메뉴 건너뛰기




Volumn 16, Issue 16, 1997, Pages 4887-4896

BAG-1 modulates the chaperone activity of Hsp70/Hsc70

Author keywords

BAG 1; Bcl 2; Chaperone; Hsc70; Hsp70

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN 70; PROTEIN; PROTEIN BCL 2;

EID: 0030871891     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.16.4887     Document Type: Article
Times cited : (446)

References (38)
  • 3
    • 0029807304 scopus 로고    scopus 로고
    • Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization
    • Farrar, M.A., Alberola-Ila, J. and Perlmutter, R.M. (1996) Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization. Nature, 383, 178-180.
    • (1996) Nature , vol.383 , pp. 178-180
    • Farrar, M.A.1    Alberola-Ila, J.2    Perlmutter, R.M.3
  • 4
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones in hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman, B.C. and Morimoto, R.I. (1996) The human cytosolic molecular chaperones in hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J., 15, 2969-2979.
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 5
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman, B.C., Myers, M.P., Schumacher, R. and Morimoto, R.I. (1995) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J., 14, 2281-2292.
    • (1995) EMBO J. , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 6
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman, B.C., Toft, D.O. and Morimoto, R.I. (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
  • 7
    • 0029787852 scopus 로고    scopus 로고
    • Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled
    • Fung, K.L., Hilgenberg, L., Wang, N.M. and Chirico, W.J. (1996) Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled. J. Biol. Chem., 271, 21559-21565.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21559-21565
    • Fung, K.L.1    Hilgenberg, L.2    Wang, N.M.3    Chirico, W.J.4
  • 8
    • 0030293446 scopus 로고    scopus 로고
    • Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-alpha and cycloheximide: A possible role in immunopathology
    • Galea-Lauri, J., Richardson, A.J., Latchman, D.S. and Katz, D.R. (1996) Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-alpha and cycloheximide: a possible role in immunopathology. J. Immunol., 157, 4109-4118.
    • (1996) J. Immunol. , vol.157 , pp. 4109-4118
    • Galea-Lauri, J.1    Richardson, A.J.2    Latchman, D.S.3    Katz, D.R.4
  • 9
    • 0002337352 scopus 로고
    • Interaction Trap-Two-hybrid system to identify interacting proteins
    • Coligan, J.E. et al. (eds), J. Wiley and Sons, Inc., New York
    • Golemis, E.A., Gyuris, J. and Brent, R. (1994) Interaction Trap-Two-hybrid system to identify interacting proteins. In Coligan, J.E. et al. (eds), Protocols in Molecular Biology. J. Wiley and Sons, Inc., New York, pp. 13.14.1-13.14.17.
    • (1994) Protocols in Molecular Biology , pp. 13141-131417
    • Golemis, E.A.1    Gyuris, J.2    Brent, R.3
  • 10
    • 0029161689 scopus 로고
    • Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding
    • Ha, J.H. and McKay, D.B. (1995) Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding. Biochemistry, 34, 11635-11644.
    • (1995) Biochemistry , vol.34 , pp. 11635-11644
    • Ha, J.H.1    McKay, D.B.2
  • 11
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature, 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 12
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones and proteotoxicity
    • Hightower, L.E. (1991) Heat shock, stress proteins, chaperones and proteotoxicity. Cell, 66, 191-197.
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 13
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Höhfeld, J., Minami, Y. and Hartl, F.-U. (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
    • 0027969323 scopus 로고
    • Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90
    • Hutchinson, K.A., Dittmar, K.D., Czar, M.J. and Pratt, W.B. (1994) Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90. J. Biol. Chem., 269, 5043-5049.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5043-5049
    • Hutchinson, K.A.1    Dittmar, K.D.2    Czar, M.J.3    Pratt, W.B.4
  • 16
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • Jakob, U. and Buchner, J. (1994) Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci., 19, 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 17
    • 0031016469 scopus 로고    scopus 로고
    • Functional specificity among Hsp70 molecular chaperones
    • James, P., Pfund, C. and Craig, E.A. (1997) Functional specificity among Hsp70 molecular chaperones. Science, 275, 387-388.
    • (1997) Science , vol.275 , pp. 387-388
    • James, P.1    Pfund, C.2    Craig, E.A.3
  • 18
    • 0028271110 scopus 로고
    • Heat-shock proteins maintain the viability of ATP-deprived cells: What is the mechanism?
    • Kabakov, A.E. and Gabai, V.L. (1994) Heat-shock proteins maintain the viability of ATP-deprived cells: what is the mechanism? Trends Cell Biol., 4, 193-196.
    • (1994) Trends Cell Biol. , vol.4 , pp. 193-196
    • Kabakov, A.E.1    Gabai, V.L.2
  • 19
    • 0029811985 scopus 로고    scopus 로고
    • Oligomerization activates c-Raf-1 through a Ras-dependent mechanism
    • Luo, Z., Tzivion, G., Belshaw, P.J., Vavvas, D., Marshall, M. and Avruch, J. (1996) Oligomerization activates c-Raf-1 through a Ras-dependent mechanism. Nature, 383, 181-185.
    • (1996) Nature , vol.383 , pp. 181-185
    • Luo, Z.1    Tzivion, G.2    Belshaw, P.J.3    Vavvas, D.4    Marshall, M.5    Avruch, J.6
  • 21
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bcl-XL, an inhibitor of programmed cell death
    • Muchmore, S.W. et al. (1996) X-ray and NMR structure of human Bcl-XL, an inhibitor of programmed cell death. Nature, 381, 335-341.
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1
  • 24
    • 0028418758 scopus 로고
    • Chaperone functions of the heat shock proteins associated with steroid receptors
    • Pratt, W.B. and Welsh, M.J. (1994) Chaperone functions of the heat shock proteins associated with steroid receptors. Cell Biol., 5, 83-93.
    • (1994) Cell Biol. , vol.5 , pp. 83-93
    • Pratt, W.B.1    Welsh, M.J.2
  • 25
    • 0028965273 scopus 로고
    • Partner proteins determine multiple functions of Hsp70
    • Rassow, J., Voos, W. and Pfanner, N. (1995) Partner proteins determine multiple functions of Hsp70. Trends Cell Biol., 5, 207-212.
    • (1995) Trends Cell Biol. , vol.5 , pp. 207-212
    • Rassow, J.1    Voos, W.2    Pfanner, N.3
  • 26
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • Reed, J.C. (1997) Double identity for proteins of the Bcl-2 family. Nature, 387, 773-776.
    • (1997) Nature , vol.387 , pp. 773-776
    • Reed, J.C.1
  • 28
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith, D.F., Whitesell, L., Nair, S.C., Chen, S., Prapapanich, V. and Rimerman, R.A. (1995) Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol., 15, 6804-6812.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6804-6812
    • Smith, D.F.1    Whitesell, L.2    Nair, S.C.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.A.6
  • 29
    • 0029060160 scopus 로고
    • Bcl-2 and thermotolerance cooperate in cell survival
    • Strasser, A. and Anderson, R.L. (1995) Bcl-2 and thermotolerance cooperate in cell survival. Cell Growth Differ., 6, 799-805.
    • (1995) Cell Growth Differ. , vol.6 , pp. 799-805
    • Strasser, A.1    Anderson, R.L.2
  • 30
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system
    • Stancato, L.F., Chow, Y.H., Hutchison, K.A., Perdew, G.H., Jove, R. and Pratt, W.B. (1993) Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system, J. Biol. Chem., 268, 21711-21716.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.H.2    Hutchison, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 31
    • 0030639056 scopus 로고    scopus 로고
    • Protein interaction cloning by far-western screening of λ phage cDNA expression libraries
    • Cowell, I.G. and Austin, C.A. (eds), Humana Press, Totowa, NJ
    • Takayama, S. and Reed, J.C. (1996) Protein interaction cloning by far-western screening of λ phage cDNA expression libraries. In Cowell, I.G. and Austin, C.A. (eds), Methods in Molecular Biology. Humana Press, Totowa, NJ, pp. 171-184.
    • (1996) Methods in Molecular Biology , pp. 171-184
    • Takayama, S.1    Reed, J.C.2
  • 32
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1: A novel Bcl-2 binding protein with anti-cell death activity
    • Takayama, S., Sato, T., Krajewski, S., Kochel, K., Irie, S., Millan, J.A. and Reed, J.C. (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
  • 33
    • 0030219848 scopus 로고    scopus 로고
    • Cloning of cDNAs encoding human BAG1 protein and localization of the human BAG1 gene to chromosome 9p12
    • Takayama, S., Kochel, K., Irie, S., Inazawa, J., Abe, T., Sato, T., Druck, T., Huebner, K. and Reed, J.C. (1996) Cloning of cDNAs encoding human BAG1 protein and localization of the human BAG1 gene to chromosome 9p12. Genomics, 35, 494-498.
    • (1996) Genomics , vol.35 , pp. 494-498
    • Takayama, S.1    Kochel, K.2    Irie, S.3    Inazawa, J.4    Abe, T.5    Sato, T.6    Druck, T.7    Huebner, K.8    Reed, J.C.9
  • 34
    • 0028144848 scopus 로고
    • Apoptosis regulation by interaction of bcl-2 protein and Raf-1 kinase
    • Wang, H.-G. et al. (1994) Apoptosis regulation by interaction of bcl-2 protein and Raf-1 kinase. Oncogene, 9, 2751-2756.
    • (1994) Oncogene , vol.9 , pp. 2751-2756
    • Wang, H.-G.1
  • 35
    • 0029937303 scopus 로고    scopus 로고
    • Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1
    • Wang, H.-G., Takayama, S., Rapp, U.R. and Reed, J.C. (1996a) 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
  • 36
    • 0345498292 scopus 로고    scopus 로고
    • Bcl-2 targets the protein kinase Raf-1 to mitochondria
    • Wang, H.G., Rapp, U.R. and Reed, J.C. (1996b) Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell, 87, 629-638.
    • (1996) Cell , vol.87 , pp. 629-638
    • Wang, H.G.1    Rapp, U.R.2    Reed, J.C.3
  • 37
    • 0028227245 scopus 로고
    • The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex
    • Wartmann, M. and Davis, R.J. (1994) The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex, J. Biol. Chem., 269, 6695-6701.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6695-6701
    • Wartmann, M.1    Davis, R.J.2
  • 38
    • 0029614713 scopus 로고
    • A protein that interacts with members of the nuclear hormone receptor family: Identification and cDNA cloning
    • Zeiner, M. and Gehring, U. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.