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Volumn 68, Issue 12, 2011, Pages 2115-2127

Amyloid β-induced FOXRED2 mediates neuronal cell death via inhibition of proteasome activity

Author keywords

Amyloid beta; Cell death; ER stress; FOXRED2; Proteasome

Indexed keywords

AMYLOID BETA PROTEIN; CASPASE 12; CELL PROTEIN; DNA 26S; PROTEASOME; PROTEIN FOXRED2; SALUBRINAL; UNCLASSIFIED DRUG;

EID: 79958272314     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-010-0561-x     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 35748959676 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in health and disease of the nervous system
    • DOI 10.1016/j.tins.2007.08.005, PII S0166223607002457
    • AN Hegde SC Upadhya 2007 The ubiquitin-proteasome pathway in health and disease of the nervous system Trends Neurosci 30 587 595 10.1016/j.tins.2007.08. 005 17950927 10.1016/j.tins.2007.08.005 1:CAS:528:DC%2BD2sXht12gu7bJ (Pubitemid 350051423)
    • (2007) Trends in Neurosciences , vol.30 , Issue.11 , pp. 587-595
    • Hegde, A.N.1    Upadhya, S.C.2
  • 2
    • 77955302229 scopus 로고    scopus 로고
    • PAC1 gene knockout reveals an essential role of chaperone-mediated 20S proteasome biogenesis and latent 20S proteasomes in cellular homeostasis
    • 10.1128/MCB.00216-10 20498273 10.1128/MCB.00216-10 1:CAS:528: DC%2BC3cXhtVOlsLjO
    • K Sasaki J Hamazaki M Koike Y Hirano M Komatsu Y Uchiyama K Tanaka S Murata 2010 PAC1 gene knockout reveals an essential role of chaperone-mediated 20S proteasome biogenesis and latent 20S proteasomes in cellular homeostasis Mol Cell Biol 30 3864 3874 10.1128/MCB.00216-10 20498273 10.1128/MCB.00216-10 1:CAS:528:DC%2BC3cXhtVOlsLjO
    • (2010) Mol Cell Biol , vol.30 , pp. 3864-3874
    • Sasaki, K.1    Hamazaki, J.2    Koike, M.3    Hirano, Y.4    Komatsu, M.5    Uchiyama, Y.6    Tanaka, K.7    Murata, S.8
  • 3
    • 34547838178 scopus 로고    scopus 로고
    • 20S Proteasome Assembly Is Orchestrated by Two Distinct Pairs of Chaperones in Yeast and in Mammals
    • DOI 10.1016/j.molcel.2007.06.025, PII S1097276507004157
    • B Le Tallec MB Barrault R Courbeyrette R Guérois MC Marsolier-Kergoat A Peyroche 2007 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals Mol Cell 27 660 674 10.1016/j.molcel.2007.06.025 17707236 10.1016/j.molcel.2007.06.025 1:CAS:528:DC%2BD2sXhtVSmtLrM (Pubitemid 47243701)
    • (2007) Molecular Cell , vol.27 , Issue.4 , pp. 660-674
    • Le Tallec, B.1    Barrault, M.-B.2    Courbeyrette, R.3    Guerois, R.4    Marsolier-Kergoat, M.-C.5    Peyroche, A.6
  • 4
    • 67649654465 scopus 로고    scopus 로고
    • Getting to first base in proteasome assembly
    • 10.1016/j.cell.2009.06.035 19596233 10.1016/j.cell.2009.06.035 1:CAS:528:DC%2BD1MXps1ygtbc%3D
    • HC Besche A Peth AL Goldberg 2009 Getting to first base in proteasome assembly Cell 138 25 28 10.1016/j.cell.2009.06.035 19596233 10.1016/j.cell.2009. 06.035 1:CAS:528:DC%2BD1MXps1ygtbc%3D
    • (2009) Cell , vol.138 , pp. 25-28
    • Besche, H.C.1    Peth, A.2    Goldberg, A.L.3
  • 5
    • 57649146490 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes
    • 10.1002/pmic.200800387 19003867 10.1002/pmic.200800387 1:CAS:528:DC%2BD1MXlsFensw%3D%3D
    • C Zong GW Young Y Wang H Lu N Deng O Drews P Ping 2008 Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes Proteomics 8 5025 5037 10.1002/pmic.200800387 19003867 10.1002/pmic.200800387 1:CAS:528:DC%2BD1MXlsFensw%3D%3D
    • (2008) Proteomics , vol.8 , pp. 5025-5037
    • Zong, C.1    Young, G.W.2    Wang, Y.3    Lu, H.4    Deng, N.5    Drews, O.6    Ping, P.7
  • 6
    • 58849143335 scopus 로고    scopus 로고
    • Accumulated amyloid-β peptide and hyperphosphorylated tau protein: Relationship and links in Alzheimer's disease
    • 10.3233/JAD-2009-0960 19158417 1:CAS:528:DC%2BD1MXjt1Siu7Y%3D
    • HC Huang ZF Jiang 2009 Accumulated amyloid-β peptide and hyperphosphorylated tau protein: relationship and links in Alzheimer's disease J Alzheimers Dis 16 15 27 10.3233/JAD-2009-0960 19158417 1:CAS:528: DC%2BD1MXjt1Siu7Y%3D
    • (2009) J Alzheimers Dis , vol.16 , pp. 15-27
    • Huang, H.C.1    Jiang, Z.F.2
  • 11
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulum-associated degradation
    • 10.1093/jb/mvp194 19923195 10.1093/jb/mvp194 1:CAS:528: DC%2BC3cXkt1KnsQ%3D%3D
    • J Hoseki R Ushioda K Nagata 2010 Mechanism and components of endoplasmic reticulum-associated degradation J Biochem 147 19 25 10.1093/jb/mvp194 19923195 10.1093/jb/mvp194 1:CAS:528:DC%2BC3cXkt1KnsQ%3D%3D
    • (2010) J Biochem , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 12
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: Disease relevance and therapeutic opportunities
    • 10.1038/nrd2755 19043451 10.1038/nrd2755 1:CAS:528:DC%2BD1cXhsVenu7%2FM
    • I Kim W Xu JC Reed 2008 Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities Nat Rev Drug Discov 7 1013 1030 10.1038/nrd2755 19043451 10.1038/nrd2755 1:CAS:528:DC%2BD1cXhsVenu7%2FM
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 13
    • 33645141853 scopus 로고    scopus 로고
    • ER stress and neurodegenerative diseases
    • 10.1038/sj.cdd.4401778 16397584 10.1038/sj.cdd.4401778 1:CAS:528:DC%2BD28Xhtl2mt7o%3D
    • D Lindholm H Wootz L Korhonen 2006 ER stress and neurodegenerative diseases Cell Death Differ 13 385 392 10.1038/sj.cdd.4401778 16397584 10.1038/sj.cdd.4401778 1:CAS:528:DC%2BD28Xhtl2mt7o%3D
    • (2006) Cell Death Differ , vol.13 , pp. 385-392
    • Lindholm, D.1    Wootz, H.2    Korhonen, L.3
  • 15
    • 77949764687 scopus 로고    scopus 로고
    • Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-β generation
    • 10.1523/JNEUROSCI.2422-09.2010 20237263 10.1523/JNEUROSCI.2422-09.2010 1:CAS:528:DC%2BC3cXlvVant7k%3D
    • M Kaneko H Koike R Saito Y Kitamura Y Okuma Y Nomura 2010 Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-β generation J Neurosci 30 3924 3932 10.1523/JNEUROSCI.2422-09. 2010 20237263 10.1523/JNEUROSCI.2422-09.2010 1:CAS:528:DC%2BC3cXlvVant7k%3D
    • (2010) J Neurosci , vol.30 , pp. 3924-3932
    • Kaneko, M.1    Koike, H.2    Saito, R.3    Kitamura, Y.4    Okuma, Y.5    Nomura, Y.6
  • 16
    • 37249041127 scopus 로고    scopus 로고
    • A molecular specificity code for the three mammalian KDEL receptors
    • DOI 10.1083/jcb.200705180
    • I Raykhel H Alanen K Salo J Jurvansuu VD Nguyen M Latva-Ranta L Ruddock 2007 A molecular specificity code for the three mammalian KDEL receptors J Cell Biol 179 1193 1204 10.1083/jcb.200705180 18086916 10.1083/jcb.200705180 1:CAS:528:DC%2BD2sXhsVOgtL7L (Pubitemid 350277738)
    • (2007) Journal of Cell Biology , vol.179 , Issue.6 , pp. 1193-1204
    • Raykhel, I.1    Alanen, H.2    Salo, K.3    Jurvansuu, J.4    Van, D.N.5    Latva-Ranta, M.6    Ruddock, L.7
  • 17
    • 70349287642 scopus 로고    scopus 로고
    • A luminal flavoprotein in endoplasmic reticulum-associated degradation
    • 10.1073/pnas.0900742106 19706418 10.1073/pnas.0900742106 1:CAS:528:DC%2BD1MXhtFGrt77L
    • J Riemer C Appenzeller-Herzog L Johansson B Bodenmiller R Hartmann-Petersen L Ellgaard 2009 A luminal flavoprotein in endoplasmic reticulum-associated degradation Proc Natl Acad Sci USA 106 14831 14836 10.1073/pnas.0900742106 19706418 10.1073/pnas.0900742106 1:CAS:528: DC%2BD1MXhtFGrt77L
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14831-14836
    • Riemer, J.1    Appenzeller-Herzog, C.2    Johansson, L.3    Bodenmiller, B.4    Hartmann-Petersen, R.5    Ellgaard, L.6
  • 18
    • 27644576445 scopus 로고    scopus 로고
    • Characterization of the proteasome using native gel electrophoresis
    • DOI 10.1016/S0076-6879(05)98029-4, PII S0076687905980294, Ubiquitin and Protein Degradation (Part A)
    • S Elsasser M Schmidt D Finley 2005 Characterization of the proteasome using native gel electrophoresis Methods Enzymol 398 353 363 10.1016/S0076-6879(05)98029-4 16275342 10.1016/S0076-6879(05)98029-4 1:CAS:528:DC%2BD28Xot1ajs7o%3D (Pubitemid 41578897)
    • (2005) Methods in Enzymology , vol.398 , pp. 353-363
    • Elsasser, S.1    Schmidt, M.2    Finley, D.3
  • 19
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • DOI 10.1093/emboj/17.10.2759
    • T Gilon O Chomsky RG Kulka 1998 Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae EMBO J 17 2759 2766 10.1093/emboj/17.10. 2759 9582269 10.1093/emboj/17.10.2759 1:CAS:528:DyaK1cXjslyksrc%3D (Pubitemid 28227122)
    • (1998) EMBO Journal , vol.17 , Issue.10 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 21
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • DOI 10.1016/j.molcel.2004.12.021, PII S1097276505010087
    • EJ Bennett NF Bence R Jayakumar RR Kopito 2005 Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation Molecular Cell 17 351 365 10.1016/j.molcel. 2004.12.021 15694337 10.1016/j.molcel.2004.12.021 1:CAS:528:DC%2BD2MXhs1OitrY%3D (Pubitemid 40193307)
    • (2005) Molecular Cell , vol.17 , Issue.3 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 22
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • M Glotzer AW Murray MW Kirschner 1991 Cyclin is degraded by the ubiquitin pathway Nature 349 132 138 10.1038/349132a0 1846030 10.1038/349132a0 1:CAS:528:DyaK3MXps12jtA%3D%3D (Pubitemid 21912025)
    • (1991) Nature , vol.349 , Issue.6305 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 23
    • 0034654399 scopus 로고    scopus 로고
    • The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1
    • CM Pfleger MW Kirschner 2000 The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1 Genes Dev 14 655 665 10733526 1:CAS:528:DC%2BD3cXisVShu7o%3D (Pubitemid 30176820)
    • (2000) Genes and Development , vol.14 , Issue.6 , pp. 655-665
    • Pfleger, C.M.1    Kirschner, M.W.2
  • 24
    • 0141704418 scopus 로고    scopus 로고
    • The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites
    • DOI 10.1074/jbc.M303725200
    • AF Kisselev M Garcia-Calvo HS Overkleeft E Peterson MW Pennington HL Ploegh NA Thornberry AL Goldberg 2003 The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites J Biol Chem 278 35869 35877 10.1074/jbc.M303725200 12815064 10.1074/jbc.M303725200 1:CAS:528: DC%2BD3sXnt1aqtL4%3D (Pubitemid 37139904)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 35869-35877
    • Kisselev, A.F.1    Garcia-Calvo, M.2    Overkleeft, H.S.3    Peterson, E.4    Pennington, M.W.5    Ploegh, H.L.6    Thornberry, N.A.7    Goldberg, A.L.8
  • 25
    • 0142093671 scopus 로고    scopus 로고
    • Pael receptor, endoplasmic reticulum stress, and Parkinson's disease
    • III25-29. doi: 10.1007/s00415-003-1305-8
    • Takahashi R, Imai Y (2003) Pael receptor, endoplasmic reticulum stress, and Parkinson's disease. J Neurol 250 [Suppl 3]:III25-29. doi: 10.1007/s00415-003-1305-8
    • (2003) J Neurol , vol.250 , Issue.SUPPL. 3
    • Takahashi, R.1    Imai, Y.2
  • 26
    • 62749084512 scopus 로고    scopus 로고
    • Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-induced cell death signalling
    • 19090789 10.1042/BJ20081212 1:CAS:528:DC%2BD1MXjtVShu7k%3D
    • A Rossin M Derouet F Abdel-Sater AO Hueber 2009 Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-induced cell death signalling Biochem J 419 185 192 19090789 10.1042/BJ20081212 1:CAS:528:DC%2BD1MXjtVShu7k%3D
    • (2009) Biochem J , vol.419 , pp. 185-192
    • Rossin, A.1    Derouet, M.2    Abdel-Sater, F.3    Hueber, A.O.4
  • 27
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • DOI 10.1146/annurev.biochem.75.103004.142539
    • U Brandt 2006 Energy converting NADH:quinone oxidoreductase (complex I) Annu Rev Biochem 75 69 92 16756485 10.1146/annurev.biochem.75.103004.142539 1:CAS:528:DC%2BD28XosVKhsr0%3D (Pubitemid 44118026)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 69-92
    • Brandt, U.1
  • 28
    • 34247863874 scopus 로고    scopus 로고
    • Mitotic regulation of the anaphase-promoting complex
    • DOI 10.1007/s00018-007-6443-1
    • DJ Baker MM Dawlaty P Galardy JM van Deursen 2007 Mitotic regulation of the anaphase-promoting complex Cell Mol Life Sci 64 589 600 10.1007/s00018-007- 6443-1 17334950 10.1007/s00018-007-6443-1 1:CAS:528:DC%2BD2sXktVOhtLc%3D (Pubitemid 46712467)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.5 , pp. 589-600
    • Baker, D.J.1    Dawlaty, M.M.2    Galardy, P.3    Van Deursen, J.M.4
  • 29
    • 49849098630 scopus 로고    scopus 로고
    • Regulation of APC/C activators in mitosis and meiosis
    • 18598214 10.1146/annurev.cellbio.041408.115949 1:CAS:528: DC%2BD1cXhtlOgtbfO
    • JA Pesin TL Orr-Weaver 2008 Regulation of APC/C activators in mitosis and meiosis Annu Rev Cell Dev Biol 24 475 499 18598214 10.1146/annurev.cellbio. 041408.115949 1:CAS:528:DC%2BD1cXhtlOgtbfO
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 475-499
    • Pesin, J.A.1    Orr-Weaver, T.L.2
  • 30
    • 76449096769 scopus 로고    scopus 로고
    • The anaphase-promoting complex/cyclosome (APC/C): Cell-cycle-dependent and -independent functions
    • 20074037 10.1042/BST0380065 1:CAS:528:DC%2BC3cXotVKjuw%3D%3D
    • E Manchado M Eguren M Malumbres 2010 The anaphase-promoting complex/cyclosome (APC/C): cell-cycle-dependent and -independent functions Biochem Soc Trans 38 65 71 20074037 10.1042/BST0380065 1:CAS:528: DC%2BC3cXotVKjuw%3D%3D
    • (2010) Biochem Soc Trans , vol.38 , pp. 65-71
    • Manchado, E.1    Eguren, M.2    Malumbres, M.3
  • 31
    • 54249140938 scopus 로고    scopus 로고
    • Do amyloid oligomers act as traps for misfolded oroteins? A hypothesis
    • 18925454 10.1080/13506120802193746 1:CAS:528:DC%2BD1cXht1KntLrF
    • JM Gruschus 2008 Do amyloid oligomers act as traps for misfolded oroteins? A hypothesis Amyloid 15 160 165 18925454 10.1080/13506120802193746 1:CAS:528:DC%2BD1cXht1KntLrF
    • (2008) Amyloid , vol.15 , pp. 160-165
    • Gruschus, J.M.1
  • 34
    • 0033618256 scopus 로고    scopus 로고
    • Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast
    • DOI 10.1074/jbc.274.31.21943
    • SJ Russell KA Steger SA Johnston 1999 Subcellular Localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast J Biol Chem 274 21943 21952 10.1074/jbc.274.31.21943 10419517 10.1074/jbc.274.31.21943 1:CAS:528:DyaK1MXltVymtLo%3D (Pubitemid 29360032)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.31 , pp. 21943-21952
    • Russell, S.J.1    Steger, K.A.2    Johnston, S.A.3
  • 35
    • 44649161981 scopus 로고    scopus 로고
    • Reversible cytoplasmic localization of the proteasome in quiescent yeast cells
    • DOI 10.1083/jcb.200711154
    • D Laporte B Salin B Daignan-Fornier I Sagot 2008 Reversible cytoplasmic localization of the proteasome in quiescent yeast cells J Cell Biol 181 737 745 10.1083/jcb.200711154 18504300 10.1083/jcb.200711154 1:CAS:528: DC%2BD1cXntVCltr0%3D (Pubitemid 351786980)
    • (2008) Journal of Cell Biology , vol.181 , Issue.5 , pp. 737-745
    • Laporte, D.1    Salin, B.2    Daignan-Fornier, B.3    Sagot, I.4
  • 36
    • 0037401916 scopus 로고    scopus 로고
    • Intracellular localization of proteasomes
    • DOI 10.1016/S1357-2725(02)00380-1
    • C Wójcik GN DeMartino 2003 Intracellular localization of proteasomes Int J Biochem Cell Biol 35 579 589 10.1016/S1357-2725(02)00380-1 12672451 10.1016/S1357-2725(02)00380-1 (Pubitemid 36369507)
    • (2003) International Journal of Biochemistry and Cell Biology , vol.35 , Issue.5 , pp. 579-589
    • Wojcik, C.1    DeMartino, G.N.2
  • 37
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • 10.1038/nature07761 19242475 10.1038/nature07761
    • J Laurén DA Gimbel HB Nygaard JW Gilbert SM Strittmatter 2009 Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers Nature 457 1128 1132 10.1038/nature07761 19242475 10.1038/nature07761
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 38
    • 66449112462 scopus 로고    scopus 로고
    • SCAMP5 links endoplasmic reticulum stress to the accumulation of expanded polyglutamine protein aggregates via endocytosis inhibition
    • 10.1074/jbc.M807620200 19240033 10.1074/jbc.M807620200 1:CAS:528:DC%2BD1MXkslalsr4%3D
    • JY Noh H Lee S Song NS Kim W Im M Kim H Seo CW Chung JW Chang RJ Ferrante YJ Yoo H Ryu YK Jung 2009 SCAMP5 links endoplasmic reticulum stress to the accumulation of expanded polyglutamine protein aggregates via endocytosis inhibition J Biol Chem 284 11318 11325 10.1074/jbc.M807620200 19240033 10.1074/jbc.M807620200 1:CAS:528:DC%2BD1MXkslalsr4%3D
    • (2009) J Biol Chem , vol.284 , pp. 11318-11325
    • Noh, J.Y.1    Lee, H.2    Song, S.3    Kim, N.S.4    Im, W.5    Kim, M.6    Seo, H.7    Chung, C.W.8    Chang, J.W.9    Ferrante, R.J.10    Yoo, Y.J.11    Ryu, H.12    Jung, Y.K.13


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