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Volumn 16, Issue 20, 1997, Pages 6209-6216

GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1

Author keywords

Apoptosis; BAG 1; GrpE; Hsc70; Molecular chaperone

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN 70; REGULATOR PROTEIN;

EID: 0344039806     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.20.6209     Document Type: Article
Times cited : (342)

References (39)
  • 2
    • 0002830140 scopus 로고
    • Modulation of steroid receptor signal transduction by heat shock proteins
    • Morimoto, R.L. Tissieres, A. and Georgopoulos, C. (eds). Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY
    • Bohen, S.P. and Yamamoto, K.R. (1994) Modulation of steroid receptor signal transduction by heat shock proteins. In Morimoto, R.L. Tissieres, A. and Georgopoulos, C. (eds). The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY. pp. 313-334.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 313-334
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 3
    • 0028382510 scopus 로고
    • A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE
    • Buchberger, A., Schröder, H., Bünner, M., Valencia, A. and Bukau, B. (1994) A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat. Struct. Biol., 1, 95-101.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 95-101
    • Buchberger, A.1    Schröder, H.2    Bünner, M.3    Valencia, A.4    Bukau, B.5
  • 4
    • 0002237472 scopus 로고
    • Cytosolic hsp70s of Saccharomyces cerevisiae: A role in protein synthesis, protein translocation, protcolysis. and rcgulation
    • Morimoto, R.I., Tissieres, A. and Georgopoulos, C. (eds). Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY
    • Craig, E.A., Baxter, B.K., Becker, J., Halladay, J. and Ziegelhoffer, T. (1994) Cytosolic hsp70s of Saccharomyces cerevisiae: a role in protein synthesis, protein translocation, protcolysis. and rcgulation. In Morimoto, R.I., Tissieres, A. and Georgopoulos, C. (eds). The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY. pp. 31-52.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 31-52
    • Craig, E.A.1    Baxter, B.K.2    Becker, J.3    Halladay, J.4    Ziegelhoffer, T.5
  • 5
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G.C., Pohl, J., Flocco, M.T. and Rothman, J.E. (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature. 353, 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 6
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones bsp90, bsp70 (bsc70) and hdj-1 have distinct roles in the recognition of a non-native protein and protein refolding
    • Freeman, B.C. and Morimoto, R.I. ( 1996) The human cytosolic molecular chaperones bsp90, bsp70 (bsc70) and hdj-1 have distinct roles in the 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
  • 7
    • 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
  • 8
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J. and Höhfeld, J. (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
  • 9
    • 0028361309 scopus 로고
    • Folding of nascent polypeptidc chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgem, E., Ohtsuka, K. and Hantl, F.U. (1994) Folding of nascent polypeptidc chains in a high molecular mass assembly with molecular chaperones. Nature. 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgem, E.2    Ohtsuka, K.3    Hantl, F.U.4
  • 10
    • 0000757557 scopus 로고
    • Properties of the heat shock proteins of Escherichia coli and the autoregulation of the heat shock response
    • Morimoto, R.L. Tissieres, A. and Georgopuulos, C. (eds). Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY
    • Georgopoulos, C., Liberek, K., Zylicz, M. and Ang, D. (1994) Properties of the heat shock proteins of Escherichia coli and the autoregulation of the heat shock response. In Morimoto, R.L. Tissieres, A. and Georgopuulos, C. (eds). The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY. pp. 209-249.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 209-249
    • Georgopoulos, C.1    Liberek, K.2    Zylicz, M.3    Ang, D.4
  • 11
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotidc exchange factor GrpE bound to the ATPase domain of the molecular chaperanc DnaK
    • Harrison, C.J., Hayer-Hartl, M., Di Liberto, M., Hartl, F.-U. and Kuriyan, J. (1997) Crystal structure of the nucleotidc exchange factor GrpE bound to the ATPase domain of the molecular chaperanc DnaK. Science. 276, 431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.-U.4    Kuriyan, J.5
  • 12
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding
    • Hartl, F.-U. (1996) Molecular chaperones in protein folding. Nature. 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.-U.1
  • 13
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser, M. (1996) Protein degradation or regulation: ub the judge. Cell. 84, 813-815.
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M.1
  • 14
    • 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
  • 15
    • 0031029286 scopus 로고    scopus 로고
    • Characterization of functional domains of the eukaryotic co-chaperone Hip
    • Irmer, H. and Höhfeld, J. (1997) Characterization of functional domains of the eukaryotic co-chaperone Hip. J. Biol. Chem., 272, 2230-2235.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2230-2235
    • Irmer, H.1    Höhfeld, J.2
  • 16
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C. and Zylicz, M. (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl Acad. Sci. USA. 88, 2874-2878.
    • (1991) Proc. Natl Acad. Sci. USA. , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 17
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty, J.S., Buchberger, A., Reinstein, J. and Bukau, B. (1995) The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol., 249, 126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 18
    • 0029741321 scopus 로고    scopus 로고
    • Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog. Hsp40
    • Minami, Y., Höhfeld, J., Ohtsuka, K. and Hartl, F.-U. (1996) Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog. Hsp40. J. Biol. Chem., 271, 19617-19624.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19617-19624
    • Minami, Y.1    Höhfeld, J.2    Ohtsuka, K.3    Hartl, F.-U.4
  • 19
    • 0030569286 scopus 로고    scopus 로고
    • Isolation and characterisation of a cDNA encoding rat mitochondrial GrrpE, a stress-induciblc nucleotide-exchange factor of ubiquitous appearance in mammalian organs
    • Naylor, D.J., Hoogenraad, N.J. and Hoj, P.B. (1996) Isolation and characterisation of a cDNA encoding rat mitochondrial GrrpE, a stress-induciblc nucleotide-exchange factor of ubiquitous appearance in mammalian organs. FEBS Lett., 396, 181-188.
    • (1996) FEBS Lett , vol.396 , pp. 181-188
    • Naylor, D.J.1    Hoogenraad, N.J.2    Hoj, P.B.3
  • 20
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros, D.R., Welch, W.J. and Fink, A.L. (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Prof. Natl Acad. Sci. USA. 88, 5719-5723.
    • (1991) Prof. Natl Acad. Sci. USA. , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 21
    • 0029964506 scopus 로고    scopus 로고
    • Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein
    • Prapapanich, V., Chen, S., Nair, S.C., Rimerman, R.A. and Smith, D.F. (1996) Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein. Mol. Endocrinol., 10, 420-131.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 420-1131
    • Prapapanich, V.1    Chen, S.2    Nair, S.C.3    Rimerman, R.A.4    Smith, D.F.5
  • 22
    • 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
  • 23
    • 0041026092 scopus 로고    scopus 로고
    • Interaction of Hsp70 chaperones with substrates
    • Rüdiger, S., Buchberger, A. and Bukau, B. (1997) Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol., 4, 342-349.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 342-349
    • Rüdiger, S.1    Buchberger, A.2    Bukau, B.3
  • 24
    • 0026799491 scopus 로고
    • Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange
    • Sadis, S. and Hightower, L.E. (1992) Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry, 31, 9407-9412.
    • (1992) Biochemistry , vol.31 , pp. 9407-9412
    • Sadis, S.1    Hightower, L.E.2
  • 25
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomcric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H., Cramer, W.A. and von Jagow, G. (1994) Analysis of molecular masses and oligomcric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem., 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 26
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • Schlossman, D.M., Schmid, S.L., Braell, W.A. and Rothman, J.H. (1984) An enzyme that removes clathrin coats: purification of an uncoating ATPase. J. Cell Biol., 99, 723-733.
    • (1984) J. Cell Biol. , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.H.4
  • 27
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., Baici, A., Gehring, H. and Christen, P. (1994) Kinetics of molecular chaperone action. Science. 263, 971-973.
    • (1994) Science , vol.263 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 29
    • 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
  • 30
    • 0023316845 scopus 로고
    • Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells
    • Sorger, P.K. and Pelham, H.R.B. (1987) Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells. EMBO J., 6, 993-998.
    • (1987) EMBO J. , vol.6 , pp. 993-998
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 31
    • 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., Hutchinson, 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    Hutchinson, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 32
    • 0027958293 scopus 로고
    • Mitochondrial molecular chaperones: Their role in protein translocation
    • Stuart, R.A., Cyr, D.M., Craig, E.A. and Neupert, W. (1994) Mitochondrial molecular chaperones: their role in protein translocation. Trends Biochem. Sci., 19, 87-92.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 87-92
    • Stuart, R.A.1    Cyr, D.M.2    Craig, E.A.3    Neupert, W.4
  • 33
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system - DnaK, DnaJ, and GrpE
    • Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B. and Hartl, F.-U. (1994) The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system - DnaK, DnaJ, and GrpE. Proc. Natl Acad. Sci. USA. 91, 10345-10349.
    • (1994) Proc. Natl Acad. Sci. USA. , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schröder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.-U.6
  • 34
    • 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
  • 35
    • 0030896688 scopus 로고    scopus 로고
    • The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila
    • Van der Straten, A., Rommel, C. Dickson, B. and Hafen, E. (1997) The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila. EMBO J., 16, 1961-1969.
    • (1997) EMBO J , vol.16 , pp. 1961-1969
    • Van der Straten, A.1    Rommel, C.2    Dickson, B.3    Hafen, E.4
  • 36
    • 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. (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
  • 37
    • 0028287525 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic
    • Willbanks, S., DeLuca-Flaherty, C. and McKay, D.B. (1994) Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. J. Biol. Chem., 269, 12893-12898.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12893-12898
    • Willbanks, S.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 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


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