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Volumn 456, Issue 1, 2009, Pages 15-19

Inhibition of lysosomal functions reduces proteasomal activity

Author keywords

Lysosomes; Proteasomes; Ubiquitin

Indexed keywords

CELL PROTEIN; CHAPERONE; HEAT SHOCK COGNATE PROTEIN 70; LYSOSOME ENZYME; PROTEASOME;

EID: 64749103447     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2009.03.085     Document Type: Article
Times cited : (47)

References (66)
  • 3
    • 34248530304 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in aging and neurodegeneration: lessons from alpha-synuclein
    • Bandhyopadhyay U., and Cuervo A.M. Chaperone-mediated autophagy in aging and neurodegeneration: lessons from alpha-synuclein. Exp. Gerontol. (2006)
    • (2006) Exp. Gerontol.
    • Bandhyopadhyay, U.1    Cuervo, A.M.2
  • 4
    • 33646482114 scopus 로고    scopus 로고
    • Reduced ubiquitin C-terminal hydrolase-1 expression levels in dementia with Lewy bodies
    • Barrachina M., Castano E., Dalfo E., Maes T., Buesa C., and Ferrer I. Reduced ubiquitin C-terminal hydrolase-1 expression levels in dementia with Lewy bodies. Neurobiol. Dis. 22 (2006) 265-273
    • (2006) Neurobiol. Dis. , vol.22 , pp. 265-273
    • Barrachina, M.1    Castano, E.2    Dalfo, E.3    Maes, T.4    Buesa, C.5    Ferrer, I.6
  • 8
    • 17644392138 scopus 로고    scopus 로고
    • Torsin-mediated protection from cellular stress in the dopaminergic neurons of Caenorhabditis elegans
    • Cao S., Gelwix C.C., Caldwell K.A., and Caldwell G.A. Torsin-mediated protection from cellular stress in the dopaminergic neurons of Caenorhabditis elegans. J. Neurosci. 25 (2005) 3801-3812
    • (2005) J. Neurosci. , vol.25 , pp. 3801-3812
    • Cao, S.1    Gelwix, C.C.2    Caldwell, K.A.3    Caldwell, G.A.4
  • 9
    • 0028220243 scopus 로고
    • Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease
    • Cataldo A.M., Hamilton D.J., and Nixon R.A. Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease. Brain Res. 640 (1994) 68-80
    • (1994) Brain Res. , vol.640 , pp. 68-80
    • Cataldo, A.M.1    Hamilton, D.J.2    Nixon, R.A.3
  • 11
    • 0034510572 scopus 로고    scopus 로고
    • Unique properties of lamp2a compared to other lamp2 isoforms
    • Cuervo A.M., and Dice J.F. Unique properties of lamp2a compared to other lamp2 isoforms. J. Cell Sci. 113 Pt 24 (2000) 4441-4450
    • (2000) J. Cell Sci. 113 Pt , vol.24 , pp. 4441-4450
    • Cuervo, A.M.1    Dice, J.F.2
  • 12
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo A.M., Stefanis L., Fredenburg R., Lansbury P.T., and Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305 (2004) 1292-1295
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 14
    • 0018713875 scopus 로고
    • Lysosomes and protein degradation
    • Dean R.T. Lysosomes and protein degradation. Ciba Found. Symp. (1979) 139-149
    • (1979) Ciba Found. Symp. , pp. 139-149
    • Dean, R.T.1
  • 15
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding W.X., Ni H.M., Gao W., Yoshimori T., Stolz D.B., Ron D., and Yin X.M. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am. J. Pathol. 171 (2007) 513-524
    • (2007) Am. J. Pathol. , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.M.7
  • 16
    • 38949096081 scopus 로고    scopus 로고
    • Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome
    • Ding W.X., and Yin X.M. Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy 4 (2008) 141-150
    • (2008) Autophagy , vol.4 , pp. 141-150
    • Ding, W.X.1    Yin, X.M.2
  • 17
    • 3542993306 scopus 로고    scopus 로고
    • Mice lacking alpha-synuclein have an attenuated loss of striatal dopamine following prolonged chronic MPTP administration
    • Drolet R.E., Behrouz B., Lookingland K.J., and Goudreau J.L. Mice lacking alpha-synuclein have an attenuated loss of striatal dopamine following prolonged chronic MPTP administration. Neurotoxicology 25 (2004) 761-769
    • (2004) Neurotoxicology , vol.25 , pp. 761-769
    • Drolet, R.E.1    Behrouz, B.2    Lookingland, K.J.3    Goudreau, J.L.4
  • 18
    • 34247113888 scopus 로고    scopus 로고
    • Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II)
    • Fujita E., Kouroku Y., Isoai A., Kumagai H., Misutani A., Matsuda C., Hayashi Y.K., and Momoi T. Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II). Hum. Mol. Genet. 16 (2007) 618-629
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 618-629
    • Fujita, E.1    Kouroku, Y.2    Isoai, A.3    Kumagai, H.4    Misutani, A.5    Matsuda, C.6    Hayashi, Y.K.7    Momoi, T.8
  • 19
    • 50549085408 scopus 로고    scopus 로고
    • Neuroinflammation and oxidation/nitration of alpha-synuclein linked to dopaminergic neurodegeneration
    • Gao H.M., Kotzbauer P.T., Uryu K., Leight S., Trojanowski J.Q., and Lee V.M. Neuroinflammation and oxidation/nitration of alpha-synuclein linked to dopaminergic neurodegeneration. J. Neurosci. 28 (2008) 7687-7698
    • (2008) J. Neurosci. , vol.28 , pp. 7687-7698
    • Gao, H.M.1    Kotzbauer, P.T.2    Uryu, K.3    Leight, S.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 20
    • 0037118259 scopus 로고    scopus 로고
    • Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein
    • Giasson B.I., Duda J.E., Quinn S.M., Zhang B., Trojanowski J.Q., and Lee V.M. Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein. Neuron 34 (2002) 521-533
    • (2002) Neuron , vol.34 , pp. 521-533
    • Giasson, B.I.1    Duda, J.E.2    Quinn, S.M.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 22
    • 32344444326 scopus 로고    scopus 로고
    • Down-regulation of alpha-synuclein expression can rescue dopaminergic cells from cell death in the substantia nigra of Parkinson's disease rat model
    • Hayashita-Kinoh H., Yamada M., Yokota T., Mizuno Y., and Mochizuki H. Down-regulation of alpha-synuclein expression can rescue dopaminergic cells from cell death in the substantia nigra of Parkinson's disease rat model. Biochem. Biophys. Res. Commun. 341 (2006) 1088-1095
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 1088-1095
    • Hayashita-Kinoh, H.1    Yamada, M.2    Yokota, T.3    Mizuno, Y.4    Mochizuki, H.5
  • 23
    • 34249802905 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system alterations in a striatal cell model of Huntington's disease
    • Hunter J.M., Lesort M., and Johnson G.V. Ubiquitin-proteasome system alterations in a striatal cell model of Huntington's disease. J. Neurosci. Res. 85 (2007) 1774-1788
    • (2007) J. Neurosci. Res. , vol.85 , pp. 1774-1788
    • Hunter, J.M.1    Lesort, M.2    Johnson, G.V.3
  • 24
    • 0030830270 scopus 로고    scopus 로고
    • Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly
    • Ii K., Ito H., Tanaka K., and Hirano A. Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly. J. Neuropathol. Exp. Neurol. 56 (1997) 125-131
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 125-131
    • Ii, K.1    Ito, H.2    Tanaka, K.3    Hirano, A.4
  • 25
    • 36949031267 scopus 로고    scopus 로고
    • Alpha-synucleinopathy models and human neuropathology: similarities and differences
    • Kahle P.J. Alpha-synucleinopathy models and human neuropathology: similarities and differences. Acta Neuropathol. 115 (2008) 87-95
    • (2008) Acta Neuropathol. , vol.115 , pp. 87-95
    • Kahle, P.J.1
  • 31
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway
    • Lee H.J., Khoshaghideh F., Patel S., and Lee S.J. Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway. J. Neurosci. 24 (2004) 1888-1896
    • (2004) J. Neurosci. , vol.24 , pp. 1888-1896
    • Lee, H.J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.J.4
  • 32
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: new targets for drug discovery
    • Lee V.M., and Trojanowski J.Q. Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: new targets for drug discovery. Neuron 52 (2006) 33-38
    • (2006) Neuron , vol.52 , pp. 33-38
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 34
    • 7244243876 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein protein with aging and familial parkinson's disease-linked A53T mutation
    • Li W., Lesuisse C., Xu Y., Troncoso J.C., Price D.L., and Lee M.K. Stabilization of alpha-synuclein protein with aging and familial parkinson's disease-linked A53T mutation. J. Neurosci. 24 (2004) 7400-7409
    • (2004) J. Neurosci. , vol.24 , pp. 7400-7409
    • Li, W.1    Lesuisse, C.2    Xu, Y.3    Troncoso, J.C.4    Price, D.L.5    Lee, M.K.6
  • 35
  • 37
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders
    • Masliah E., Rockenstein E., Veinbergs I., Mallory M., Hashimoto M., Takeda A., Sagara Y., Sisk A., and Mucke L. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science 287 (2000) 1265-1269
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 39
    • 33745023775 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in aging and disease
    • Massey A.C., Zhang C., and Cuervo A.M. Chaperone-mediated autophagy in aging and disease. Curr. Top. Dev. Biol. 73 (2006) 205-235
    • (2006) Curr. Top. Dev. Biol. , vol.73 , pp. 205-235
    • Massey, A.C.1    Zhang, C.2    Cuervo, A.M.3
  • 40
    • 0035859226 scopus 로고    scopus 로고
    • Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons
    • McLean P.J., Kawamata H., and Hyman B.T. Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons. Neuroscience 104 (2001) 901-912
    • (2001) Neuroscience , vol.104 , pp. 901-912
    • McLean, P.J.1    Kawamata, H.2    Hyman, B.T.3
  • 43
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught K.S., and Jenner P. Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 297 (2001) 191-194
    • (2001) Neurosci. Lett. , vol.297 , pp. 191-194
    • McNaught, K.S.1    Jenner, P.2
  • 45
    • 0037159608 scopus 로고    scopus 로고
    • Lysosomal malfunction accompanies alpha-synuclein aggregation in a progressive mouse model of Parkinson's disease
    • Meredith G.E., Totterdell S., Petroske E., Santa C.K., Callison Jr. R.C., and Lau Y.S. Lysosomal malfunction accompanies alpha-synuclein aggregation in a progressive mouse model of Parkinson's disease. Brain Res. 956 (2002) 156-165
    • (2002) Brain Res. , vol.956 , pp. 156-165
    • Meredith, G.E.1    Totterdell, S.2    Petroske, E.3    Santa, C.K.4    Callison Jr., R.C.5    Lau, Y.S.6
  • 51
    • 4344583898 scopus 로고    scopus 로고
    • Involvement of macroautophagy in the dissolution of neuronal inclusions
    • Rideout H.J., Lang-Rollin I., and Stefanis L. Involvement of macroautophagy in the dissolution of neuronal inclusions. Int. J. Biochem. Cell Biol. 36 (2004) 2551-2562
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2551-2562
    • Rideout, H.J.1    Lang-Rollin, I.2    Stefanis, L.3
  • 52
    • 0036432029 scopus 로고    scopus 로고
    • Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination
    • Rideout H.J., and Stefanis L. Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination. Mol. Cell. Neurosci. 21 (2002) 223-238
    • (2002) Mol. Cell. Neurosci. , vol.21 , pp. 223-238
    • Rideout, H.J.1    Stefanis, L.2
  • 53
    • 2642553802 scopus 로고    scopus 로고
    • Developmental loss and resistance to MPTP toxicity of dopaminergic neurones in substantia nigra pars compacta of gamma-synuclein, alpha-synuclein and double alpha/gamma-synuclein null mutant mice
    • Robertson D.C., Schmidt O., Ninkina N., Jones P.A., Sharkey J., and Buchman V.L. Developmental loss and resistance to MPTP toxicity of dopaminergic neurones in substantia nigra pars compacta of gamma-synuclein, alpha-synuclein and double alpha/gamma-synuclein null mutant mice. J. Neurochem. 89 (2004) 1126-1136
    • (2004) J. Neurochem. , vol.89 , pp. 1126-1136
    • Robertson, D.C.1    Schmidt, O.2    Ninkina, N.3    Jones, P.A.4    Sharkey, J.5    Buchman, V.L.6
  • 54
    • 0038307156 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies
    • Sampathu D.M., Giasson B.I., Pawlyk A.C., Trojanowski J.Q., and Lee V.M. Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies. Am. J. Pathol. 163 (2003) 91-100
    • (2003) Am. J. Pathol. , vol.163 , pp. 91-100
    • Sampathu, D.M.1    Giasson, B.I.2    Pawlyk, A.C.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 55
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar S., Davies J.E., Huang Z., Tunnacliffe A., and Rubinsztein D.C. Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J. Biol. Chem. 282 (2007) 5641-5652
    • (2007) J. Biol. Chem. , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 56
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • Sarkar S., Krishna G., Imarisio S., Saiki S., O'Kane C.J., and Rubinsztein D.C. A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. Hum. Mol. Genet. 17 (2008) 170-178
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 170-178
    • Sarkar, S.1    Krishna, G.2    Imarisio, S.3    Saiki, S.4    O'Kane, C.J.5    Rubinsztein, D.C.6
  • 57
    • 33645916698 scopus 로고    scopus 로고
    • Inositol and IP3 levels regulate autophagy: biology and therapeutic speculations
    • Sarkar S., and Rubinsztein D.C. Inositol and IP3 levels regulate autophagy: biology and therapeutic speculations. Autophagy 2 (2006) 132-134
    • (2006) Autophagy , vol.2 , pp. 132-134
    • Sarkar, S.1    Rubinsztein, D.C.2
  • 58
    • 51549106105 scopus 로고    scopus 로고
    • Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species
    • Sevlever D., Jiang P., and Yen S.H. Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species. Biochemistry (2008)
    • (2008) Biochemistry
    • Sevlever, D.1    Jiang, P.2    Yen, S.H.3
  • 59
    • 21244499845 scopus 로고    scopus 로고
    • The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways
    • Shin Y., Klucken J., Patterson C., Hyman B.T., and McLean P.J. The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways. J. Biol. Chem. 280 (2005) 23727-23734
    • (2005) J. Biol. Chem. , vol.280 , pp. 23727-23734
    • Shin, Y.1    Klucken, J.2    Patterson, C.3    Hyman, B.T.4    McLean, P.J.5
  • 61
    • 0035976835 scopus 로고    scopus 로고
    • Alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris G.K., Layfield R., and Spillantini M.G. Alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 509 (2001) 22-26
    • (2001) FEBS Lett. , vol.509 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 65
    • 0345189365 scopus 로고    scopus 로고
    • Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein
    • Willingham S., Outeiro T.F., DeVit M.J., Lindquist S.L., and Muchowski P.J. Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science 302 (2003) 1769-1772
    • (2003) Science , vol.302 , pp. 1769-1772
    • Willingham, S.1    Outeiro, T.F.2    DeVit, M.J.3    Lindquist, S.L.4    Muchowski, P.J.5


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