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Volumn 124, Issue 6, 2004, Pages 375-382

Neurodegeneration caused by ER stress? - The pathogenetic mechanisms underlying AR-JP

Author keywords

CHIP; ER stress; Hsp70; Pael receptor

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; CYCLIN E; G PROTEIN COUPLED RECEPTOR; HEAT SHOCK PROTEIN 70; MITOGEN ACTIVATED PROTEIN KINASE P38; PAEL RECEPTOR; PARKIN; POLYGLUTAMINE; SYNAPTOTAGMIN; UNCLASSIFIED DRUG;

EID: 10944262709     PISSN: 00155691     EISSN: None     Source Type: Journal    
DOI: 10.1254/fpj.124.375     Document Type: Review
Times cited : (2)

References (37)
  • 1
    • 0037240325 scopus 로고    scopus 로고
    • Rare genetic mutations shed light on the pathogenesis of Parkinson disease
    • Dawson TM, Dawson VL. Rare genetic mutations shed light on the pathogenesis of Parkinson disease. J Clin Invest. 2003;111 (2):145-151.
    • (2003) J Clin Invest , vol.111 , Issue.2 , pp. 145-151
    • Dawson, T.M.1    Dawson, V.L.2
  • 2
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, Gispert S, et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science. 2004;304 (5674):1158-1160.
    • (2004) Science , vol.304 , Issue.5674 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3    Muqit, M.M.4    Harvey, K.5    Gispert, S.6
  • 4
    • 3142675793 scopus 로고    scopus 로고
    • Parkin and relatives: The RBR family of ubiquitin ligases
    • Marin I, Lucas JI, Gradilla AC, Ferrus A. Parkin and relatives: the RBR family of ubiquitin ligases. Physiol Genomics. 2004;17 (3):253-263.
    • (2004) Physiol Genomics , vol.17 , Issue.3 , pp. 253-263
    • Marin, I.1    Lucas, J.I.2    Gradilla, A.C.3    Ferrus, A.4
  • 5
    • 3242746009 scopus 로고    scopus 로고
    • Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING
    • Capili AD, Edghill EL, Wu K, Borden KL. Structure of the C-terminal RING finger from a RING-IBR-RING/ TRIAD motif reveals a novel zinc-binding domain distinct from a RING. J Mol Biol. 2004;340 (5):1117-1129.
    • (2004) J Mol Biol , vol.340 , Issue.5 , pp. 1117-1129
    • Capili, A.D.1    Edghill, E.L.2    Wu, K.3    Borden, K.L.4
  • 6
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H, Hattori N, Kubo S, Mizuno Y, Asakawa S, Minoshima S, et al. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet. 2000;25 (3):302-305.
    • (2000) Nat Genet , vol.25 , Issue.3 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3    Mizuno, Y.4    Asakawa, S.5    Minoshima, S.6
  • 7
    • 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 KK, Huang H, Dawson VL, Dawson TM. 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. 2000;97 (24):13354-13359.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.24 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 8
    • 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. 2000;275 (46):35661-35664.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 10
    • 0037368598 scopus 로고    scopus 로고
    • Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain
    • Sakata E, Yamaguchi Y, Kurimoto E, Kikuchi J, Yokoyama S, Yamada S, et al. Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain. EMBO Rep. 2003;4 (3):301-306.
    • (2003) EMBO Rep , vol.4 , Issue.3 , pp. 301-306
    • Sakata, E.1    Yamaguchi, Y.2    Kurimoto, E.3    Kikuchi, J.4    Yokoyama, S.5    Yamada, S.6
  • 11
    • 2942541204 scopus 로고    scopus 로고
    • How do Parkin mutations result in neurodegeneration?
    • Imai Y, Takahashi R. How do Parkin mutations result in neurodegeneration? Curr Opin Neurobiol. 2004;14 (3): 384-389.
    • (2004) Curr Opin Neurobiol , vol.14 , Issue.3 , pp. 384-389
    • Imai, Y.1    Takahashi, R.2
  • 12
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of alpha-synuclein by parkin from human brain: Implications for Parkinson's disease
    • Shimura H, Schlossmacher MG, Hattori N, Frosch MP, Trockenbacher A, Schneider R. Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science. 2001;293 (5528):263-269.
    • (2001) Science , vol.293 , Issue.5528 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3    Frosch, M.P.4    Trockenbacher, A.5    Schneider, R.6
  • 13
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body formation in Parkinson disease
    • Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, et al. Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat Med. 2001;7 (10):1144-1150.
    • (2001) Nat Med , vol.7 , Issue.10 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6
  • 14
    • 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. 2001;105 (7):891-902.
    • (2001) Cell , vol.105 , Issue.7 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 15
    • 0032952414 scopus 로고    scopus 로고
    • Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions
    • Engelender S, Kaminsky Z, Guo X, Sharp AH, Amaravi RK, Kleiderlein JJ, et al. Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions. Nat Genet. 1999;22 (1):110-114.
    • (1999) Nat Genet , vol.22 , Issue.1 , pp. 110-114
    • Engelender, S.1    Kaminsky, Z.2    Guo, X.3    Sharp, A.H.4    Amaravi, R.K.5    Kleiderlein, J.J.6
  • 17
    • 10744220754 scopus 로고    scopus 로고
    • The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: Linking protein biosynthesis and neurodegeneration
    • Corti O, Hampe C, Koutnikova H, Darios F, Jacquier S, Prigent A, et al. The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration. Hum Mol Genet. 2003;12 (12):1427-1437.
    • (2003) Hum Mol Genet , vol.12 , Issue.12 , pp. 1427-1437
    • Corti, O.1    Hampe, C.2    Koutnikova, H.3    Darios, F.4    Jacquier, S.5    Prigent, A.6
  • 18
    • 0141995596 scopus 로고    scopus 로고
    • The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI
    • Huynh DP, Scoles DR, Nguyen D, Pulst SM. The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Hum Mol Genet. 2003;12 (20):2587-2597.
    • (2003) Hum Mol Genet , vol.12 , Issue.20 , pp. 2587-2597
    • Huynh, D.P.1    Scoles, D.R.2    Nguyen, D.3    Pulst, S.M.4
  • 19
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai YC, Fishman PS, Thakor NV, Oyler GA. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J Biol Chem. 2003;278 (24):22044-22055.
    • (2003) J Biol Chem , vol.278 , Issue.24 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 20
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata S, Minami Y, Minami M, Chiba T, Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2001;2 (12):1133-1138.
    • (2001) EMBO Rep , vol.2 , Issue.12 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 21
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic eurons from kainate excitotoxicity
    • Staropoli JF, McDermott C, Martinat C, Schulman B, Demireva E, Abeliovich A. Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic eurons from kainate excitotoxicity. Neuron. 2003;37 (5):735-749.
    • (2003) Neuron , vol.37 , Issue.5 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 23
    • 0031575918 scopus 로고    scopus 로고
    • A novel endothelin receptor type-B-like gene enriched in the brain
    • Zeng Z, Su K, Kyaw H, Li Y. A novel endothelin receptor type-B-like gene enriched in the brain. Biochem Biophys Res Commun. 1997;233 (2):559-567.
    • (1997) Biochem Biophys Res Commun , vol.233 , Issue.2 , pp. 559-567
    • Zeng, Z.1    Su, K.2    Kyaw, H.3    Li, Y.4
  • 24
  • 25
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum- associated degradation (ERAD)
    • McCracken AA, Brodsky JL. Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays. 2003;25 (9):868-877.
    • (2003) Bioessays , vol.25 , Issue.9 , pp. 868-877
    • McCracken, A.A.1    Brodsky, J.L.2
  • 26
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: Coping with stress
    • Rutkowski DT, Kaufman RJ. A trip to the ER: coping with stress. Trends Cell Biol. 2004;14 (1):20-28.
    • (2004) Trends Cell Biol , vol.14 , Issue.1 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 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 KI, et al. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell. 2002;10 (1):55-67.
    • (2002) Mol Cell , vol.10 , Issue.1 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6
  • 28
    • 0142093671 scopus 로고    scopus 로고
    • Pael receptor, endoplasmic reticulum stress, and Parkinson's disease
    • Takahashi R, Imai Y. Pael receptor, endoplasmic reticulum stress, and Parkinson's disease. J Neurol. 2003;250 Suppl 3:III25-29.
    • (2003) J Neurol , vol.250 , Issue.SUPPL. 3
    • Takahashi, R.1    Imai, Y.2
  • 29
    • 0142059791 scopus 로고    scopus 로고
    • Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1
    • Dong Z, Ferger B, Paterna JC, Vogel D, Furler S, Osinde M, et al. Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1. Proc Natl Acad Sci USA. 2003;100 (21):12438-12443.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.21 , pp. 12438-12443
    • Dong, Z.1    Ferger, B.2    Paterna, J.C.3    Vogel, D.4    Furler, S.5    Osinde, M.6
  • 30
    • 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. 2003;37 (6):911-924.
    • (2003) Neuron , vol.37 , Issue.6 , pp. 911-924
    • Yang, Y.1    Nishimura, I.2    Imai, Y.3    Takahashi, R.4    Lu, B.5
  • 31
    • 2542560342 scopus 로고    scopus 로고
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
    • Pesah Y, Pham T, Burgess H, Middlebrooks B, Verstreken P, Zhou Y, et al. Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development. 2004;131 (9):2183-2194.
    • (2004) Development , vol.131 , Issue.9 , pp. 2183-2194
    • Pesah, Y.1    Pham, T.2    Burgess, H.3    Middlebrooks, B.4    Verstreken, P.5    Zhou, Y.6
  • 33
    • 10744221310 scopus 로고    scopus 로고
    • Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse
    • Itier JM, Ibanez P, Mena MA, Abbas N, Cohen-Salmon C, Bohme GA, et al. Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse. Hum Mol Genet. 2003;12 (18):2277-2291.
    • (2003) Hum Mol Genet , vol.12 , Issue.18 , pp. 2277-2291
    • Itier, J.M.1    Ibanez, P.2    Mena, M.A.3    Abbas, N.4    Cohen-Salmon, C.5    Bohme, G.A.6
  • 34
    • 0141891953 scopus 로고    scopus 로고
    • Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons
    • Goldberg MS, Fleming SM, Palacino JJ, Cepeda C, Lam HA, Bhatnagar A, et al. Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons. J Biol Chem. 2003;278 (44):43628-43635.
    • (2003) J Biol Chem , vol.278 , Issue.44 , pp. 43628-43635
    • Goldberg, M.S.1    Fleming, S.M.2    Palacino, J.J.3    Cepeda, C.4    Lam, H.A.5    Bhatnagar, A.6
  • 36
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • Palacino JJ, Sagi D, Goldberg MS, Krauss S, Motz C, Wacker M, et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J Biol Chem. 2004;279 (18):18614-18622.
    • (2004) J Biol Chem , vol.279 , Issue.18 , pp. 18614-18622
    • Palacino, J.J.1    Sagi, D.2    Goldberg, M.S.3    Krauss, S.4    Motz, C.5    Wacker, M.6
  • 37
    • 2642516493 scopus 로고    scopus 로고
    • Parkin counteracts symptoms in a Drosophila model of Parkinson's disease
    • Haywood AF, Staveley BE. Parkin counteracts symptoms in a Drosophila model of Parkinson's disease. BMC Neurosci. 2004;5 (1):14.
    • (2004) BMC Neurosci , vol.5 , Issue.1 , pp. 14
    • Haywood, A.F.1    Staveley, B.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.