메뉴 건너뛰기




Volumn 111, Issue 2, 2002, Pages 209-218

The UCH-L1 gene encodes two opposing enzymatic activities that affect α-synuclein degradation and Parkinson's disease susceptibility

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; BRAIN ENZYME; HYDROLASE; LIGASE; MUTANT PROTEIN; PROTEASOME; UBIQUITIN C TERMINAL HYDROLASE 1; UBIQUITYL LIGASE; UNCLASSIFIED DRUG;

EID: 0037131567     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)01012-7     Document Type: Article
Times cited : (728)

References (47)
  • 1
    • 0035947372 scopus 로고    scopus 로고
    • Impariment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impariment 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
  • 3
    • 0028799949 scopus 로고
    • Persistent activation of cAMP-dependent protein kinase by regulated proteolysis suggests a neuron-specific function of the ubiquitin system in Aplysia
    • Chain D.G., Hegde A.N., Yamamoto N., Liu-Marsh B., Schwartz J.H. Persistent activation of cAMP-dependent protein kinase by regulated proteolysis suggests a neuron-specific function of the ubiquitin system in Aplysia. J. Neurosci. 15:1995;7592-7603.
    • (1995) J. Neurosci. , vol.15 , pp. 7592-7603
    • Chain, D.G.1    Hegde, A.N.2    Yamamoto, N.3    Liu-Marsh, B.4    Schwartz, J.H.5
  • 4
    • 0018187738 scopus 로고
    • A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
    • Ciechanover A., Hod Y., Hershko A. A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem. Biophys. Res. Commun. 81:1978;1100-1105.
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 1100-1105
    • Ciechanover, A.1    Hod, Y.2    Hershko, A.3
  • 5
    • 0035208654 scopus 로고    scopus 로고
    • Cytosolic O-glycosylation is abundant in nerve terminals
    • Cole R.N., Hart G.W. Cytosolic O-glycosylation is abundant in nerve terminals. J. Neurochem. 79:2001;1080-1089.
    • (2001) J. Neurochem. , vol.79 , pp. 1080-1089
    • Cole, R.N.1    Hart, G.W.2
  • 6
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct
    • Conway K.A., Rochet J.-C., Bieganski R.M., Lansbury P.T. Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct. Science. 294:2001;1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.-C.2    Bieganski, R.M.3    Lansbury, P.T.4
  • 7
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang L.C., Melandri F.D., Stein R.L. Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry. 37:1998;1868-1879.
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 8
    • 0035870881 scopus 로고    scopus 로고
    • Inducible expression of mutant α-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
    • Engelender T.Y., Igarashi S., Rao R.K., Wanner T., Tanzi R.E., Sawa A.L., Dawson V., Dawson T.M., Ross C.A. Inducible expression of mutant α-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis. Hum. Mol. Genet. 10:2001;919-926.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 919-926
    • Engelender, T.Y.1    Igarashi, S.2    Rao, R.K.3    Wanner, T.4    Tanzi, R.E.5    Sawa, A.L.6    Dawson, V.7    Dawson, T.M.8    Ross, C.A.9
  • 9
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G., Standaert R.F., Lane W.S., Choi S., Corey E.J., Schreiber S.L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science. 268:1995;726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 11
    • 0031662116 scopus 로고    scopus 로고
    • Bioenergetic characterization of gamma-aminobutyric acid transporter of synaptic vesicles
    • Hell J.W., Jahn R. Bioenergetic characterization of gamma-aminobutyric acid transporter of synaptic vesicles. Methods Enzymol. 296:1998;116-124.
    • (1998) Methods Enzymol. , vol.296 , pp. 116-124
    • Hell, J.W.1    Jahn, R.2
  • 12
    • 0035958926 scopus 로고    scopus 로고
    • In vitro assembly and recognition of Lys-63 polyubiquitin chains
    • Hofmann R.M., Pickart C.M. In vitro assembly and recognition of Lys-63 polyubiquitin chains. J. Biol. Chem. 276:2001;27936-27943.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27936-27943
    • Hofmann, R.M.1    Pickart, C.M.2
  • 13
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution
    • Johnston S.C., Larsen C.N., Cook W.J., Wilkinson K.D., Hill C.P. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J. 16:1997;3787-3796.
    • (1997) EMBO J. , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 14
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston S.C., Riddle S.M., Cohen R.E., Hill C.P. Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18:1999;3877-3887.
    • (1999) EMBO J. , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 16
    • 0035444169 scopus 로고    scopus 로고
    • Loss of Uch-L1 and Uch-L3 leads to neurodegeneration, posterior paralysis and dysphagia
    • Kurihara L.J., Kikuchi T., Wada K., Tilghman S.M. Loss of Uch-L1 and Uch-L3 leads to neurodegeneration, posterior paralysis and dysphagia. Hum. Mol. Genet. 10:2001;1963-1970.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1963-1970
    • Kurihara, L.J.1    Kikuchi, T.2    Wada, K.3    Tilghman, S.M.4
  • 18
    • 0036591668 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease and biochemical studies of implicated gene products
    • Lansbury P.T. Jr., Brice A. Genetics of Parkinson's disease and biochemical studies of implicated gene products. Curr. Opin. Genet. Dev. 12:2002;299-306.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 299-306
    • Lansbury, P.T.1    Brice, A.2
  • 19
    • 0029999683 scopus 로고    scopus 로고
    • Substrate binding and catalysis by ubiquitin C-terminal hydrolases: Identification of two active site residues
    • Larsen C.N., Price J.S., Wilkinson K.D. Substrate binding and catalysis by ubiquitin C-terminal hydrolases. identification of two active site residues Biochemistry. 35:1996;6735-6744.
    • (1996) Biochemistry , vol.35 , pp. 6735-6744
    • Larsen, C.N.1    Price, J.S.2    Wilkinson, K.D.3
  • 20
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: Ubiquitin C-terminal hydrolases
    • Larsen C.N., Krantz B.A., Wilkinson K.D. Substrate specificity of deubiquitinating enzymes. ubiquitin C-terminal hydrolases Biochemistry. 37:1998;3358-3368.
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 23
    • 0034864346 scopus 로고    scopus 로고
    • No genetic association of the ubiquitin carboxy-terminal hydrolase-L1 gene S18Y polymorphism with familial Parkinson's disease
    • Levecque C., Destee A., Mouroux V., Becquet E., Defebvre L., Amouyel P., Chartier-Harlin M.C. No genetic association of the ubiquitin carboxy-terminal hydrolase-L1 gene S18Y polymorphism with familial Parkinson's disease. J. Neural Transm. 108:2001;979-984.
    • (2001) J. Neural Transm. , vol.108 , pp. 979-984
    • Levecque, C.1    Destee, A.2    Mouroux, V.3    Becquet, E.4    Defebvre, L.5    Amouyel, P.6    Chartier-Harlin, M.C.7
  • 24
    • 0033544368 scopus 로고    scopus 로고
    • Case-control study of the ubiquitin carboxy-terminal hydrolase L1 gene in Parkinson's disease
    • Maraganore D.M., Farrer M.J., Hardy J.A., Lincoln S.J., McDonnell S.K., Rocca W.A. Case-control study of the ubiquitin carboxy-terminal hydrolase L1 gene in Parkinson's disease. Neurology. 53:1999;1858-1860.
    • (1999) Neurology , vol.53 , pp. 1858-1860
    • Maraganore, D.M.1    Farrer, M.J.2    Hardy, J.A.3    Lincoln, S.J.4    McDonnell, S.K.5    Rocca, W.A.6
  • 25
    • 0033578781 scopus 로고    scopus 로고
    • E2/E3-mediated assembly of lysine 29-linked polyubiquitin chains
    • Mastrandrea L.D., You J., Niles E.G., Pickart C.M. E2/E3-mediated assembly of lysine 29-linked polyubiquitin chains. J. Biol. Chem. 274:1999;27299-27306.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27299-27306
    • Mastrandrea, L.D.1    You, J.2    Niles, E.G.3    Pickart, C.M.4
  • 28
    • 0036316947 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures
    • McNaught K.S., Mytilineou C., JnoBaptiste R., Yabut J., Shashidharan P., Jenner P., Olanow C.W. Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures. J. Neurochem. 81:2002;301-306. b.
    • (2002) J. Neurochem. , vol.81 , pp. 301-306
    • McNaught, K.S.1    Mytilineou, C.2    JnoBaptiste, R.3    Yabut, J.4    Shashidharan, P.5    Jenner, P.6    Olanow, C.W.7
  • 29
    • 0027467185 scopus 로고
    • Progressive degeneration of motor nerve terminals in GAD mutant mouse with hereditary sensory axonopathy
    • Miura H., Oda K., Endo C., Yamazaki K., Shibasaki H., Kikuchi T. Progressive degeneration of motor nerve terminals in GAD mutant mouse with hereditary sensory axonopathy. Neuropathol. Appl. Neurobiol. 19:1993;41-51.
    • (1993) Neuropathol. Appl. Neurobiol. , vol.19 , pp. 41-51
    • Miura, H.1    Oda, K.2    Endo, C.3    Yamazaki, K.4    Shibasaki, H.5    Kikuchi, T.6
  • 30
    • 0036135090 scopus 로고    scopus 로고
    • Association studies of multiple candidate genes for Parkinson's disease using single nucleotide polymorphisms
    • Momose Y., Murata M., Kobayashi K., Tachikawa M., Nakabayashi Y., Kanazawa I., Toda T. Association studies of multiple candidate genes for Parkinson's disease using single nucleotide polymorphisms. Ann. Neurol. 51:2002;133-136.
    • (2002) Ann. Neurol. , vol.51 , pp. 133-136
    • Momose, Y.1    Murata, M.2    Kobayashi, K.3    Tachikawa, M.4    Nakabayashi, Y.5    Kanazawa, I.6    Toda, T.7
  • 32
    • 0024810802 scopus 로고
    • Neuropathology of gracile axonal dystrophy (GAD) mouse. An animal model of central distal axonopathy in primary sensory neurons
    • Mukoyama M., Yamazaki K., Kikuchi T., Tomita T. Neuropathology of gracile axonal dystrophy (GAD) mouse. An animal model of central distal axonopathy in primary sensory neurons. Acta Neuropathol. 79:1989;294-299.
    • (1989) Acta Neuropathol. , vol.79 , pp. 294-299
    • Mukoyama, M.1    Yamazaki, K.2    Kikuchi, T.3    Tomita, T.4
  • 33
    • 0037008355 scopus 로고    scopus 로고
    • Mutation analysis and association studies of ubiquitin carboxy-terminal hydrolase L1 gene in Huntington's disease
    • Naze P., Vuillaume I., Destee A., Pasquier F., Sablonniere B. Mutation analysis and association studies of ubiquitin carboxy-terminal hydrolase L1 gene in Huntington's disease. Neurosci. Lett. 328:2002;1-4.
    • (2002) Neurosci. Lett. , vol.328 , pp. 1-4
    • Naze, P.1    Vuillaume, I.2    Destee, A.3    Pasquier, F.4    Sablonniere, B.5
  • 34
    • 0026547946 scopus 로고
    • Dying back type axonal degeneration of sensory nerve terminals in muscle spindles of the gracile axonal dystrophy (GAD) mutant mouse
    • Oda K., Yamazaki K., Miura H., Shibasaki H., Kikuchi T. Dying back type axonal degeneration of sensory nerve terminals in muscle spindles of the gracile axonal dystrophy (GAD) mutant mouse. Neuropathol. Appl. Neurobiol. 18:1992;265-281.
    • (1992) Neuropathol. Appl. Neurobiol. , vol.18 , pp. 265-281
    • Oda, K.1    Yamazaki, K.2    Miura, H.3    Shibasaki, H.4    Kikuchi, T.5
  • 35
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 36
    • 0034884622 scopus 로고    scopus 로고
    • Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells
    • Rideout H.J., Larsen K.E., Sulzer D., Stefanis L. Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells. J. Neurochem. 78:2001;899-908.
    • (2001) J. Neurochem. , vol.78 , pp. 899-908
    • Rideout, H.J.1    Larsen, K.E.2    Sulzer, D.3    Stefanis, L.4
  • 37
  • 39
    • 0035881339 scopus 로고    scopus 로고
    • A polymorphic variation of serine to tyrosine at codon 18 in the ubiquitin C-terminal hydrolase-L1 gene is associated with a reduced risk of sporadic Parkinson's disease in a Japanese population
    • Satoh J., Kuroda Y. A polymorphic variation of serine to tyrosine at codon 18 in the ubiquitin C-terminal hydrolase-L1 gene is associated with a reduced risk of sporadic Parkinson's disease in a Japanese population. J. Neurol. Sci. 189:2001;113-117.
    • (2001) J. Neurol. Sci. , vol.189 , pp. 113-117
    • Satoh, J.1    Kuroda, Y.2
  • 40
    • 0037177250 scopus 로고    scopus 로고
    • Molecular crowding accelerates fibrillization of alpha-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease?
    • Shtilerman M.D., Ding T.T., Lansbury P.T. Jr. Molecular crowding accelerates fibrillization of alpha-synuclein. could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry. 41:2002;3855-3860.
    • (2002) Biochemistry , vol.41 , pp. 3855-3860
    • Shtilerman, M.D.1    Ding, T.T.2    Lansbury, P.T.3
  • 41
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford W.F. 3rd. Boundary analysis in sedimentation transport experiments. a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile Anal. Biochem. 203:1992;295-301.
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford W.F. III1
  • 42
    • 0035976835 scopus 로고    scopus 로고
    • Alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris G.K., Layfield R., 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
  • 43
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer
    • VanDemark A.P., Hofmann R.M., Tsui C., Pickart C.M., Wolberger C. Molecular insights into polyubiquitin chain assembly. crystal structure of the Mms2/Ubc13 heterodimer Cell. 105:2001;711-720.
    • (2001) Cell , vol.105 , pp. 711-720
    • VanDemark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 44
    • 0036654541 scopus 로고    scopus 로고
    • ACT and UCH-L1 polymorphisms in Parkinson's disease and age of onset
    • Wang J., Zhao C.-Y., Si Y.-M., Liu Z.-L., Chen B., Yu L. ACT and UCH-L1 polymorphisms in Parkinson's disease and age of onset. Mov. Disord. 17:2002;767-771.
    • (2002) Mov. Disord. , vol.17 , pp. 767-771
    • Wang, J.1    Zhao, C.-Y.2    Si, Y.-M.3    Liu, Z.-L.4    Chen, B.5    Yu, L.6
  • 45
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman A.M. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2:2001;169-178.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 47
    • 0029133951 scopus 로고
    • Ubiquitin immunoreactivity in the central nervous system of gracile axonal dystrophy (GAD) mouse
    • Wu J., Ichihara N., Chui D.H., Yamazaki K., Kikuchi T. Ubiquitin immunoreactivity in the central nervous system of gracile axonal dystrophy (GAD) mouse. No To Shinkei. 47:1995;881-885.
    • (1995) No To Shinkei , vol.47 , pp. 881-885
    • Wu, J.1    Ichihara, N.2    Chui, D.H.3    Yamazaki, K.4    Kikuchi, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.