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Volumn 9, Issue 3, 2014, Pages 1135-1150

A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; HUNTINGTIN; POLYGLUTAMINE; PROTEOME; CHAPERONE; HTT PROTEIN, HUMAN; NERVE PROTEIN;

EID: 84919764653     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2014.09.042     Document Type: Article
Times cited : (423)

References (62)
  • 1
    • 77955518815 scopus 로고    scopus 로고
    • Link communities reveal multiscale complexity in networks
    • Ahn, Y.Y., Bagrow, J.P., and Lehmann, S. (2010). Link communities reveal multiscale complexity in networks. Nature 466, 761-764.
    • (2010) Nature , vol.466 , pp. 761-764
    • Ahn, Y.Y.1    Bagrow, J.P.2    Lehmann, S.3
  • 2
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • Albanèse, V., Yam, A.Y., Baughman, J., Parnot, C., and Frydman, J. (2006). Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124, 75-88.
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanèse, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 3
    • 24744467563 scopus 로고    scopus 로고
    • Cdh1/Hct1-APC is essential for the survival of postmitotic neurons
    • Almeida, A., Bolaños, J.P., and Moreno, S. (2005). Cdh1/Hct1-APC is essential for the survival of postmitotic neurons. J. Neurosci. 25, 8115-8121.
    • (2005) J. Neurosci. , vol.25 , pp. 8115-8121
    • Almeida, A.1    Bolaños, J.P.2    Moreno, S.3
  • 4
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W.E., Morimoto, R.I., Dillin, A., and Kelly, J.W. (2008). Adapting proteostasis for disease intervention. Science 319, 916-919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 6
    • 40749152391 scopus 로고    scopus 로고
    • Parkinson's disease: a genetic perspective
    • Belin, A.C., and Westerlund, M. (2008). Parkinson's disease: a genetic perspective. FEBS J. 275, 1377-1383.
    • (2008) FEBS J. , vol.275 , pp. 1377-1383
    • Belin, A.C.1    Westerlund, M.2
  • 7
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • Ben-Zvi, A., Miller, E.A., and Morimoto, R.I. (2009). Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc. Natl. Acad. Sci. USA 106, 14914-14919.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 9
    • 58049217323 scopus 로고    scopus 로고
    • Unexpected link between anaphase promoting complex and the toxicity of expanded polyglutamines expressed in yeast
    • Bocharova, N.A., Sokolov, S.S., Knorre, D.A., Skulachev, V.P., and Severin, F.F. (2008). Unexpected link between anaphase promoting complex and the toxicity of expanded polyglutamines expressed in yeast. Cell Cycle 7, 3943-3946.
    • (2008) Cell Cycle , vol.7 , pp. 3943-3946
    • Bocharova, N.A.1    Sokolov, S.S.2    Knorre, D.A.3    Skulachev, V.P.4    Severin, F.F.5
  • 10
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. (1974). The genetics of Caenorhabditis elegans. Genetics 77, 71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 11
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • Cohen, E., Bieschke, J., Perciavalle, R.M., Kelly, J.W., and Dillin, A. (2006). Opposing activities protect against age-onset proteotoxicity. Science 313, 1604-1610.
    • (2006) Science , vol.313 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 12
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings, C.J., Mancini, M.A., Antalffy, B., DeFranco, D.B., Orr, H.T., and Zoghbi, H.Y. (1998). Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19, 148-154.
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 13
    • 77956362155 scopus 로고    scopus 로고
    • Protein homeostasis and aging in neurodegeneration
    • Douglas, P.M., and Dillin, A. (2010). Protein homeostasis and aging in neurodegeneration. J. Cell Biol. 190, 719-729.
    • (2010) J. Cell Biol. , vol.190 , pp. 719-729
    • Douglas, P.M.1    Dillin, A.2
  • 14
    • 80255122786 scopus 로고    scopus 로고
    • Convergent pathogenic pathways in Alzheimer's and Huntington's diseases: shared targets for drug development
    • Ehrnhoefer, D.E., Wong, B.K.Y., and Hayden, M.R. (2011). Convergent pathogenic pathways in Alzheimer's and Huntington's diseases: shared targets for drug development. Nat. Rev. Drug Discov. 10, 853-867.
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 853-867
    • Ehrnhoefer, D.E.1    Wong, B.K.Y.2    Hayden, M.R.3
  • 16
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • Gidalevitz, T., Ben-Zvi, A., Ho, K.H., Brignull, H.R., and Morimoto, R.I. (2006). Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311, 1471-1474.
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 17
    • 0033613270 scopus 로고    scopus 로고
    • Expression of the CDH1-associated form of the anaphase-promoting complex in postmitotic neurons
    • Gieffers, C., Peters, B.H., Kramer, E.R., Dotti, C.G., and Peters, J.M. (1999). Expression of the CDH1-associated form of the anaphase-promoting complex in postmitotic neurons. Proc. Natl. Acad. Sci. USA 96, 11317-11322.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11317-11322
    • Gieffers, C.1    Peters, B.H.2    Kramer, E.R.3    Dotti, C.G.4    Peters, J.M.5
  • 18
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass, C., and Selkoe, D.J. (2007). Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 8, 101-112.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 21
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl, F.U., and Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 22
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 26
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
    • Jana, N.R., Tanaka, M., Wang, Gh., and Nukina, N. (2000). Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet. 9, 2009-2018.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 27
    • 0038725897 scopus 로고    scopus 로고
    • Genome-wide RNAi screening in Caenorhabditis elegans
    • Kamath, R.S., and Ahringer, J. (2003). Genome-wide RNAi screening in Caenorhabditis elegans. Methods 30, 313-321.
    • (2003) Methods , vol.30 , pp. 313-321
    • Kamath, R.S.1    Ahringer, J.2
  • 28
    • 58249091452 scopus 로고    scopus 로고
    • A centrosomal Cdc20-APC pathway controls dendrite morphogenesis in postmitotic neurons
    • Kim, A.H., Puram, S.V., Bilimoria, P.M., Ikeuchi, Y., Keough, S., Wong, M., Rowitch, D., and Bonni, A. (2009). A centrosomal Cdc20-APC pathway controls dendrite morphogenesis in postmitotic neurons. Cell 136, 322-336.
    • (2009) Cell , vol.136 , pp. 322-336
    • Kim, A.H.1    Puram, S.V.2    Bilimoria, P.M.3    Ikeuchi, Y.4    Keough, S.5    Wong, M.6    Rowitch, D.7    Bonni, A.8
  • 30
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen, B., and Braakman, I. (2004). Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16, 343-349.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 32
    • 1842477303 scopus 로고    scopus 로고
    • A new model for prediction of the age of onset and penetrance for Huntington's disease based on CAG length
    • Langbehn, D.R., Brinkman, R.R., Falush, D., Paulsen, J.S., and Hayden, M.R.; International Huntington's Disease Collaborative Group (2004). A new model for prediction of the age of onset and penetrance for Huntington's disease based on CAG length. Clin. Genet. 65, 267-277.
    • (2004) Clin. Genet. , vol.65 , pp. 267-277
    • Langbehn, D.R.1    Brinkman, R.R.2    Falush, D.3    Paulsen, J.S.4    Hayden, M.R.5
  • 33
    • 51049088378 scopus 로고    scopus 로고
    • The adaptor protein of the anaphase promoting complex Cdh1 is essential in maintaining replicative lifespan and in learning and memory
    • Li, M., Shin, Y.H., Hou, L., Huang, X., Wei, Z., Klann, E., and Zhang, P. (2008). The adaptor protein of the anaphase promoting complex Cdh1 is essential in maintaining replicative lifespan and in learning and memory. Nat. Cell Biol. 10, 1083-1089.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1083-1089
    • Li, M.1    Shin, Y.H.2    Hou, L.3    Huang, X.4    Wei, Z.5    Klann, E.6    Zhang, P.7
  • 35
    • 0028981288 scopus 로고
    • Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans
    • Link, C.D. (1995). Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 92, 9368-9372.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9368-9372
    • Link, C.D.1
  • 39
    • 67649212161 scopus 로고    scopus 로고
    • The APC/C E3 ligase remains active in most post-mitotic Arabidopsis cells and is required for proper vasculature development and organization
    • Marrocco, K., Thomann, A., Parmentier, Y., Genschik, P., and Criqui, M.C. (2009). The APC/C E3 ligase remains active in most post-mitotic Arabidopsis cells and is required for proper vasculature development and organization. Development 136, 1475-1485.
    • (2009) Development , vol.136 , pp. 1475-1485
    • Marrocco, K.1    Thomann, A.2    Parmentier, Y.3    Genschik, P.4    Criqui, M.C.5
  • 40
    • 84884589727 scopus 로고    scopus 로고
    • Hsp70 chaperone dynamics and molecular mechanism
    • Mayer, M.P. (2013). Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem. Sci. 38, 507-514.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 507-514
    • Mayer, M.P.1
  • 41
    • 33644658492 scopus 로고    scopus 로고
    • Whole genome expression profiling of the medial and lateral substantia nigra in Parkinson's disease
    • Moran, L.B., Duke, D.C., Deprez, M., Dexter, D.T., Pearce, R.K., and Graeber, M.B. (2006). Whole genome expression profiling of the medial and lateral substantia nigra in Parkinson's disease. Neurogenetics 7, 1-11.
    • (2006) Neurogenetics , vol.7 , pp. 1-11
    • Moran, L.B.1    Duke, D.C.2    Deprez, M.3    Dexter, D.T.4    Pearce, R.K.5    Graeber, M.B.6
  • 42
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley, J.F., Brignull, H.R., Weyers, J.J., and Morimoto, R.I. (2002). The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 99, 10417-10422.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 45
    • 84879920420 scopus 로고    scopus 로고
    • PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone
    • Park, S.H., Kukushkin, Y., Gupta, R., Chen, T., Konagai, A., Hipp, M.S., Hayer-Hartl, M., and Hartl, F.U. (2013). PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 154, 134-145.
    • (2013) Cell , vol.154 , pp. 134-145
    • Park, S.H.1    Kukushkin, Y.2    Gupta, R.3    Chen, T.4    Konagai, A.5    Hipp, M.S.6    Hayer-Hartl, M.7    Hartl, F.U.8
  • 46
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl, L.H., and Prodromou, C. (2006). Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 47
    • 84875461582 scopus 로고    scopus 로고
    • Diversity in the origins of proteostasis networks-a driver for protein function in evolution
    • Powers, E.T., and Balch, W.E. (2013). Diversity in the origins of proteostasis networks-a driver for protein function in evolution. Nat. Rev. Mol. Cell Biol. 14, 237-248.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 237-248
    • Powers, E.T.1    Balch, W.E.2
  • 48
  • 50
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch, C., Sangster, T.A., and Lindquist, S. (2002). Hsp90 as a capacitor of phenotypic variation. Nature 417, 618-624.
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 51
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford, S.L., and Lindquist, S. (1998). Hsp90 as a capacitor for morphological evolution. Nature 396, 336-342.
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 54
    • 84890203542 scopus 로고    scopus 로고
    • Regulation of proteasome activity in health and disease
    • Schmidt, M., and Finley, D. (2014). Regulation of proteasome activity in health and disease. Biochim. Biophys. Acta 1843, 13-25.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 13-25
    • Schmidt, M.1    Finley, D.2
  • 55
    • 84855258498 scopus 로고    scopus 로고
    • A genetic screening strategy identifies novel regulators of the proteostasis network
    • Silva, M.C., Fox, S., Beam, M., Thakkar, H., Amaral, M.D., and Morimoto, R.I. (2011). A genetic screening strategy identifies novel regulators of the proteostasis network. PLoS Genet. 7, e1002438.
    • (2011) PLoS Genet. , vol.7
    • Silva, M.C.1    Fox, S.2    Beam, M.3    Thakkar, H.4    Amaral, M.D.5    Morimoto, R.I.6
  • 56
    • 79551587720 scopus 로고    scopus 로고
    • Cytoscape 2.8: new features for data integration and network visualization
    • Smoot, M.E., Ono, K., Ruscheinski, J., Wang, P.L., and Ideker, T. (2011). Cytoscape 2.8: new features for data integration and network visualization. Bioinformatics 27, 431-432.
    • (2011) Bioinformatics , vol.27 , pp. 431-432
    • Smoot, M.E.1    Ono, K.2    Ruscheinski, J.3    Wang, P.L.4    Ideker, T.5
  • 57
    • 26644453716 scopus 로고    scopus 로고
    • Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1)
    • Song, Y., and Masison, D.C. (2005). Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1). J. Biol. Chem. 280, 34178-34185.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34178-34185
    • Song, Y.1    Masison, D.C.2
  • 58
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • Tam, S., Geller, R., Spiess, C., and Frydman, J. (2006). The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat. Cell Biol. 8, 1155-1162.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 59
    • 11144336620 scopus 로고    scopus 로고
    • Formation of membrane-bound ring complexes by prohibitins in mitochondria
    • Tatsuta, T., Model, K., and Langer, T. (2005). Formation of membrane-bound ring complexes by prohibitins in mitochondria. Mol. Biol. Cell 16, 248-259.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 248-259
    • Tatsuta, T.1    Model, K.2    Langer, T.3
  • 60
    • 84878873702 scopus 로고    scopus 로고
    • Regulation of organismal proteostasis by transcellular chaperone signaling
    • van Oosten-Hawle, P., Porter, R.S., and Morimoto, R.I. (2013). Regulation of organismal proteostasis by transcellular chaperone signaling. Cell 153, 1366-1378.
    • (2013) Cell , vol.153 , pp. 1366-1378
    • van Oosten-Hawle, P.1    Porter, R.S.2    Morimoto, R.I.3
  • 62
    • 84898779814 scopus 로고    scopus 로고
    • Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition
    • Yu, A., Shibata, Y., Shah, B., Calamini, B., Lo, D.C., and Morimoto, R.I. (2014). Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition. Proc. Natl. Acad. Sci. USA 111, E1481-E1490.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E1481-E1490
    • Yu, A.1    Shibata, Y.2    Shah, B.3    Calamini, B.4    Lo, D.C.5    Morimoto, R.I.6


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