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Volumn 7, Issue 10, 2012, Pages 1677-1686

Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 2; CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; INTERLEUKIN ENHANCER BINDING FACTOR 3; NUCLEIC ACID BINDING PROTEIN; PROTEOME; TAU PROTEIN; TRANSCRIPTION FACTOR NFAT; UNCLASSIFIED DRUG; PROTEIN BINDING;

EID: 84867809427     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb3002599     Document Type: Article
Times cited : (63)

References (61)
  • 1
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel, D. N., Hyman, A. A., Cobb, M. H., and Kirschner, M. W. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau Mol. Biol. Cell 3, 1141-1154
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 2
    • 0022395021 scopus 로고
    • Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors
    • Drubin, D. G., Feinstein, S. C., Shooter, E. M., and Kirschner, M. W. (1985) Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors J. Cell Biol. 101, 1799-1807
    • (1985) J. Cell Biol. , vol.101 , pp. 1799-1807
    • Drubin, D.G.1    Feinstein, S.C.2    Shooter, E.M.3    Kirschner, M.W.4
  • 3
    • 0029812945 scopus 로고    scopus 로고
    • Tau binds to the distal axon early in development of polarity in a microtubule- and microfilament-dependent manner
    • Kempf, M., Clement, A., Faissner, A., Lee, G., and Brandt, R. (1996) Tau binds to the distal axon early in development of polarity in a microtubule- and microfilament-dependent manner J. Neurosci. 16, 5583-5592
    • (1996) J. Neurosci. , vol.16 , pp. 5583-5592
    • Kempf, M.1    Clement, A.2    Faissner, A.3    Lee, G.4    Brandt, R.5
  • 4
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E. M., and Mandelkow, E. (1997) MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption Cell 89, 297-308
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 5
    • 0003374626 scopus 로고    scopus 로고
    • Tau protein pathology in neurodegenerative diseases
    • Spillantini, M. G. and Goedert, M. (1998) Tau protein pathology in neurodegenerative diseases Trends Neurosci. 21, 428-433
    • (1998) Trends Neurosci. , vol.21 , pp. 428-433
    • Spillantini, M.G.1    Goedert, M.2
  • 6
    • 33748372746 scopus 로고    scopus 로고
    • Tauopathies: Classification and clinical update on neurodegenerative diseases associated with microtubule-associated protein tau
    • Williams, D. R. (2006) Tauopathies: classification and clinical update on neurodegenerative diseases associated with microtubule-associated protein tau Int. Med. J. 36, 652-660
    • (2006) Int. Med. J. , vol.36 , pp. 652-660
    • Williams, D.R.1
  • 7
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimerâ's disease
    • Kidd, M. (1963) Paired helical filaments in electron microscopy of Alzheimerâ's disease Nature 197, 192-193
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 11
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimerâ's disease mouse model
    • Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G. Q., and Mucke, L. (2007) Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimerâ's disease mouse model Science 316, 750-754
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6    Gerstein, H.7    Yu, G.Q.8    Mucke, L.9
  • 16
    • 80052488572 scopus 로고    scopus 로고
    • Molecular chaperones and regulation of tau quality control: Strategies for drug discovery in tauopathies
    • Miyata, Y., Koren, J., Kiray, J., Dickey, C. A., and Gestwicki, J. E. (2011) Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies Future Med. Chem. 3, 1523-1537
    • (2011) Future Med. Chem. , vol.3 , pp. 1523-1537
    • Miyata, Y.1    Koren, J.2    Kiray, J.3    Dickey, C.A.4    Gestwicki, J.E.5
  • 22
    • 2342444942 scopus 로고    scopus 로고
    • Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival
    • Shimura, H., Miura-Shimura, Y., and Kosik, K. S. (2004) Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival J. Biol. Chem. 279, 17957-17962
    • (2004) J. Biol. Chem. , vol.279 , pp. 17957-17962
    • Shimura, H.1    Miura-Shimura, Y.2    Kosik, K.S.3
  • 23
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky, V. N., Oldfield, C. J., and Dunker, A. K. (2008) Intrinsically disordered proteins in human diseases: introducing the D2 concept Annu. Rev. Biophys. 37, 215-246
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 24
    • 77952332824 scopus 로고    scopus 로고
    • Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation
    • Wang, A. M., Morishima, Y., Clapp, K. M., Peng, H. M., Pratt, W. B., Gestwicki, J. E., Osawa, Y., and Lieberman, A. P. (2010) Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation J. Biol. Chem. 285, 15714-15723
    • (2010) J. Biol. Chem. , vol.285 , pp. 15714-15723
    • Wang, A.M.1    Morishima, Y.2    Clapp, K.M.3    Peng, H.M.4    Pratt, W.B.5    Gestwicki, J.E.6    Osawa, Y.7    Lieberman, A.P.8
  • 25
    • 35949001344 scopus 로고    scopus 로고
    • Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila
    • Bilen, J. and Bonini, N. M. (2007) Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila PLoS Genet. 3, 1950-1964
    • (2007) PLoS Genet. , vol.3 , pp. 1950-1964
    • Bilen, J.1    Bonini, N.M.2
  • 26
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman, J. M. and Feany, M. B. (2003) Genetic modifiers of tauopathy in Drosophila Genetics 165, 1233-1242
    • (2003) Genetics , vol.165 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 27
    • 33846651282 scopus 로고    scopus 로고
    • Molecular chaperones and protein kinase quality control
    • Caplan, A. J., Mandal, A. K., and Theodoraki, M. A. (2007) Molecular chaperones and protein kinase quality control Trends Cell Biol. 17, 87-92
    • (2007) Trends Cell Biol. , vol.17 , pp. 87-92
    • Caplan, A.J.1    Mandal, A.K.2    Theodoraki, M.A.3
  • 29
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan, A. J., Scott, M. D., and Frydman, J. (2005) Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways Cell 121, 739-748
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 30
    • 0035816574 scopus 로고    scopus 로고
    • Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70
    • Gusarova, V., Caplan, A. J., Brodsky, J. L., and Fisher, E. A. (2001) Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70 J. Biol. Chem. 276, 24891-24900
    • (2001) J. Biol. Chem. , vol.276 , pp. 24891-24900
    • Gusarova, V.1    Caplan, A.J.2    Brodsky, J.L.3    Fisher, E.A.4
  • 33
    • 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
  • 34
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rudiger, S., Germeroth, L., Schneider-Mergener, J., and Bukau, B. (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries EMBO J. 16, 1501-1507
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 35
    • 1242341923 scopus 로고    scopus 로고
    • Incipient Alzheimerâ's disease: Microarray correlation analyses reveal major transcriptional and tumor suppressor responses
    • Blalock, E. M., Geddes, J. W., Chen, K. C., Porter, N. M., Markesbery, W. R., and Landfield, P. W. (2004) Incipient Alzheimerâ's disease: microarray correlation analyses reveal major transcriptional and tumor suppressor responses Proc. Natl. Acad. Sci. U.S.A. 101, 2173-2178
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2173-2178
    • Blalock, E.M.1    Geddes, J.W.2    Chen, K.C.3    Porter, N.M.4    Markesbery, W.R.5    Landfield, P.W.6
  • 38
    • 69549135264 scopus 로고    scopus 로고
    • Methylene blue and Alzheimerâ's disease
    • Oz, M., Lorke, D. E., and Petroianu, G. A. (2009) Methylene blue and Alzheimerâ's disease Biochem. Pharmacol. 78, 927-932
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 927-932
    • Oz, M.1    Lorke, D.E.2    Petroianu, G.A.3
  • 40
    • 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
  • 41
    • 0034674783 scopus 로고    scopus 로고
    • Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket
    • Morishima, Y., Murphy, P. J., Li, D. P., Sanchez, E. R., and Pratt, W. B. (2000) Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket J. Biol. Chem. 275, 18054-18060
    • (2000) J. Biol. Chem. , vol.275 , pp. 18054-18060
    • Morishima, Y.1    Murphy, P.J.2    Li, D.P.3    Sanchez, E.R.4    Pratt, W.B.5
  • 44
    • 33646246733 scopus 로고    scopus 로고
    • HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites
    • Dickey, C. A., Dunmore, J., Lu, B., Wang, J. W., Lee, W. C., Kamal, A., Burrows, F., Eckman, C., Hutton, M., and Petrucelli, L. (2006) HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites FASEB J. 20, 753-755
    • (2006) FASEB J. , vol.20 , pp. 753-755
    • Dickey, C.A.1    Dunmore, J.2    Lu, B.3    Wang, J.W.4    Lee, W.C.5    Kamal, A.6    Burrows, F.7    Eckman, C.8    Hutton, M.9    Petrucelli, L.10
  • 50
    • 54949129419 scopus 로고    scopus 로고
    • ProteoWizard: Open source software for rapid proteomics tools development
    • Kessner, D., Chambers, M., Burke, R., Agus, D., and Mallick, P. (2008) ProteoWizard: open source software for rapid proteomics tools development Bioinformatics 24, 2534-2536
    • (2008) Bioinformatics , vol.24 , pp. 2534-2536
    • Kessner, D.1    Chambers, M.2    Burke, R.3    Agus, D.4    Mallick, P.5
  • 51
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • Craig, R. and Beavis, R. C. (2004) TANDEM: matching proteins with tandem mass spectra Bioinformatics 20, 1466-1467
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 52
    • 33750979860 scopus 로고    scopus 로고
    • General framework for developing and evaluating database scoring algorithms using the TANDEM search engine
    • MacLean, B., Eng, J. K., Beavis, R. C., and McIntosh, M. (2006) General framework for developing and evaluating database scoring algorithms using the TANDEM search engine Bioinformatics 22, 2830-2832
    • (2006) Bioinformatics , vol.22 , pp. 2830-2832
    • MacLean, B.1    Eng, J.K.2    Beavis, R.C.3    McIntosh, M.4
  • 53
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search Anal. Chem. 74, 5383-5392
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 54
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., Kolker, E., and Aebersold, R. (2003) A statistical model for identifying proteins by tandem mass spectrometry Anal. Chem. 75, 4646-4658
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 55
    • 79953062776 scopus 로고    scopus 로고
    • Abacus: A computational tool for extracting and pre-processing spectral count data for label-free quantitative proteomic analysis
    • Fermin, D., Basrur, V., Yocum, A. K., and Nesvizhskii, A. I. (2011) Abacus: a computational tool for extracting and pre-processing spectral count data for label-free quantitative proteomic analysis Proteomics 11, 1340-1345
    • (2011) Proteomics , vol.11 , pp. 1340-1345
    • Fermin, D.1    Basrur, V.2    Yocum, A.K.3    Nesvizhskii, A.I.4
  • 56
    • 58149299336 scopus 로고    scopus 로고
    • Significance analysis of spectral count data in label-free shotgun proteomics
    • Choi, H., Fermin, D., and Nesvizhskii, A. I. (2008) Significance analysis of spectral count data in label-free shotgun proteomics Mol. Cell. Proteomics 7, 2373-2385
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2373-2385
    • Choi, H.1    Fermin, D.2    Nesvizhskii, A.I.3
  • 57
    • 77954377096 scopus 로고    scopus 로고
    • Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)
    • Chang, L., Thompson, A. D., Ung, P., Carlson, H. A., and Gestwicki, J. E. (2010) Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK) J. Biol. Chem. 285, 21282-21291
    • (2010) J. Biol. Chem. , vol.285 , pp. 21282-21291
    • Chang, L.1    Thompson, A.D.2    Ung, P.3    Carlson, H.A.4    Gestwicki, J.E.5
  • 58
    • 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., Wisen, 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    Wisen, S.3    Larsen, E.M.4    Zuiderweg, E.R.5    Gestwicki, J.E.6
  • 59
    • 56849131626 scopus 로고    scopus 로고
    • Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
    • Southworth, D. R. and Agard, D. A. (2008) Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle Mol. Cell 32, 631-640
    • (2008) Mol. Cell , vol.32 , pp. 631-640
    • Southworth, D.R.1    Agard, D.A.2
  • 60
    • 22844445324 scopus 로고    scopus 로고
    • Purification of recombinant tau protein and preparation of Alzheimer-paired helical filaments in vitro
    • Barghorn, S., Biernat, J., and Mandelkow, E. (2005) Purification of recombinant tau protein and preparation of Alzheimer-paired helical filaments in vitro Methods Mol. Biol. 299, 35-51
    • (2005) Methods Mol. Biol. , vol.299 , pp. 35-51
    • Barghorn, S.1    Biernat, J.2    Mandelkow, E.3
  • 61
    • 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. Screening 15, 1211-1219
    • (2010) J. Biomol. Screening , 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


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