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Volumn 290, Issue 21, 2015, Pages 13115-13127

Isoform-selective genetic inhibition of constitutive cytosolic Hsp70 activity promotes client Tau degradation using an altered co-chaperone complement

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NUCLEOTIDES;

EID: 84929994763     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.637595     Document Type: Article
Times cited : (38)

References (72)
  • 1
    • 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., and Fink, A. L. (1993) ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis. Nature 365, 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
  • 2
    • 0028099817 scopus 로고
    • Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b
    • Cheetham, M. E., Jackson, A. P., and Anderton, B. H. (1994) Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b. Eur. J. Biochem. 226, 99-107
    • (1994) Eur. J. Biochem. , vol.226 , pp. 99-107
    • Cheetham, M.E.1    Jackson, A.P.2    Anderton, B.H.3
  • 3
    • 0038523841 scopus 로고    scopus 로고
    • The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70
    • Wittung-Stafshede, P., Guidry, J., Horne, B. E., and Landry, S. J. (2003) The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70. Biochemistry 42, 4937-4944
    • (2003) Biochemistry , vol.42 , pp. 4937-4944
    • Wittung-Stafshede, P.1    Guidry, J.2    Horne, B.E.3    Landry, S.J.4
  • 4
    • 0027818242 scopus 로고
    • Structure and mechanism of 70-kDa heat-shock-related proteins
    • McKay, D. B. (1993) Structure and mechanism of 70-kDa heat-shock-related proteins. Adv. Protein Chem. 44, 67-98
    • (1993) Adv. Protein Chem. , vol.44 , pp. 67-98
    • McKay, D.B.1
  • 5
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • Mayer, M. P. (2010) Gymnastics of molecular chaperones. Mol. Cell 39, 321-331
    • (2010) Mol. Cell , vol.39 , pp. 321-331
    • Mayer, M.P.1
  • 7
    • 40749101072 scopus 로고    scopus 로고
    • hsp70 genes in the human genome: Conservation and differentiation patterns predict a wide array of overlapping and specialized functions
    • Brocchieri, L., Conway de Macario, E., and Macario, A. J. (2008) hsp70 genes in the human genome: conservation and differentiation patterns predict a wide array of overlapping and specialized functions. BMC Evol. Biol. 8, 19
    • (2008) BMC Evol. Biol. , vol.8 , pp. 19
    • Brocchieri, L.1    Conway De Macario, E.2    Macario, A.J.3
  • 8
    • 0034770879 scopus 로고    scopus 로고
    • Insights into the function of Hsp70 chaperones
    • Zylicz, M., and Wawrzynow, A. (2001) Insights into the function of Hsp70 chaperones. IUBMB life 51, 283-287
    • (2001) IUBMB Life , vol.51 , pp. 283-287
    • Zylicz, M.1    Wawrzynow, A.2
  • 9
    • 0022346828 scopus 로고
    • ATP catalyzes the sequestration of clathrin during enzymatic uncoating
    • Schmid, S. L., Braell, W. A., and Rothman, J. E. (1985) ATP catalyzes the sequestration of clathrin during enzymatic uncoating. J. Biol. Chem. 260, 10057-10062
    • (1985) J. Biol. Chem. , vol.260 , pp. 10057-10062
    • Schmid, S.L.1    Braell, W.A.2    Rothman, J.E.3
  • 11
    • 0023649886 scopus 로고
    • Structure and expression of a human gene coding for a 71-kDa heat shock "cognate" protein
    • Dworniczak, B., and Mirault, M. E. (1987) Structure and expression of a human gene coding for a 71-kDa heat shock "cognate" protein. Nucleic Acids Res. 15, 5181-5197
    • (1987) Nucleic Acids Res. , vol.15 , pp. 5181-5197
    • Dworniczak, B.1    Mirault, M.E.2
  • 12
    • 0030991023 scopus 로고    scopus 로고
    • Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein
    • Chamberlain, L. H., and Burgoyne, R. D. (1997) Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein. Biochem. J. 322, 853-858
    • (1997) Biochem. J. , vol.322 , pp. 853-858
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 13
    • 0034698087 scopus 로고    scopus 로고
    • The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor
    • Rajapandi, T., Greene, L. E., and Eisenberg, E. (2000) The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor. J. Biol. Chem. 275, 22597-22604
    • (2000) J. Biol. Chem. , vol.275 , pp. 22597-22604
    • Rajapandi, T.1    Greene, L.E.2    Eisenberg, E.3
  • 14
    • 19644387113 scopus 로고    scopus 로고
    • Evidence for regulation of ER/Golgi SNARE complex formation by hsc70 chaperones
    • Joglekar, A. P., and Hay, J. C. (2005) Evidence for regulation of ER/Golgi SNARE complex formation by hsc70 chaperones. Eur. J. Cell Biol. 84, 529-542
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 529-542
    • Joglekar, A.P.1    Hay, J.C.2
  • 15
    • 0033566936 scopus 로고    scopus 로고
    • The HSC73 molecular chaperone: Involvement in MHC class II antigen presentation
    • Panjwani, N., Akbari, O., Garcia, S., Brazil, M., and Stockinger, B. (1999) The HSC73 molecular chaperone: involvement in MHC class II antigen presentation. J. Immunol. 163, 1936-1942
    • (1999) J. Immunol. , vol.163 , pp. 1936-1942
    • Panjwani, N.1    Akbari, O.2    Garcia, S.3    Brazil, M.4    Stockinger, B.5
  • 16
    • 56349090843 scopus 로고    scopus 로고
    • Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions
    • Turturici, G., Geraci, F., Candela, M. E., Giudice, G., Gonzalez, F., and Sconzo, G. (2008) Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions. J. Mol. Histol. 39, 571-578
    • (2008) J. Mol. Histol. , vol.39 , pp. 571-578
    • Turturici, G.1    Geraci, F.2    Candela, M.E.3    Giudice, G.4    Gonzalez, F.5    Sconzo, G.6
  • 17
    • 0033710919 scopus 로고    scopus 로고
    • Tubulin and neurofilament proteins are transported differently in axons of chicken motoneurons
    • Yuan, A., Mills, R. G., Chia, C. P., and Bray, J. J. (2000) Tubulin and neurofilament proteins are transported differently in axons of chicken motoneurons. Cell. Mol. Neurobiol. 20, 623-632
    • (2000) Cell. Mol. Neurobiol. , vol.20 , pp. 623-632
    • Yuan, A.1    Mills, R.G.2    Chia, C.P.3    Bray, J.J.4
  • 19
    • 57049139853 scopus 로고    scopus 로고
    • Two motifs within the Tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone
    • Sarkar, M., Kuret, J., and Lee, G. (2008) Two motifs within the Tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone. J. Neurosci. Res. 86, 2763-2773
    • (2008) J. Neurosci. Res. , vol.86 , pp. 2763-2773
    • Sarkar, M.1    Kuret, J.2    Lee, G.3
  • 21
    • 0042924434 scopus 로고    scopus 로고
    • Differential regulation of microtubule dynamics by three- and four-repeat Tau: Implications for the onset of neurodegenerative disease
    • Panda, D., Samuel, J. C., Massie, M., Feinstein, S. C., and Wilson, L. (2003) Differential regulation of microtubule dynamics by three- and four-repeat Tau: implications for the onset of neurodegenerative disease. Proc. Natl. Acad. Sci. U.S.A. 100, 9548-9553
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9548-9553
    • Panda, D.1    Samuel, J.C.2    Massie, M.3    Feinstein, S.C.4    Wilson, L.5
  • 22
    • 2542464892 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics by Tau in living cells: Implications for development and neurodegeneration
    • Bunker, J. M., Wilson, L., Jordan, M. A., and Feinstein, S. C. (2004) Modulation of microtubule dynamics by Tau in living cells: implications for development and neurodegeneration. Mol. Biol. Cell 15, 2720-2728
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2720-2728
    • Bunker, J.M.1    Wilson, L.2    Jordan, M.A.3    Feinstein, S.C.4
  • 24
    • 0009364134 scopus 로고
    • Microtubule-associated protein Tau (Tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik, K. S., Joachim, C. L., and Selkoe, D. J. (1986) Microtubule-associated protein Tau (Tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 83, 4044-4048
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 26
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., and Hyman, B. T. (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42, 631-639
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 29
    • 84879767467 scopus 로고    scopus 로고
    • Synthesis and initial evaluation of YM-08, a blood-brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces Tau levels
    • Miyata, Y., Li, X., Lee, H. F., Jinwal, U. K., Srinivasan, S. R., Seguin, S. P., Young, Z. T., Brodsky, J. L., Dickey, C. A., Sun, D., and Gestwicki, J. E. (2013) Synthesis and initial evaluation of YM-08, a blood-brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces Tau levels. ACS Chem. Neurosci. 4, 930-939
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 930-939
    • Miyata, Y.1    Li, X.2    Lee, H.F.3    Jinwal, U.K.4    Srinivasan, S.R.5    Seguin, S.P.6    Young, Z.T.7    Brodsky, J.L.8    Dickey, C.A.9    Sun, D.10    Gestwicki, J.E.11
  • 31
    • 84896860139 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibitors. 1. 2,5′-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70
    • Kang, Y., Taldone, T., Patel, H. J., Patel, P. D., Rodina, A., Gozman, A., Maharaj, R., Clement, C. C., Patel, M. R., Brodsky, J. L., Young, J. C., and Chiosis, G. (2014) Heat shock protein 70 inhibitors. 1. 2,5′-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70. J. Med. Chem. 57, 1188-1207
    • (2014) J. Med. Chem. , vol.57 , pp. 1188-1207
    • Kang, Y.1    Taldone, T.2    Patel, H.J.3    Patel, P.D.4    Rodina, A.5    Gozman, A.6    Maharaj, R.7    Clement, C.C.8    Patel, M.R.9    Brodsky, J.L.10    Young, J.C.11    Chiosis, G.12
  • 33
    • 79960927001 scopus 로고    scopus 로고
    • Allosteric drugs: The interaction of antitumor compound MKT-077 with human Hsp70 chaperones
    • Rousaki, A., Miyata, Y., Jinwal, U. K., Dickey, C. A., Gestwicki, J. E., and Zuiderweg, E. R. (2011) Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones. J. Mol. Biol. 411, 614-632
    • (2011) J. Mol. Biol. , vol.411 , pp. 614-632
    • Rousaki, A.1    Miyata, Y.2    Jinwal, U.K.3    Dickey, C.A.4    Gestwicki, J.E.5    Zuiderweg, E.R.6
  • 34
    • 84896815426 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibitors. 2. 2,5′-thiodipyrimidines, 5-(phenylthio)pyrimidines, 2-(pyridin-3-ylthio)pyrimidines, and 3-(phenylthio)pyridines as reversible binders to an allosteric site on heat shock protein 70
    • Taldone, T., Kang, Y., Patel, H. J., Patel, M. R., Patel, P. D., Rodina, A., Patel, Y., Gozman, A., Maharaj, R., Clement, C. C., Lu, A., Young, J. C., and Chiosis, G. (2014) Heat shock protein 70 inhibitors. 2. 2,5′-thiodipyrimidines, 5-(phenylthio)pyrimidines, 2-(pyridin-3-ylthio)pyrimidines, and 3-(phenylthio)pyridines as reversible binders to an allosteric site on heat shock protein 70. J. Med. Chem. 57, 1208-1224
    • (2014) J. Med. Chem. , vol.57 , pp. 1208-1224
    • Taldone, T.1    Kang, Y.2    Patel, H.J.3    Patel, M.R.4    Patel, P.D.5    Rodina, A.6    Patel, Y.7    Gozman, A.8    Maharaj, R.9    Clement, C.C.10    Lu, A.11    Young, J.C.12    Chiosis, G.13
  • 35
    • 37549046818 scopus 로고    scopus 로고
    • Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase
    • Wisén, S., Androsavich, J., Evans, C. G., Chang, L., and Gestwicki, J. E. (2008) Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase. Bioorg. Med. Chem. Lett. 18, 60-65
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 60-65
    • Wisén, S.1    Androsavich, J.2    Evans, C.G.3    Chang, L.4    Gestwicki, J.E.5
  • 37
    • 84892653392 scopus 로고    scopus 로고
    • Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro
    • Rauch, J. N., and Gestwicki, J. E. (2014) Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J. Biol. Chem. 289, 1402-1414
    • (2014) J. Biol. Chem. , vol.289 , pp. 1402-1414
    • Rauch, J.N.1    Gestwicki, J.E.2
  • 38
    • 36148989163 scopus 로고    scopus 로고
    • High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
    • Chang, L., Bertelsen, E. B., Wisén, S., Larsen, E. M., Zuiderweg, E. R., and Gestwicki, J. E. (2008) High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. Anal. Biochem. 372, 167-176
    • (2008) Anal. Biochem. , vol.372 , pp. 167-176
    • Chang, L.1    Bertelsen, E.B.2    Wisén, S.3    Larsen, E.M.4    Zuiderweg, E.R.5    Gestwicki, J.E.6
  • 39
    • 78650143677 scopus 로고    scopus 로고
    • High-throughput screen for Escherichia coli heat shock protein 70 (Hsp70/DnaK): ATPase assay in low volume by exploiting energy transfer
    • Miyata, Y., Chang, L., Bainor, A., McQuade, T. J., Walczak, C. P., Zhang, Y., Larsen, M. J., Kirchhoff, P., and Gestwicki, J. E. (2010) High-throughput screen for Escherichia coli heat shock protein 70 (Hsp70/DnaK): ATPase assay in low volume by exploiting energy transfer. J. Biomol. Screen. 15, 1211-1219
    • (2010) J. Biomol. Screen. , vol.15 , pp. 1211-1219
    • Miyata, Y.1    Chang, L.2    Bainor, A.3    McQuade, T.J.4    Walczak, C.P.5    Zhang, Y.6    Larsen, M.J.7    Kirchhoff, P.8    Gestwicki, J.E.9
  • 40
    • 39149117364 scopus 로고    scopus 로고
    • Identification of small molecules that modify the protein folding activity of heat shock protein 70
    • Wisén, S., and Gestwicki, J. E. (2008) Identification of small molecules that modify the protein folding activity of heat shock protein 70. Anal. Biochem. 374, 371-377
    • (2008) Anal. Biochem. , vol.374 , pp. 371-377
    • Wisén, S.1    Gestwicki, J.E.2
  • 41
    • 0001610304 scopus 로고
    • Notes on bias in estimation
    • Quenouille, M. H. (1956) Notes on bias in estimation. Biometrika 43, 353-360, 10.1093/biomet/43.3-4.353
    • (1956) Biometrika , vol.43 , pp. 353-360
    • Quenouille, M.H.1
  • 42
    • 34548851413 scopus 로고    scopus 로고
    • Staining protocol for organotypic hippocampal slice cultures
    • Gogolla, N., Galimberti, I., DePaola, V., and Caroni, P. (2006) Staining protocol for organotypic hippocampal slice cultures. Nat. Protoc. 1, 2452-2456
    • (2006) Nat. Protoc. , vol.1 , pp. 2452-2456
    • Gogolla, N.1    Galimberti, I.2    DePaola, V.3    Caroni, P.4
  • 43
    • 0028240468 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment
    • Flaherty, K. M., Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment. J. Biol. Chem. 269, 12899-12907
    • (1994) J. Biol. Chem. , vol.269 , pp. 12899-12907
    • Flaherty, K.M.1    Wilbanks, S.M.2    DeLuca-Flaherty, C.3    McKay, D.B.4
  • 44
    • 0028287525 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants
    • Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants. J. Biol. Chem. 269, 12893-12898
    • (1994) J. Biol. Chem. , vol.269 , pp. 12893-12898
    • Wilbanks, S.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 45
    • 0033578346 scopus 로고    scopus 로고
    • Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein
    • Johnson, E. R., and McKay, D. B. (1999) Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein. Biochemistry 38, 10823-10830
    • (1999) Biochemistry , vol.38 , pp. 10823-10830
    • Johnson, E.R.1    McKay, D.B.2
  • 46
    • 85056045733 scopus 로고    scopus 로고
    • Development of fluorescence polarization assays for the molecular chaperone Hsp70 family members: Hsp72 and DnaK
    • Ricci, L., and Williams, K. P. (2008) Development of fluorescence polarization assays for the molecular chaperone Hsp70 family members: Hsp72 and DnaK. Curr. Chem. genomics 2, 90-95
    • (2008) Curr. Chem. Genomics , vol.2 , pp. 90-95
    • Ricci, L.1    Williams, K.P.2
  • 47
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • Swain, J. F., Dinler, G., Sivendran, R., Montgomery, D. L., Stotz, M., and Gierasch, L. M. (2007) Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol. Cell 26, 27-39
    • (2007) Mol. Cell , vol.26 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 48
    • 79955565642 scopus 로고    scopus 로고
    • Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
    • Zhuravleva, A., and Gierasch, L. M. (2011) Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc. Natl. Acad. Sci. U.S.A. 108, 6987-6992
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6987-6992
    • Zhuravleva, A.1    Gierasch, L.M.2
  • 51
    • 84864389698 scopus 로고    scopus 로고
    • Degradation of Tau protein by autophagy and proteasomal pathways
    • Wang, Y., and Mandelkow, E. (2012) Degradation of Tau protein by autophagy and proteasomal pathways. Biochem. Soc. Trans. 40, 644-652
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 644-652
    • Wang, Y.1    Mandelkow, E.2
  • 53
    • 0030018744 scopus 로고    scopus 로고
    • Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis
    • O'Brien, M. C., Flaherty, K. M., and McKay, D. B. (1996) Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis. J. Biol. Chem. 271, 15874-15878
    • (1996) J. Biol. Chem. , vol.271 , pp. 15874-15878
    • O'Brien, M.C.1    Flaherty, K.M.2    McKay, D.B.3
  • 54
    • 0027484169 scopus 로고
    • Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis
    • O'Brien, M. C., and McKay, D. B. (1993) Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis. J. Biol. Chem. 268, 24323-24329
    • (1993) J. Biol. Chem. , vol.268 , pp. 24323-24329
    • O'Brien, M.C.1    McKay, D.B.2
  • 55
    • 0026320296 scopus 로고
    • The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein
    • Liberek, K., Skowyra, D., Zylicz, M., Johnson, C., and Georgopoulos, C. (1991) The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J. Biol. Chem. 266, 14491-14496
    • (1991) J. Biol. Chem. , vol.266 , pp. 14491-14496
    • Liberek, K.1    Skowyra, D.2    Zylicz, M.3    Johnson, C.4    Georgopoulos, C.5
  • 56
    • 84870916379 scopus 로고    scopus 로고
    • An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
    • Zhuravleva, A., Clerico, E. M., and Gierasch, L. M. (2012) An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151, 1296-1307
    • (2012) Cell , vol.151 , pp. 1296-1307
    • Zhuravleva, A.1    Clerico, E.M.2    Gierasch, L.M.3
  • 57
    • 84901650125 scopus 로고    scopus 로고
    • ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones
    • General, I. J., Liu, Y., Blackburn, M. E., Mao, W., Gierasch, L. M., and Bahar, I. (2014) ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones. PLoS Comput. Biol. 10, e1003624
    • (2014) PLoS Comput. Biol. , vol.10 , pp. e1003624
    • General, I.J.1    Liu, Y.2    Blackburn, M.E.3    Mao, W.4    Gierasch, L.M.5    Bahar, I.6
  • 58
    • 3142677815 scopus 로고    scopus 로고
    • The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains
    • Zhang, Y., and Zuiderweg, E. R. (2004) The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains. Proc. Natl. Acad. Sci. U.S.A. 101, 10272-10277
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10272-10277
    • Zhang, Y.1    Zuiderweg, E.R.2
  • 60
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • Bertelsen, E. B., Chang, L., Gestwicki, J. E., and Zuiderweg, E. R. (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc. Natl. Acad. Sci. U.S.A. 106, 8471-8476
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.4
  • 61
    • 84871689599 scopus 로고    scopus 로고
    • Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones
    • Kityk, R., Kopp, J., Sinning, I., and Mayer, M. P. (2012) Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol. Cell 48, 863-874
    • (2012) Mol. Cell , vol.48 , pp. 863-874
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 62
    • 77955257617 scopus 로고    scopus 로고
    • CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates
    • Stankiewicz, M., Nikolay, R., Rybin, V., and Mayer, M. P. (2010) CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates. FEBS J. 277, 3353-3367
    • (2010) FEBS J. , vol.277 , pp. 3353-3367
    • Stankiewicz, M.1    Nikolay, R.2    Rybin, V.3    Mayer, M.P.4
  • 64
    • 84879625944 scopus 로고    scopus 로고
    • Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting
    • Shiber, A., Breuer, W., Brandeis, M., and Ravid, T. (2013) Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting. Mol. Biol. Cell 24, 2076-2087
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2076-2087
    • Shiber, A.1    Breuer, W.2    Brandeis, M.3    Ravid, T.4
  • 65
    • 33646255923 scopus 로고    scopus 로고
    • The triage of damaged proteins: Degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones
    • Marques, C., Guo, W., Pereira, P., Taylor, A., Patterson, C., Evans, P. C., and Shang, F. (2006) The triage of damaged proteins: degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones. FASEB J. 20, 741-743
    • (2006) FASEB J. , vol.20 , pp. 741-743
    • Marques, C.1    Guo, W.2    Pereira, P.3    Taylor, A.4    Patterson, C.5    Evans, P.C.6    Shang, F.7
  • 66
    • 0035628187 scopus 로고    scopus 로고
    • A constitutive 70 kDa heat-shock protein is localized on the fibres of spindles and asters at metaphase in an ATP-dependent manner: A new chaperone role is proposed
    • Agueli, C., Geraci, F., Giudice, G., Chimenti, L., Cascino, D., and Sconzo, G. (2001) A constitutive 70 kDa heat-shock protein is localized on the fibres of spindles and asters at metaphase in an ATP-dependent manner: a new chaperone role is proposed. Biochem. J. 360, 413-419
    • (2001) Biochem. J. , vol.360 , pp. 413-419
    • Agueli, C.1    Geraci, F.2    Giudice, G.3    Chimenti, L.4    Cascino, D.5    Sconzo, G.6
  • 67
    • 77149135259 scopus 로고    scopus 로고
    • Kinesin-1/Hsc70-dependent mechanism of slow axonal transport and its relation to fast axonal transport
    • Terada, S., Kinjo, M., Aihara, M., Takei, Y., and Hirokawa, N. (2010) Kinesin-1/Hsc70-dependent mechanism of slow axonal transport and its relation to fast axonal transport. EMBO J. 29, 843-854
    • (2010) EMBO J. , vol.29 , pp. 843-854
    • Terada, S.1    Kinjo, M.2    Aihara, M.3    Takei, Y.4    Hirokawa, N.5
  • 68
    • 0034086882 scopus 로고    scopus 로고
    • Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport
    • Tsai, M. Y., Morfini, G., Szebenyi, G., and Brady, S. T. (2000) Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport. Mol. Biol. Cell 11, 2161-2173
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2161-2173
    • Tsai, M.Y.1    Morfini, G.2    Szebenyi, G.3    Brady, S.T.4
  • 69
    • 77952061607 scopus 로고    scopus 로고
    • Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP
    • Zhang, Y., Liu, R., Ni, M., Gill, P., and Lee, A. S. (2010) Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP. J. Biol. Chem. 285, 15065-15075
    • (2010) J. Biol. Chem. , vol.285 , pp. 15065-15075
    • Zhang, Y.1    Liu, R.2    Ni, M.3    Gill, P.4    Lee, A.S.5
  • 70
    • 49949105827 scopus 로고    scopus 로고
    • The unfolded protein response regulator GRP78/BiP is required for endoplasmic reticulum integrity and stress-induced autophagy in mammalian cells
    • Li, J., Ni, M., Lee, B., Barron, E., Hinton, D. R., and Lee, A. S. (2008) The unfolded protein response regulator GRP78/BiP is required for endoplasmic reticulum integrity and stress-induced autophagy in mammalian cells. Cell Death Differ. 15, 1460-1471
    • (2008) Cell Death Differ. , vol.15 , pp. 1460-1471
    • Li, J.1    Ni, M.2    Lee, B.3    Barron, E.4    Hinton, D.R.5    Lee, A.S.6
  • 71
    • 14244268253 scopus 로고    scopus 로고
    • Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential, and ROS accumulation following glucose deprivation in PC12 cells
    • Liu, Y., Liu, W., Song, X. D., and Zuo, J. (2005) Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential, and ROS accumulation following glucose deprivation in PC12 cells. Mol. Cell. Biochem. 268, 45-51
    • (2005) Mol. Cell. Biochem. , vol.268 , pp. 45-51
    • Liu, Y.1    Liu, W.2    Song, X.D.3    Zuo, J.4


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