopus 로고    scopus 로고
    • Regulation of Hsp70 function by HspBP1: Structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange 2665
    • 2005. Feb. 4. 17: 367-379
    • Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC et al. (2005) Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange 2665. Mol. Cell. 2005. Feb. 4.;17. (3.) : 367. -79. 17: 367-379.
    • (2005) Mol. Cell. , vol.17 , Issue.3 , pp. 367-379
    • Shomura, Y.1    Dragovic, Z.2    Chang, H.C.3    Tzvetkov, N.4    Young, J.C.5
  • 17
    • 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, Chernenko G, Hao Y, Ding Z, Pater MM et al. (1998) Human BAG-1/RAP46 protein is generated as four isoforms by alternative translation initiation and overexpressed in cancer cells. Oncogene 17: 981-989. (Pubitemid 28425408)
    • (1998) Oncogene , vol.17 , Issue.8 , 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
  • 19
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • Lüders J, Demand J, Höhfeld J (2000) The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J Biol Chem 275: 4613-4617.
    • (2000) J Biol Chem , vol.275 , pp. 4613-4617
    • Lüders, J.1    Demand, J.2    Höhfeld, J.3
  • 20
    • 0344443774 scopus 로고    scopus 로고
    • BAG-1 - A nucleotide exchange factor of Hsc70 with multiple cellular functions
    • DOI 10.1379/1466-1268(2003)008<0225:BNEFOH>2.0
    • Alberti S, Esser C, Hohfeld J (2003) BAG-1-a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress. Chaperones. 8: 225-231. (Pubitemid 37484716)
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.3 , pp. 225-231
    • Alberti, S.1    Esser, C.2    Hohfeld, J.3
  • 21
    • 0039598518 scopus 로고    scopus 로고
    • Distinct Isoforms of the Cofactor BAG-1 Differentially Affect Hsc70 Chaperone Function
    • Lüders J, Demand J, Papp O, Höhfeld J (2000) Distinct Isoforms of the Cofactor BAG-1 Differentially Affect Hsc70 Chaperone Function. J. Biol. Chem. 275: 14817-14823.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14817-14823
    • Lüders, J.1    Demand, J.2    Papp, O.3    Höhfeld, J.4
  • 22
    • 0032496242 scopus 로고    scopus 로고
    • BAG-1L protein enhances androgen receptor function
    • DOI 10.1074/jbc.273.19.11660
    • Froesch BA, Takayama S, Reed JC (1998) BAG-1L protein enhances androgen receptor function. J Biol Chem 273: 11660-11666. (Pubitemid 28272067)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.19 , pp. 11660-11666
    • Froesch, B.A.1    Takayama, S.2    Reed, J.C.3
  • 24
    • 0344200100 scopus 로고    scopus 로고
    • A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity
    • DOI 10.1083/jcb.146.5.929
    • Schneikert J, Hübner S, Martin E, Cato AC (1999) A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity. J Cell Biol 146: 929-940. (Pubitemid 29430437)
    • (1999) Journal of Cell Biology , vol.146 , Issue.5 , pp. 929-940
    • Schneikert, J.1    Hubner, S.2    Martin, E.3    Cato, A.C.B.4
  • 26
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • DOI 10.1126/science.1057268
    • Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU et al. (2001) Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors. Science 291: 1553-1557. (Pubitemid 32179223)
    • (2001) Science , vol.291 , Issue.5508 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.-U.5    Moarefi, I.6
  • 27
    • 0023794190 scopus 로고
    • Multiple and cooperative trans-activation domains of the human glucocorticoid receptor
    • Hollenberg SM, Evans RM (1988) Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell 55: 899-906.
    • (1988) Cell , vol.55 , pp. 899-906
    • Hollenberg, S.M.1    Evans, R.M.2
  • 29
    • 14244262261 scopus 로고    scopus 로고
    • FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells
    • DOI 10.1074/jbc.M407498200
    • Wochnik GM, Rüegg J, Abel GA, Schmidt U, Holsboer F et al. (2005) FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells. J. Biol. Chem. 280: 4609-4616. (Pubitemid 40288629)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4609-4616
    • Wochnik, G.M.1    Ruegg, J.2    Abel, G.A.3    Schmidt, U.4    Holsboer, F.5    Rein, T.6
  • 31
    • 0037031902 scopus 로고    scopus 로고
    • Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M204624200
    • Sondermann H, Ho AK, Listenberger LL, Siegers K, Moarefi I et al. (2002) Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. J. Biol. Chem. 277: 33220-33227. (Pubitemid 34984841)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 33220-33227
    • Sondermann, H.1    Ho, A.K.2    Listenberger, L.L.3    Siegers, K.4    Moarefi, I.5    Wente, S.R.6    Hartl, F.U.7    Young, J.C.8
  • 32
    • 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, Zeiner M, Gehring U (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. (Pubitemid 28500514)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.11 , pp. 6238-6244
    • Gebauer, M.1    Zeiner, M.2    Gehring, U.3
  • 33
    • 0032402812 scopus 로고    scopus 로고
    • BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release
    • Bimston D, Song J, Winchester D, Takayama S, Reed JC et al. (1998) BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878. (Pubitemid 28550281)
    • (1998) EMBO Journal , vol.17 , Issue.23 , pp. 6871-6878
    • Bimston, D.1    Song, J.2    Winchester, D.3    Takayama, S.4    Reed, J.C.5    Morimoto, R.I.6
  • 34
    • 0034700318 scopus 로고    scopus 로고
    • hsp70 interacting protein hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except To oppose the effect of BAG-1
    • Kanelakis KC, Murphy PJ, Galigniana MD, Morishima Y, Takayama S et al. (2000) hsp70 interacting protein hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except To oppose the effect of BAG-1. Biochemistry 39: 14314-14321.
    • (2000) Biochemistry , vol.39 , pp. 14314-14321
    • Kanelakis, K.C.1    Murphy, P.J.2    Galigniana, M.D.3    Morishima, Y.4    Takayama, S.5
  • 35
    • 0035980016 scopus 로고    scopus 로고
    • Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor
    • Gässler CS, Wiederkehr T, Brehmer D, Bukau B, Mayer MP (2001) Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J. Biol. Chem. 276: 32538-32544.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32538-32544
    • Gässler, C.S.1    Wiederkehr, T.2    Brehmer, D.3    Bukau, B.4    Mayer, M.P.5
  • 38
    • 0035918305 scopus 로고    scopus 로고
    • Structure-function analysis of bag1 proteins. Effects on androgen receptor transcriptional activity
    • Knee DA, Froesch BA, Nuber U, Takayama S, Reed JC (2001) Structure-function analysis of bag1 proteins. effects on androgen receptor transcriptional activity. J. Biol. Chem. 276: 12718-12724.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12718-12724
    • Knee, D.A.1    Froesch, B.A.2    Nuber, U.3    Takayama, S.4    Reed, J.C.5
  • 39
    • 77950594362 scopus 로고    scopus 로고
    • Nuclear or cytoplasmic localization of Bag-1 distinctly correlates with pathologic behavior and outcome of gastric carcinomas
    • Zheng HC, Xu XY, Xing YN, Wei ZL, Takahashi H et al. (2010) Nuclear or cytoplasmic localization of Bag-1 distinctly correlates with pathologic behavior and outcome of gastric carcinomas. Hum. Pathol. 41: 724-736.
    • (2010) Hum. Pathol. , vol.41 , pp. 724-736
    • Zheng, H.C.1    Xu, X.Y.2    Xing, Y.N.3    Wei, Z.L.4    Takahashi, H.5
  • 40
    • 4344578534 scopus 로고    scopus 로고
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator
    • DOI 10.1091/mbc.E04-04-0293
    • Alberti S, Bohse K, Arndt V, Schmitz A, Hohfeld J (2004) The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Mol. Biol. Cell 15: 4003-4010. (Pubitemid 39122006)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.9 , pp. 4003-4010
    • Alberti, S.1    Bohse, K.2    Arndt, V.3    Schmitz, A.4    Hohfeld, J.5
  • 41
    • 84876042495 scopus 로고    scopus 로고
    • Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins
    • Gowda NK, Kandasamy G, Froehlich MS, Dohmen RJ, Andreasson C (2013) Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins. Proc. Natl. Acad. Sci. U. S. A 110: 5975-5980.
    • (2013) Proc. Natl. Acad. Sci. U. S. A , vol.110 , pp. 5975-5980
    • Gowda, N.K.1    Kandasamy, G.2    Froehlich, M.S.3    Dohmen, R.J.4    Andreasson, C.5
  • 43
    • 3042821267 scopus 로고    scopus 로고
    • Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation
    • Oh WK, Song J (2003) Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation. Mol. Cells 16: 84-91.
    • (2003) Mol. Cells , vol.16 , pp. 84-91
    • Oh, W.K.1    Song, J.2
  • 44
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • DOI 10.1126/science.1073051
    • Freeman BC, Yamamoto KR (2002) Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296: 2232-2235. (Pubitemid 34680310)
    • (2002) Science , vol.296 , Issue.5576 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 45
    • 67849116564 scopus 로고    scopus 로고
    • Bag-1M inhibits the transactivation of the glucocorticoid receptor via recruitment of corepressors
    • Hong W, Baniahmad A, Li J, Chang C, Gao W et al. (2009) Bag-1M inhibits the transactivation of the glucocorticoid receptor via recruitment of corepressors. FEBS Lett. 583: 2451-2456.
    • (2009) FEBS Lett. , vol.583 , pp. 2451-2456
    • Hong, W.1    Baniahmad, A.2    Li, J.3    Chang, C.4    Gao, W.5
  • 46
    • 54249091505 scopus 로고    scopus 로고
    • Bag-1M is a component of the in vivo DNA-glucocorticoid receptor complex at hormone-regulated promoter
    • Hong W, Baniahmad A, Liu Y, Li H (2008) Bag-1M is a component of the in vivo DNA-glucocorticoid receptor complex at hormone-regulated promoter. J. Mol. Biol. 384: 22-30.
    • (2008) J. Mol. Biol. , vol.384 , pp. 22-30
    • Hong, W.1    Baniahmad, A.2    Liu, Y.3    Li, H.4
  • 47
    • 1542327611 scopus 로고    scopus 로고
    • Increased expression of the Hsp70 cochaperone HspBP1 in tumors
    • DOI 10.1159/000076459
    • Raynes DA, Graner MW, Bagatell R, McLellan C, Guerriero V (2003) Increased expression of the Hsp70 cochaperone HspBP1 in tumors. Tumour. Biol. 24: 281-285. (Pubitemid 38327989)
    • (2003) Tumor Biology , vol.24 , Issue.6 , pp. 281-285
    • Raynes, D.A.1    Graner, M.W.2    Bagatell, R.3    McLellan, C.4    Guerriero, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.