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Volumn 28, Issue 33, 2008, Pages 8189-8198

Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and lewy-like inclusions resembling human pale bodies

Author keywords

Dementia; Genetics; Neuronal death; Neuropathology; Parkinson's disease; Proteolysis; Transgenic

Indexed keywords

ALPHA SYNUCLEIN; DNA 26S; PROTEASOME; UBIQUITIN; ATP DEPENDENT 26S PROTEASE;

EID: 51149121890     PISSN: 02706474     EISSN: 02706474     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.2218-08.2008     Document Type: Article
Times cited : (266)

References (60)
  • 1
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • Abou-Sleiman PM, Muqit MM, Wood NW (2006) Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat Rev Neurosci 7:207-219.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 2
    • 0029114373 scopus 로고
    • Time of neuron origin and gradients of neurogenesis in midbrain dopaminergic neurons in the mouse
    • Bayer SA, Wills KV, Triarhou LC, Ghetti B (1995) Time of neuron origin and gradients of neurogenesis in midbrain dopaminergic neurons in the mouse. Exp Brain Res 105:191-199.
    • (1995) Exp Brain Res , vol.105 , pp. 191-199
    • Bayer, S.A.1    Wills, K.V.2    Triarhou, L.C.3    Ghetti, B.4
  • 4
    • 26844505808 scopus 로고    scopus 로고
    • Toxin-induced models of Parkinson's disease
    • Bové J, Prou D, Perier C, Przedborski S (2005) Toxin-induced models of Parkinson's disease. NeuroRx 2:484-494.
    • (2005) NeuroRx , vol.2 , pp. 484-494
    • Bové, J.1    Prou, D.2    Perier, C.3    Przedborski, S.4
  • 7
    • 34249085552 scopus 로고    scopus 로고
    • Proteasomes: Machines for all reasons
    • Demartino GN, Gillette TG (2007) Proteasomes: machines for all reasons. Cell 129:659-662.
    • (2007) Cell , vol.129 , pp. 659-662
    • Demartino, G.N.1    Gillette, T.G.2
  • 9
    • 37349008891 scopus 로고    scopus 로고
    • Progranulin: Normal function and role in neurodegeneration
    • Eriksen JL, Mackenzie IR (2008) Progranulin: normal function and role in neurodegeneration. J Neurochem 104:287-297.
    • (2008) J Neurochem , vol.104 , pp. 287-297
    • Eriksen, J.L.1    Mackenzie, I.R.2
  • 10
    • 38149082008 scopus 로고    scopus 로고
    • Increased expression and altered subunit composition of proteasomes induced by continuous proteasome inhibition establish apoptosis resistance and hyperproliferation of Burkitt lymphoma cells
    • Fuchs D, Berges C, Opelz G, Daniel V, Naujokat C (2008) Increased expression and altered subunit composition of proteasomes induced by continuous proteasome inhibition establish apoptosis resistance and hyperproliferation of Burkitt lymphoma cells. J Cell Biochem 103:270-283.
    • (2008) J Cell Biochem , vol.103 , pp. 270-283
    • Fuchs, D.1    Berges, C.2    Opelz, G.3    Daniel, V.4    Naujokat, C.5
  • 11
    • 0033669319 scopus 로고    scopus 로고
    • In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies
    • Gai WP, Yuan HX, Li XQ, Power JT, Blumbergs PC, Jensen PH (2000) In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies. Exp Neurol 166:324-333.
    • (2000) Exp Neurol , vol.166 , pp. 324-333
    • Gai, W.P.1    Yuan, H.X.2    Li, X.Q.3    Power, J.T.4    Blumbergs, P.C.5    Jensen, P.H.6
  • 12
    • 24944525045 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson's disease
    • Gandhi S, Wood NW (2005) Molecular pathogenesis of Parkinson's disease. Hum Mol Genet 14:2749-2755.
    • (2005) Hum Mol Genet , vol.14 , pp. 2749-2755
    • Gandhi, S.1    Wood, N.W.2
  • 13
    • 0035959931 scopus 로고    scopus 로고
    • Parkin and the molecular pathways of parkinson's disease
    • Giasson BI, Lee VM (2001) Parkin and the molecular pathways of parkinson's disease. Neuron 31:885-888.
    • (2001) Neuron , vol.31 , pp. 885-888
    • Giasson, B.I.1    Lee, V.M.2
  • 14
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82:373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 15
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • Gonzalez F, Delahodde A, Kodadek T, Johnston SA (2002) Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 296:548-550.
    • (2002) Science , vol.296 , pp. 548-550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 16
    • 0027379925 scopus 로고
    • Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit
    • Gordon C, McGurk G, Dillon P, Rosen C, Hastie ND (1993) Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit. Nature 366:355-357.
    • (1993) Nature , vol.366 , pp. 355-357
    • Gordon, C.1    McGurk, G.2    Dillon, P.3    Rosen, C.4    Hastie, N.D.5
  • 17
    • 0037401695 scopus 로고    scopus 로고
    • Substrate access and processing by the 20S proteasome core particle
    • Groll M, Huber R (2003) Substrate access and processing by the 20S proteasome core particle. Int J Biochem Cell Biol 35:606-616.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 606-616
    • Groll, M.1    Huber, R.2
  • 22
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR (1998) Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143:1883-1898.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 23
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • Köhler A, Cascio P, Leggett DS, Woo KM, Goldberg AL, Finley D (2001) The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol Cell 7:1143-1152.
    • (2001) Mol Cell , vol.7 , pp. 1143-1152
    • Köhler, A.1    Cascio, P.2    Leggett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 26
    • 41649091606 scopus 로고    scopus 로고
    • Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome
    • Koulich E, Li X, Demartino GN (2008) Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol Biol Cell 19:1072-1082.
    • (2008) Mol Biol Cell , vol.19 , pp. 1072-1082
    • Koulich, E.1    Li, X.2    Demartino, G.N.3
  • 27
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognises the polyubiquitin degradation signal
    • Lam YA, Lawson TG, Velayutham M, Zweier JL, Pickart CM (2002) A proteasomal ATPase subunit recognises the polyubiquitin degradation signal. Nature 416:763-767.
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.M.5
  • 28
    • 0026031271 scopus 로고
    • Immunogold localisation of ubiquitin-protein conjugates in primary (azurophilic) granules of polymorphonuclear neutrophils
    • László L, Doherty FJ, Watson A, Self T, Landon M, Lowe J, Mayer RJ (1991) Immunogold localisation of ubiquitin-protein conjugates in primary (azurophilic) granules of polymorphonuclear neutrophils. FEBS Lett 279:175-178.
    • (1991) FEBS Lett , vol.279 , pp. 175-178
    • László, L.1    Doherty, F.J.2    Watson, A.3    Self, T.4    Landon, M.5    Lowe, J.6    Mayer, R.J.7
  • 29
    • 0036217859 scopus 로고    scopus 로고
    • Timing the doxycycline yields different patterns of genomic recombination in brain neurons with a new inducible Cre transgene
    • Lindeberg J, Mattsson R, Ebendal T (2002) Timing the doxycycline yields different patterns of genomic recombination in brain neurons with a new inducible Cre transgene. J Neurosci Res 68:248-253.
    • (2002) J Neurosci Res , vol.68 , pp. 248-253
    • Lindeberg, J.1    Mattsson, R.2    Ebendal, T.3
  • 31
    • 0023927981 scopus 로고
    • Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease
    • Lowe J, Blanchard A, Morrell K, Lennox G, Reynolds L, Billett M, Landon M, Mayer RJ (1988) Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease. J Pathol 155:9-15.
    • (1988) J Pathol , vol.155 , pp. 9-15
    • Lowe, J.1    Blanchard, A.2    Morrell, K.3    Lennox, G.4    Reynolds, L.5    Billett, M.6    Landon, M.7    Mayer, R.J.8
  • 32
    • 18944392199 scopus 로고    scopus 로고
    • Identification and characterization of a Drosophila proteasome regulatory network
    • Lundgren J, Masson P, Mirzaei Z, Young P (2005) Identification and characterization of a Drosophila proteasome regulatory network. Mol Cell Biol 25:4662-4675.
    • (2005) Mol Cell Biol , vol.25 , pp. 4662-4675
    • Lundgren, J.1    Masson, P.2    Mirzaei, Z.3    Young, P.4
  • 33
    • 0029807527 scopus 로고    scopus 로고
    • Control of memory formation through regulated expression of a CaMKII transgene
    • Mayford M, Bach ME, Huang YY, Wang L, Hawkins RD, Kandel ER (1996) Control of memory formation through regulated expression of a CaMKII transgene. Science 274:1678-1683.
    • (1996) Science , vol.274 , pp. 1678-1683
    • Mayford, M.1    Bach, M.E.2    Huang, Y.Y.3    Wang, L.4    Hawkins, R.D.5    Kandel, E.R.6
  • 34
    • 33646126924 scopus 로고    scopus 로고
    • A decade of modeling Alzheimer's disease in transgenic mice
    • McGowan E, Eriksen J, Hutton M (2006) A decade of modeling Alzheimer's disease in transgenic mice. Trends Genet 22:281-289.
    • (2006) Trends Genet , vol.22 , pp. 281-289
    • McGowan, E.1    Eriksen, J.2    Hutton, M.3
  • 35
    • 3042794162 scopus 로고    scopus 로고
    • Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease
    • McNaught KS, Perl DP, Brownell AL, Olanow CW (2004) Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann Neurol 56:149-162.
    • (2004) Ann Neurol , vol.56 , pp. 149-162
    • McNaught, K.S.1    Perl, D.P.2    Brownell, A.L.3    Olanow, C.W.4
  • 36
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes
    • Meiners S, Heyken D, Weller A, Ludwig A, Stangl K, Kloetzel PM, Krüger E (2003) Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes. J Biol Chem 278:21517-21525.
    • (2003) J Biol Chem , vol.278 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Ludwig, A.4    Stangl, K.5    Kloetzel, P.M.6    Krüger, E.7
  • 38
    • 33745827004 scopus 로고    scopus 로고
    • Protective roles for induction of autophagy in multiple proteinopathies
    • Menzies FM, Ravikumar B, Rubinsztein DC (2006) Protective roles for induction of autophagy in multiple proteinopathies. Autophagy 2:224-225.
    • (2006) Autophagy , vol.2 , pp. 224-225
    • Menzies, F.M.1    Ravikumar, B.2    Rubinsztein, D.C.3
  • 39
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 40
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart CM, Cohen RE (2004) Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 5:177-187.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 43
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • Rubin DM, Glickman MH, Larsen CN, Dhruvakumar S, Finley D (1998) Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J 17:4909-4919.
    • (1998) EMBO J , vol.17 , pp. 4909-4919
    • Rubin, D.M.1    Glickman, M.H.2    Larsen, C.N.3    Dhruvakumar, S.4    Finley, D.5
  • 44
    • 41649088465 scopus 로고    scopus 로고
    • Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb polyubiquitin gene
    • Ryu KY, Garza JC, Lu XY, Barsh GS, Kopito RR (2008) Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb polyubiquitin gene. Proc Natl Acad Sci U S A 105:4016-4021.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4016-4021
    • Ryu, K.Y.1    Garza, J.C.2    Lu, X.Y.3    Barsh, G.S.4    Kopito, R.R.5
  • 45
    • 26844433577 scopus 로고    scopus 로고
    • Proteasome-associated proteins: Regulation of a proteolytic machine
    • Schmidt M, Hanna J, Elsasser S, Finley D (2005) Proteasome-associated proteins: regulation of a proteolytic machine. Biol Chem 386:725-737.
    • (2005) Biol Chem , vol.386 , pp. 725-737
    • Schmidt, M.1    Hanna, J.2    Elsasser, S.3    Finley, D.4
  • 46
    • 0030297778 scopus 로고    scopus 로고
    • Characteristics of 26S proteases from fission yeast mutants, which arrest in mitosis
    • Seeger M, Gordon C, Ferrell K, Dubiel W (1996) Characteristics of 26S proteases from fission yeast mutants, which arrest in mitosis. J Mol Biol 263:423-431.
    • (1996) J Mol Biol , vol.263 , pp. 423-431
    • Seeger, M.1    Gordon, C.2    Ferrell, K.3    Dubiel, W.4
  • 48
    • 33748753648 scopus 로고    scopus 로고
    • Widespread, but non-identical, association of proteasomal 19 and 20 S proteins with yeast chromatin
    • Sikder D, Johnston SA, Kodadek T (2006) Widespread, but non-identical, association of proteasomal 19 and 20 S proteins with yeast chromatin. J Biol Chem 281:27346-27355.
    • (2006) J Biol Chem , vol.281 , pp. 27346-27355
    • Sikder, D.1    Johnston, S.A.2    Kodadek, T.3
  • 49
    • 28444452611 scopus 로고    scopus 로고
    • ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins
    • Smith DM, Kafri G, Cheng Y, Ng D, Walz T, Goldberg AL (2005) ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins. Mol Cell 20:687-698.
    • (2005) Mol Cell , vol.20 , pp. 687-698
    • Smith, D.M.1    Kafri, G.2    Cheng, Y.3    Ng, D.4    Walz, T.5    Goldberg, A.L.6
  • 50
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry
    • Smith DM, Chang SC, Park S, Finley D, Cheng Y, Goldberg AL (2007) Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry. Mol Cell 27:731-744.
    • (2007) Mol Cell , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 51
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • Tanahashi N, Murakami Y, Minami Y, Shimbara N, Hendil KB, Tanaka K (2000) Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J Biol Chem 275:14336-14345.
    • (2000) J Biol Chem , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 52
    • 0035220337 scopus 로고    scopus 로고
    • Aggregation chimeras. Combining ES cells, diploid and tetraploid embryos
    • Tanaka M, Hadjantonakis AK, Nagy A (2001) Aggregation chimeras. Combining ES cells, diploid and tetraploid embryos. Methods Mol Biol 158:135-154.
    • (2001) Methods Mol Biol , vol.158 , pp. 135-154
    • Tanaka, M.1    Hadjantonakis, A.K.2    Nagy, A.3
  • 53
    • 0035976835 scopus 로고    scopus 로고
    • alpha-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris GK, Layfield R, Spillantini MG (2001) alpha-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett 509:22-26.
    • (2001) FEBS Lett , vol.509 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 56
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68:1015-1068.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 57
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • Wang J, Wang CE, Orr A, Tydlacka S, Li SH, Li XJ (2008) Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. J Cell Biol 180:1177-1189.
    • (2008) J Cell Biol , vol.180 , pp. 1177-1189
    • Wang, J.1    Wang, C.E.2    Orr, A.3    Tydlacka, S.4    Li, S.H.5    Li, X.J.6
  • 58
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • Welchman RL, Gordon C, Mayer RJ (2005) Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Biol 6:599-609.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 59
    • 0037155196 scopus 로고    scopus 로고
    • Analysis of Drosophila 26S proteasome using RNA interference
    • Wójcik C, DeMartino GN (2002) Analysis of Drosophila 26S proteasome using RNA interference. J Biol Chem 277:6188-6197.
    • (2002) J Biol Chem , vol.277 , pp. 6188-6197
    • Wójcik, C.1    DeMartino, G.N.2
  • 60
    • 33847410541 scopus 로고    scopus 로고
    • Emerging roles for ubiquitin and protein degradation in neuronal function
    • Yi JJ, Ehlers MD (2007) Emerging roles for ubiquitin and protein degradation in neuronal function. Pharmacol Rev 59:14-39.
    • (2007) Pharmacol Rev , vol.59 , pp. 14-39
    • Yi, J.J.1    Ehlers, M.D.2


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