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Volumn 330, Issue 1, 2003, Pages 137-144

Modulation of the ATPase cycle of BiP by peptides and proteins

Author keywords

Antibody folding; Hsp70; MAK33; Molecular chaperone; Nucleotide binding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; GLUCOSE REGULATED PROTEIN 78; HEAT SHOCK PROTEIN 70; PEPTIDE DERIVATIVE; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG; ANTIBODY; CARRIER PROTEIN; HEAT SHOCK PROTEIN; MOLECULAR CHAPERONE GRP78; PEPTIDE; PROTEIN;

EID: 0037666981     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00556-4     Document Type: Article
Times cited : (37)

References (51)
  • 1
    • 0031925150 scopus 로고    scopus 로고
    • Hsp70 chaperone systems: Diversity of cellular functions and mechanism of action
    • Mayer M.P., Bukau B. Hsp70 chaperone systems: diversity of cellular functions and mechanism of action. Biol. Chem. 379:1998;261-268.
    • (1998) Biol. Chem. , vol.379 , pp. 261-268
    • Mayer, M.P.1    Bukau, B.2
  • 2
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • Haas I.G., Wabl M. Immunoglobulin heavy chain binding protein. Nature. 306:1983;387-389.
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 3
    • 0017665008 scopus 로고
    • Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoptotein synthesis or glucose deprivation
    • Pouyssegur J., Shiu R.P.C., Pastan I. Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoptotein synthesis or glucose deprivation. Cell. 11:1977;941-947.
    • (1977) Cell , vol.11 , pp. 941-947
    • Pouyssegur, J.1    Shiu, R.P.C.2    Pastan, I.3
  • 4
    • 0026569212 scopus 로고
    • Interaction of BiP with newly synthesized immunoglobulin light chain molecules: Cycles of sequential binding and release
    • Knittler M.R., Haas I.G. Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release. EMBO J. 11:1992;1573-1581.
    • (1992) EMBO J. , vol.11 , pp. 1573-1581
    • Knittler, M.R.1    Haas, I.G.2
  • 5
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
    • Matlack K.E., Misselwitz B., Plath K., Rapoport T.A. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell. 97:1999;553-564.
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 6
    • 0033957668 scopus 로고    scopus 로고
    • Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity
    • Chillaron J., Haas I.G. Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity. Mol. Biol. Cell. 11:2000;217-226.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 217-226
    • Chillaron, J.1    Haas, I.G.2
  • 7
    • 0034694896 scopus 로고    scopus 로고
    • Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast
    • Okamura K., Kimata Y., Higashio H., Tsuru A., Kohno K. Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast. Biochem. Biophys. Res. Commun. 279:2000;445-450.
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 445-450
    • Okamura, K.1    Kimata, Y.2    Higashio, H.3    Tsuru, A.4    Kohno, K.5
  • 8
    • 0029682888 scopus 로고    scopus 로고
    • Protein folding and assembly in the endoplasmic reticulum
    • Wei J., Hendershot L.M. Protein folding and assembly in the endoplasmic reticulum. EXS. 77:1996;41-55.
    • (1996) EXS , vol.77 , pp. 41-55
    • Wei, J.1    Hendershot, L.M.2
  • 9
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick J., Dul J.L., Argon Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature. 370:1994;373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 10
    • 0034703009 scopus 로고    scopus 로고
    • BiP and DI cooperate in the oxidative folding of antibodies in vitro
    • Mayer M., Kies U., Kammermeier R., Buchner J. BiP and DI cooperate in the oxidative folding of antibodies in vitro. J. Biol. Chem. 275:2000;29421-29425.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29421-29425
    • Mayer, M.1    Kies, U.2    Kammermeier, R.3    Buchner, J.4
  • 11
    • 0031038002 scopus 로고    scopus 로고
    • Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding
    • Leitzgen K., Knittler M.R., Haas I.G. Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding. J. Biol. Chem. 272:1997;3117-3123.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3117-3123
    • Leitzgen, K.1    Knittler, M.R.2    Haas, I.G.3
  • 12
    • 0029890917 scopus 로고    scopus 로고
    • Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants
    • Hendershot L., Wei J., Gaut J., Melnick J., Aviel S., Argon Y. Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants. Proc. Natl Acad. Sci. USA. 93:1996;5269-5274.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5269-5274
    • Hendershot, L.1    Wei, J.2    Gaut, J.3    Melnick, J.4    Aviel, S.5    Argon, Y.6
  • 13
    • 0027528476 scopus 로고
    • Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain
    • Gaut J.R., Hendershot L.M. Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain. J. Biol. Chem. 268:1993;7248-7255.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7248-7255
    • Gaut, J.R.1    Hendershot, L.M.2
  • 14
    • 0032838622 scopus 로고    scopus 로고
    • BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly
    • Lee Y.K., Brewer J.W., Hellman R., Hendershot L.M. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Mol. Biol. Cell. 10:1999;2209-2219.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2209-2219
    • Lee, Y.K.1    Brewer, J.W.2    Hellman, R.3    Hendershot, L.M.4
  • 16
    • 0033545187 scopus 로고    scopus 로고
    • The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
    • Hellman R., Vanhove M., Lejeune A., Stevens F.J., Hendershot L.M. The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. J. Cell Biol. 144:1999;21-30.
    • (1999) J. Cell Biol. , vol.144 , pp. 21-30
    • Hellman, R.1    Vanhove, M.2    Lejeune, A.3    Stevens, F.J.4    Hendershot, L.M.5
  • 17
    • 0024400060 scopus 로고
    • Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • Hurtley S.M., Bole D.G., Hoover-Litty H., Helenius A., Copeland C.S. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 108:1989;2117-2126.
    • (1989) J. Cell Biol. , vol.108 , pp. 2117-2126
    • Hurtley, S.M.1    Bole, D.G.2    Hoover-Litty, H.3    Helenius, A.4    Copeland, C.S.5
  • 18
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 19
    • 0029037015 scopus 로고
    • Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication
    • Buchberger A., Theyssen H., Schroder H., McCarty J.S., Virgallita G., Milkereit P., Reinstein J., Bukau B. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270:1995;16903-16910.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Theyssen, H.2    Schroder, H.3    McCarty, J.S.4    Virgallita, G.5    Milkereit, P.6    Reinstein, J.7    Bukau, B.8
  • 20
    • 0035793209 scopus 로고    scopus 로고
    • Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE
    • Groemping Y., Klostermeier D., Herrmann C., Veit T., Seidel R., Reinstein J. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE. J. Mol. Biol. 305:2001;1173-1183.
    • (2001) J. Mol. Biol. , vol.305 , pp. 1173-1183
    • Groemping, Y.1    Klostermeier, D.2    Herrmann, C.3    Veit, T.4    Seidel, R.5    Reinstein, J.6
  • 21
    • 0030945296 scopus 로고    scopus 로고
    • GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism
    • Packschies L., Theyssen H., Buchberger A., Bukau B., Goody R.S., Reinstein J. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry. 36:1997;3417-3422.
    • (1997) Biochemistry , vol.36 , pp. 3417-3422
    • Packschies, L.1    Theyssen, H.2    Buchberger, A.3    Bukau, B.4    Goody, R.S.5    Reinstein, J.6
  • 23
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty J.S., Buchberger A., Reinstein J., Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249:1995;126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 24
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of protein assembly
    • Flynn G.C., Chappell T.G., Rothman J.E. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science. 245:1989;385-390.
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 25
    • 0027818242 scopus 로고
    • Structure and mechanism of 70 kDa heat-shock-related proteins
    • McKay D.B. Structure and mechanism of 70 kDa heat-shock-related proteins. Advan. Protein Chem. 44:1993;67-80.
    • (1993) Advan. Protein Chem. , vol.44 , pp. 67-80
    • McKay, D.B.1
  • 27
    • 0028853568 scopus 로고
    • In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis
    • Wei J., Gaut J.R., Hendershot L.M. In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis. J. Biol. Chem. 270:1995;26677-26682.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26677-26682
    • Wei, J.1    Gaut, J.R.2    Hendershot, L.M.3
  • 28
    • 0036303473 scopus 로고    scopus 로고
    • Interaction of the chaperone BiP with an antibody domain: Implications for the chaperone cycle
    • Knarr G., Kies U., Bell S., Mayer M., Buchner J. Interaction of the chaperone BiP with an antibody domain: implications for the chaperone cycle. J. Mol. Biol. 318:2002;611-620.
    • (2002) J. Mol. Biol. , vol.318 , pp. 611-620
    • Knarr, G.1    Kies, U.2    Bell, S.3    Mayer, M.4    Buchner, J.5
  • 29
    • 0028832266 scopus 로고
    • Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria
    • Wei J., Hendershot L.M. Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria. J. Biol. Chem. 270:1995;26670-26676.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26670-26676
    • Wei, J.1    Hendershot, L.M.2
  • 30
    • 0024325535 scopus 로고
    • Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides
    • Kassenbrock C.K., Kelly R.B. Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides. EMBO J. 8:1989;1461-1467.
    • (1989) EMBO J. , vol.8 , pp. 1461-1467
    • Kassenbrock, C.K.1    Kelly, R.B.2
  • 31
    • 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., McKay D.B. 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. 34:1995;11635-11644.
    • (1995) Biochemistry , vol.34 , pp. 11635-11644
    • Ha, J.-H.1    McKay, D.B.2
  • 32
    • 0027513927 scopus 로고
    • Nucleotide binding properties of bovine brain uncoating ATPase
    • Gao B., Yumiko E., Greene L.E., Eisenberg E. Nucleotide binding properties of bovine brain uncoating ATPase. J. Biol. Chem. 268:1993;8513.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8513
    • Gao, B.1    Yumiko, E.2    Greene, L.E.3    Eisenberg, E.4
  • 33
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn G.C., Pohl J., Flocco M.T., Rothman J.E. Peptide-binding specificity of the molecular chaperone BiP. Nature. 353:1991;726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 34
    • 0029911568 scopus 로고    scopus 로고
    • Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone
    • Takeda S., McKay D.B. Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone. Biochemistry. 35:1996;4636-4644.
    • (1996) Biochemistry , vol.35 , pp. 4636-4644
    • Takeda, S.1    McKay, D.B.2
  • 35
    • 0027426041 scopus 로고
    • ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis
    • Palleros D.R., Reid K.L., Shi L., Welch W.J., Fink A.L. ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis. Nature. 365:1993;664-666.
    • (1993) Nature , vol.365 , pp. 664-666
    • Palleros, D.R.1    Reid, K.L.2    Shi, L.3    Welch, W.J.4    Fink, A.L.5
  • 36
  • 38
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd M.J., Viitanen P.V., Lorimer G.H. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science. 265:1994;659-664.
    • (1994) Science , vol.265 , pp. 659-664
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 39
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • Weissman J.S., Rye H.S., Fenton W.A., Beechem J.M., Horwich A.L. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell. 84:1996;481-490.
    • (1996) Cell , vol.84 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.M.4    Horwich, A.L.5
  • 40
    • 0034617057 scopus 로고    scopus 로고
    • Limits of protein folding inside GroE complexes
    • Grallert H., Rutkat K., Buchner J. Limits of protein folding inside GroE complexes. J. Biol. Chem. 275:2000;20424-20430.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20424-20430
    • Grallert, H.1    Rutkat, K.2    Buchner, J.3
  • 41
    • 0036049850 scopus 로고    scopus 로고
    • The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase?
    • Slepenkov S.V., Witt S.N. The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? Mol. Microbiol. 45:2002;1197-1206.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1197-1206
    • Slepenkov, S.V.1    Witt, S.N.2
  • 42
  • 43
    • 0033569993 scopus 로고    scopus 로고
    • BiP-binding sequences in HIV gp160. Implications for the binding specificity of bip
    • Knarr G., Modrow S., Todd A., Gething M.J., Buchner J. BiP-binding sequences in HIV gp160. Implications for the binding specificity of bip. J. Biol. Chem. 274:1999;29850-29857.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29850-29857
    • Knarr, G.1    Modrow, S.2    Todd, A.3    Gething, M.J.4    Buchner, J.5
  • 45
    • 0035920236 scopus 로고    scopus 로고
    • Characterization of a lidless form of the molecular chaperone DnaK: Deletion of the lid increases peptide on- and off-rate constants
    • Buczynski G., Slepenkov S.V., Sehorn M.G., Witt S.N. Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants. J. Biol. Chem. 276:2001;27231-27236.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27231-27236
    • Buczynski, G.1    Slepenkov, S.V.2    Sehorn, M.G.3    Witt, S.N.4
  • 46
    • 0037044301 scopus 로고    scopus 로고
    • Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state
    • Slepenkov S.V., Witt S.N. Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state. Biochemistry. 41:2002;12224-12235.
    • (2002) Biochemistry , vol.41 , pp. 12224-12235
    • Slepenkov, S.V.1    Witt, S.N.2
  • 48
    • 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., Büttner M., Valencia A., Bukau B. A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Struct. Biol. 1:1994;95-101.
    • (1994) Struct. Biol. , vol.1 , pp. 95-101
    • Buchberger, A.1    Schröder, H.2    Büttner, M.3    Valencia, A.4    Bukau, B.5
  • 50
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • McCarty J.S., Walker G.C. DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc. Natl Acad. Sci. USA. 88:1991;9513-9517.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9513-9517
    • McCarty, J.S.1    Walker, G.C.2
  • 51
    • 0027519155 scopus 로고
    • Aspartyl residue 10 is essential for ATPase activity of rat hsc70
    • Huang S., Tsai M.Y., Tzou W., Wang C. Aspartyl residue 10 is essential for ATPase activity of rat hsc70. J. Biol. Chem. 268:1993;2063-2086.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2063-2086
    • Huang, S.1    Tsai, M.Y.2    Tzou, W.3    Wang, C.4


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