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Volumn 44, Issue 6, 2004, Pages 931-945

BAG5 inhibits parkin and enhances dopaminergic neuron degeneration

Author keywords

[No Author keywords available]

Indexed keywords

BAG 5 PROTEIN; DOPAMINE; HEAT SHOCK PROTEIN 70; PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 10444241856     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuron.2004.11.026     Document Type: Article
Times cited : (185)

References (67)
  • 1
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi H., Katsuno M., Minamiyama M., Sang C., Pagoulatos G., Angelidis C., Kusakabe M., Yoshiki A., Kobayashi Y., Doyu M., Sobue G. Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J. Neurosci. 23:2003;2203-2211
    • (2003) J. Neurosci. , vol.23 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Sang, C.4    Pagoulatos, G.5    Angelidis, C.6    Kusakabe, M.7    Yoshiki, A.8    Kobayashi, Y.9    Doyu, M.10    Sobue, G.11
  • 2
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • Alberti S., Demand J., Esser C., Emmerich N., Schild H., Hohfeld J. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J. Biol. Chem. 277:2002;45920-45927
    • (2002) J. Biol. Chem. , vol.277 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 3
    • 0242531029 scopus 로고    scopus 로고
    • Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells over-expressing Parkin
    • Ardley H.C., Scott G.B., Rose S.A., Tan N.G., Markham A.F., Robinson P.A. Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells over-expressing Parkin. Mol. Biol. Cell. 14:2003;4541-4556
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4541-4556
    • Ardley, H.C.1    Scott, G.B.2    Rose, S.A.3    Tan, N.G.4    Markham, A.F.5    Robinson, P.A.6
  • 4
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck P.K., Chan H.Y., Trojanowski J.Q., Lee V.M., Bonini N.M. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science. 295:2002;865-868
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 6
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292:2001;1552-1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 11
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila
    • Chan H.Y., Warrick J.M., Gray-Board G.L., Paulson H.L., Bonini N.M. Mechanisms of chaperone suppression of polyglutamine disease. selectivity, synergy and modulation of protein solubility in Drosophila Hum. Mol. Genet. 9:2000;2811-2820
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2811-2820
    • Chan, H.Y.1    Warrick, J.M.2    Gray-Board, G.L.3    Paulson, H.L.4    Bonini, N.M.5
  • 12
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body formation in Parkinson disease
    • Chung K.K., Zhang Y., Lim K.L., Tanaka Y., Huang H., Gao J., Ross C.A., Dawson V.L., Dawson T.M. Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1. implications for Lewy-body formation in Parkinson disease Nat. Med. 7:2001;1144-1150
    • (2001) Nat. Med. , vol.7 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6    Ross, C.A.7    Dawson, V.L.8    Dawson, T.M.9
  • 17
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W., Przedborski S. Parkinson's disease. mechanisms and models Neuron. 39:2003;889-909
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 18
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand J., Alberti S., Patterson C., Hohfeld J. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 11:2001;1569-1577
    • (2001) Curr. Biol. , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 19
    • 0042208135 scopus 로고    scopus 로고
    • CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: Accumulation of poly-ubiquitinated Hsp90 client proteins
    • Doong H., Rizzo K., Fang S., Kulpa V., Weissman A.M., Kohn E.C. CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation. accumulation of poly-ubiquitinated Hsp90 client proteins J. Biol. Chem. 278:2003;28490-28500
    • (2003) J. Biol. Chem. , vol.278 , pp. 28490-28500
    • Doong, H.1    Rizzo, K.2    Fang, S.3    Kulpa, V.4    Weissman, A.M.5    Kohn, E.C.6
  • 20
    • 0038784529 scopus 로고    scopus 로고
    • Are ubiquitination pathways central to Parkinson's disease?
    • Giasson B.I., Lee V.M. Are ubiquitination pathways central to Parkinson's disease? Cell. 114:2003;1-8
    • (2003) Cell , vol.114 , pp. 1-8
    • Giasson, B.I.1    Lee, V.M.2
  • 22
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Hohfeld J., Jentsch S. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16:1997;6209-6216
    • (1997) EMBO J. , vol.16 , pp. 6209-6216
    • Hohfeld, J.1    Jentsch, S.2
  • 23
    • 0141995596 scopus 로고    scopus 로고
    • The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI
    • Huynh D.P., Scoles D.R., Nguyen D., Pulst S.M. The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Hum. Mol. Genet. 12:2003;2587-2597
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2587-2597
    • Huynh, D.P.1    Scoles, D.R.2    Nguyen, D.3    Pulst, S.M.4
  • 24
    • 0038342507 scopus 로고    scopus 로고
    • Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies
    • Ihara M., Tomimoto H., Kitayama H., Morioka Y., Akiguchi I., Shibasaki H., Noda M., Kinoshita M. Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies. J. Biol. Chem. 278:2003;24095-24102
    • (2003) J. Biol. Chem. , vol.278 , pp. 24095-24102
    • Ihara, M.1    Tomimoto, H.2    Kitayama, H.3    Morioka, Y.4    Akiguchi, I.5    Shibasaki, H.6    Noda, M.7    Kinoshita, M.8
  • 25
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y., Soda M., Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275:2000;35661-35664
    • (2000) J. Biol. Chem. , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 26
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell. 105:2001;891-902
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 27
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K.I., Takahashi R. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell. 10:2002;55-67
    • (2002) Mol. Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6    Takahashi, R.7
  • 28
    • 0037033074 scopus 로고    scopus 로고
    • Parkin accumulation in aggresomes due to proteasome impairment
    • Junn E., Lee S.S., Suhr U.T., Mouradian M.M. Parkin accumulation in aggresomes due to proteasome impairment. J. Biol. Chem. 277:2002;47870-47877
    • (2002) J. Biol. Chem. , vol.277 , pp. 47870-47877
    • Junn, E.1    Lee, S.S.2    Suhr, U.T.3    Mouradian, M.M.4
  • 33
    • 0032497504 scopus 로고    scopus 로고
    • Parkinson's disease. First of two parts
    • Lang A.E., Lozano A.M. Parkinson's disease. First of two parts. N. Engl. J. Med. 339:1998;1044-1053
    • (1998) N. Engl. J. Med. , vol.339 , pp. 1044-1053
    • Lang, A.E.1    Lozano, A.M.2
  • 34
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • Luders J., Demand J., Hohfeld J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 275:2000;4613-4617
    • (2000) J. Biol. Chem. , vol.275 , pp. 4613-4617
    • Luders, J.1    Demand, J.2    Hohfeld, J.3
  • 37
    • 0347917234 scopus 로고    scopus 로고
    • Parkin is recruited into aggresomes in a stress-specific manner: Over-expression of parkin reduces aggresome formation but can be dissociated from parkin's effect on neuronal survival
    • Muqit M.M.K., Davidson S.M., Payne-Smith M.D., MacCormac L.P., Kahns S., Jensen P.H., Wood N.W., Latchman D.S. Parkin is recruited into aggresomes in a stress-specific manner. Over-expression of parkin reduces aggresome formation but can be dissociated from parkin's effect on neuronal survival Hum. Mol. Genet. 13:2003;117-135
    • (2003) Hum. Mol. Genet. , vol.13 , pp. 117-135
    • Muqit, M.M.K.1    Davidson, S.M.2    Payne-Smith, M.D.3    MacCormac, L.P.4    Kahns, S.5    Jensen, P.H.6    Wood, N.W.7    Latchman, D.S.8
  • 38
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins
    • Nollen E.A., Morimoto R.I. Chaperoning signaling pathways. molecular chaperones as stress-sensing 'heat shock' proteins J. Cell Sci. 115:2002;2809-2816
    • (2002) J. Cell Sci. , vol.115 , pp. 2809-2816
    • Nollen, E.A.1    Morimoto, R.I.2
  • 42
    • 0037089589 scopus 로고    scopus 로고
    • Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cells
    • Paddison P.J., Caudy A.A., Bernstein E., Hannon G.J., Conklin D.S. Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cells. Genes Dev. 16:2002;948-958
    • (2002) Genes Dev. , vol.16 , pp. 948-958
    • Paddison, P.J.1    Caudy, A.A.2    Bernstein, E.3    Hannon, G.J.4    Conklin, D.S.5
  • 44
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation
    • Ren Y., Zhao J., Feng J. Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J. Neurosci. 23:2003;3316-3324
    • (2003) J. Neurosci. , vol.23 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 46
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., Goldberg A.L. Cellular defenses against unfolded proteins. a cell biologist thinks about neurodegenerative diseases Neuron. 29:2001;15-32
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 50
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • Sondermann H., Scheufler C., Schneider C., Hohfeld J., Hartl F.U., Moarefi I. Structure of a Bag/Hsc70 complex. convergent functional evolution of Hsp70 nucleotide exchange factors Science. 291:2001;1553-1557
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 51
    • 0037031902 scopus 로고    scopus 로고
    • Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae
    • Sondermann H., Ho A.K., Listenberger L.L., Siegers K., Moarefi I., Wente S.R., Hartl F.U., Young J.C. Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. J. Biol. Chem. 277:2002;33220-33227
    • (2002) J. Biol. Chem. , vol.277 , pp. 33220-33227
    • Sondermann, H.1    Ho, A.K.2    Listenberger, L.L.3    Siegers, K.4    Moarefi, I.5    Wente, S.R.6    Hartl, F.U.7    Young, J.C.8
  • 52
    • 0034745354 scopus 로고    scopus 로고
    • Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth
    • Song J., Takeda M., Morimoto R.I. Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Nat. Cell Biol. 3:2001;276-282
    • (2001) Nat. Cell Biol. , vol.3 , pp. 276-282
    • Song, J.1    Takeda, M.2    Morimoto, R.I.3
  • 54
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
    • Staropoli J.F., McDermott C., Martinat C., Schulman B., Demireva E., Abeliovich A. Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron. 37:2003;735-749
    • (2003) Neuron , vol.37 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 55
    • 0034790768 scopus 로고    scopus 로고
    • Molecular chaperone targeting and regulation by BAG family proteins
    • Takayama S., Reed J.C. Molecular chaperone targeting and regulation by BAG family proteins. Nat. Cell Biol. 3:2001;E237-E241
    • (2001) Nat. Cell Biol. , vol.3
    • Takayama, S.1    Reed, J.C.2
  • 56
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity
    • Takayama S., Sato T., Krajewski S., Kochel K., Irie S., Millan J.A., Reed J.C. Cloning and functional analysis of BAG-1. a novel Bcl-2-binding protein with anti-cell death activity Cell. 80:1995;279-284
    • (1995) Cell , vol.80 , pp. 279-284
    • Takayama, S.1    Sato, T.2    Krajewski, S.3    Kochel, K.4    Irie, S.5    Millan, J.A.6    Reed, J.C.7
  • 58
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama S., Reed J.C., Homma S. Heat-shock proteins as regulators of apoptosis. Oncogene. 22:2003;9041-9047
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 59
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai Y.C., Fishman P.S., Thakor N.V., Oyler G.A. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J. Biol. Chem. 278:2003;22044-22055
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 60
    • 0038205745 scopus 로고    scopus 로고
    • Targeting programmed cell death in neurodegenerative diseases
    • Vila M., Przedborski S. Targeting programmed cell death in neurodegenerative diseases. Nat. Rev. Neurosci. 4:2003;365-375
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 365-375
    • Vila, M.1    Przedborski, S.2
  • 61
    • 3142523288 scopus 로고    scopus 로고
    • Genetic clues to the pathogenesis of Parkinson's disease
    • Vila M., Przedborski S. Genetic clues to the pathogenesis of Parkinson's disease. Nat. Med. 10:2004;S58-S62
    • (2004) Nat. Med. , vol.10
    • Vila, M.1    Przedborski, S.2
  • 62
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick J.M., Chan H.Y., Gray-Board G.L., Chai Y., Paulson H.L., Bonini N.M. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet. 23:1999;425-428
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 63
    • 0344875488 scopus 로고    scopus 로고
    • Inactivation of parkin by oxidative stress and C-terminal truncations: A protective role of molecular chaperones
    • Winklhofer K.F., Henn I.H., Kay-Jackson P., Heller U., Tatzelt J. Inactivation of parkin by oxidative stress and C-terminal truncations. a protective role of molecular chaperones J. Biol. Chem. 278:2003;47199-47208
    • (2003) J. Biol. Chem. , vol.278 , pp. 47199-47208
    • Winklhofer, K.F.1    Henn, I.H.2    Kay-Jackson, P.3    Heller, U.4    Tatzelt, J.5
  • 64
    • 0037468831 scopus 로고    scopus 로고
    • Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila
    • Yang Y., Nishimura I., Imai Y., Takahashi R., Lu B. Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila. Neuron. 37:2003;911-924
    • (2003) Neuron , vol.37 , pp. 911-924
    • Yang, Y.1    Nishimura, I.2    Imai, Y.3    Takahashi, R.4    Lu, B.5
  • 66
    • 0030766734 scopus 로고    scopus 로고
    • Mammalian protein RAP46: An interaction partner and modulator of 70 kDa heat shock proteins
    • Zeiner M., Gebauer M., Gehring U. Mammalian protein RAP46. an interaction partner and modulator of 70 kDa heat shock proteins EMBO J. 16:1997;5483-5490
    • (1997) EMBO J. , vol.16 , pp. 5483-5490
    • Zeiner, M.1    Gebauer, M.2    Gehring, U.3
  • 67
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y., Gao J., Chung K.K.K., Huang H., Dawson V.L., Dawson T.M. Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl. Acad. Sci. USA. 97:2000;13354-13359
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6


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