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Volumn 379, Issue 10, 1998, Pages 1217-1226

Cofactor-induced modulation of the functional specificity of the molecular chaperone Hsc70

Author keywords

ATPase; Hdj 1; Hsp70; RAP46; Refolding

Indexed keywords

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

EID: 0031731598     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.10.1217     Document Type: Article
Times cited : (34)

References (35)
  • 1
    • 0002237472 scopus 로고
    • Cytosolic hsp70s of Saccharomyces cerevisiae: Roles in protein synthesis, protein translocation, proteolysis, and regulation
    • R.I. Morimoto, A. Tissieres and C. Georgopoulos, eds. (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press)
    • Craig, E.A., Baxter, B.K., Becker, J., Halladay, J., and Ziegelhoffer, T. (1994). Cytosolic hsp70s of Saccharomyces cerevisiae: roles in protein synthesis, protein translocation, proteolysis, and regulation. In: The Biology of Heat Shock Proteins and Molecular Chaperones, R.I. Morimoto, A. Tissieres and C. Georgopoulos, eds. (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press), 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
  • 2
    • 2642689664 scopus 로고    scopus 로고
    • The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
    • Demand, J., Lüders, J., and Höhfeld, J. (1998). The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol. Cell. Biol. 18, 2023-2028.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2023-2028
    • Demand, J.1    Lüders, J.2    Höhfeld, J.3
  • 3
    • 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
  • 4
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) 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 hsp90, hsp70 (hsc70) 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
  • 5
    • 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
  • 6
    • 0030671388 scopus 로고    scopus 로고
    • Proteins interacting with the molecular chaperone hsp70/hsc70: Physical associations and effects on refolding activity
    • Gebauer, M., Zeiner, M., and Gehring, U. (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
  • 7
    • 0031034563 scopus 로고    scopus 로고
    • Controlling cell death
    • Golstein, P. (1997). Controlling cell death. Science 275, 1081-1082.
    • (1997) Science , vol.275 , pp. 1081-1082
    • Golstein, P.1
  • 8
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding
    • Hartl, F.-U. (1996). Molecular chaperones in protein folding. Nature 387, 571-580.
    • (1996) Nature , vol.387 , pp. 571-580
    • Hartl, F.-U.1
  • 9
    • 0038217763 scopus 로고    scopus 로고
    • Regulation of the heat shock cognate Hsc70 in the mammalian cell: The characterization of the anti-apoptotic protein BAG-1 provides novel insights
    • Höhfeld, J. (1998). Regulation of the heat shock cognate Hsc70 in the mammalian cell: the characterization of the anti-apoptotic protein BAG-1 provides novel insights. Biol. Chem. 379, 269-274.
    • (1998) Biol. Chem. , vol.379 , pp. 269-274
    • Höhfeld, J.1
  • 10
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Höhfeld, J., and Jentsch, S. (1997). GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16, 6209-6216.
    • (1997) EMBO J. , vol.16 , pp. 6209-6216
    • Höhfeld, J.1    Jentsch, S.2
  • 11
    • 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
  • 12
    • 0029846829 scopus 로고    scopus 로고
    • Mechanism of clathrin basket dissociation: Separate functions of protein domains of the DnaJ homologue auxilin
    • Holstein, S.E.H., Ungewickell, H., and Ungewickell, E. (1996). Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin. J. Cell Biol. 135, 925-937.
    • (1996) J. Cell Biol. , vol.135 , pp. 925-937
    • Holstein, S.E.H.1    Ungewickell, H.2    Ungewickell, E.3
  • 13
    • 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
  • 14
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates hsp70/hsp90 interactions in protein folding
    • Johnson, B.D., Schumacher, R.J., Ross, E.D., and Toft, D.O. (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
  • 15
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson, J.L., and Craig, E.A. (1997). Protein folding in vivo: unraveling complex pathways. Cell 90, 201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 16
    • 0025740247 scopus 로고
    • A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes
    • Klappa, P., Mayinger, P., Pipkorn, R., Zimmermann, M., and Zimmermann, R. (1991). A microsomal protein is involved In ATP-dependent transport of presecretory proteins into mammalian microsomes. EMBO J. 10, 2795-2803.
    • (1991) EMBO J. , vol.10 , pp. 2795-2803
    • Klappa, P.1    Mayinger, P.2    Pipkorn, R.3    Zimmermann, M.4    Zimmermann, R.5
  • 17
    • 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
  • 19
    • 0031469912 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells
    • Michels, A.A., Kanon, B., Konings, A.W.T., Ohtsuka, K., Bensaude, O., and Kampinga, H.H. (1997). Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J. Biol. Chem. 272, 33283-33289.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33283-33289
    • Michels, A.A.1    Kanon, B.2    Konings, A.W.T.3    Ohtsuka, K.4    Bensaude, O.5    Kampinga, H.H.6
  • 20
    • 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. 277, 19617-19624.
    • (1996) J. Biol. Chem. , vol.277 , pp. 19617-19624
    • Minami, Y.1    Höhfeld, J.2    Ohtsuka, K.3    Hartl, F.-U.4
  • 21
    • 0031466639 scopus 로고    scopus 로고
    • Mammalian cells express two differently localized Bag-1 isoforms generated by alternative initiation
    • Packham, G., Brimmell, M., and Cleveland, J.L. (1997). Mammalian cells express two differently localized Bag-1 isoforms generated by alternative initiation. Biochem. J. 328, 807-813.
    • (1997) Biochem. J. , vol.328 , pp. 807-813
    • Packham, G.1    Brimmell, M.2    Cleveland, J.L.3
  • 22
    • 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, 420-431.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 420-431
    • Prapapanich, V.1    Chen, S.2    Nair, S.C.3    Rimerman, R.A.4    Smith, D.F.5
  • 23
    • 0031931061 scopus 로고    scopus 로고
    • Mutation of Hip's carboxy-terminal region inhibits a transitional stage of progesterone receptor assembly
    • Prapapanich, V., Chen, S., and Smith, D.F. (1998). Mutation of Hip's carboxy-terminal region inhibits a transitional stage of progesterone receptor assembly. Mol. Cell. Biol. 18, 944-952.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 944-952
    • Prapapanich, V.1    Chen, S.2    Smith, D.F.3
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0025006519 scopus 로고
    • A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and post-translationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes
    • Schlenstedt, G., Gudmundsson, G.H., Boman, H.G., and Zimmermann, R. (1990). A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and post-translationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes. J. Biol. Chem. 265, 13960-13968.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13960-13968
    • Schlenstedt, G.1    Gudmundsson, G.H.2    Boman, H.G.3    Zimmermann, R.4
  • 28
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder, H., Langer, T., Hartl, F.-U., and Bukau, B. (1993). DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137-4144.
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.-U.3    Bukau, B.4
  • 30
    • 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
  • 31
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1 : A novel Bcl-2-bindlng 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-bindlng 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
    • 0030830249 scopus 로고    scopus 로고
    • The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding
    • Terada, K., Kanazawa, M., Bukau, B., and Mori, M. (1997). The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell Biol. 139, 1089-1095.
    • (1997) J. Cell Biol. , vol.139 , pp. 1089-1095
    • Terada, K.1    Kanazawa, M.2    Bukau, B.3    Mori, M.4
  • 34
    • 0029847609 scopus 로고    scopus 로고
    • Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate
    • Thulasiraman, V., and Matts, R. L. (1996). Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate. Biochemistry 35, 13443-13450.
    • (1996) Biochemistry , vol.35 , pp. 13443-13450
    • Thulasiraman, V.1    Matts, R.L.2
  • 35
    • 0030766734 scopus 로고    scopus 로고
    • Mammalian protein RAP46; an interaction partner and modulator of 70 kDa heat shock proteins
    • Zeiner, M., Gebauer, M., and Gehring, U. (1997). Mammalian protein RAP46; an interaction partner and modulator of 70 kDa heat shock proteins. EMBO J. 16, 5483-5490.
    • (1997) EMBO J. , vol.16 , pp. 5483-5490
    • Zeiner, M.1    Gebauer, M.2    Gehring, U.3


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