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Volumn 43, Issue 1, 2011, Pages 9-16

K63-linked ubiquitination and neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; DJ 1 PROTEIN; HISTONE DEACETYLASE 6; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PARKIN; PROTEASOME; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME 13; UBIQUITIN LINKED VIA LYSINE 48; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 79955978424     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2010.08.001     Document Type: Review
Times cited : (62)

References (102)
  • 1
    • 33748741301 scopus 로고    scopus 로고
    • CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation
    • Al-Ramahi I., et al. CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation. J. Biol. Chem. 2006, 281:26714-26724.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26714-26724
    • Al-Ramahi, I.1
  • 2
    • 33749570292 scopus 로고    scopus 로고
    • Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease
    • Anderson J.P., et al. Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J. Biol. Chem. 2006, 281:29739-29752.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29739-29752
    • Anderson, J.P.1
  • 3
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Arnason T., Ellison M.J. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol. 1994, 14:7876-7883.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.J.2
  • 4
    • 51149121890 scopus 로고    scopus 로고
    • Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies
    • Bedford L., et al. Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies. J. Neurosci. 2008, 28:8189-8198.
    • (2008) J. Neurosci. , vol.28 , pp. 8189-8198
    • Bedford, L.1
  • 5
    • 34547807613 scopus 로고    scopus 로고
    • Global changes to the ubiquitin system in Huntington's disease
    • Bennett E.J., et al. Global changes to the ubiquitin system in Huntington's disease. Nature 2007, 448:704-708.
    • (2007) Nature , vol.448 , pp. 704-708
    • Bennett, E.J.1
  • 6
    • 33745612296 scopus 로고    scopus 로고
    • Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system
    • Betarbet R., et al. Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system. Neurobiol. Dis. 2006, 22:404-420.
    • (2006) Neurobiol. Dis. , vol.22 , pp. 404-420
    • Betarbet, R.1
  • 7
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G., et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 2005, 171:603-614.
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjorkoy, G.1
  • 8
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • Bowman A.B., et al. Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum. Mol. Genet. 2005, 14:679-691.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 679-691
    • Bowman, A.B.1
  • 9
    • 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., et al. Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat. Med. 2001, 7:1144-1150.
    • (2001) Nat. Med. , vol.7 , pp. 1144-1150
    • Chung, K.K.1
  • 10
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: biological regulation via destruction
    • Ciechanover A., et al. Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 2000, 22:442-451.
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1
  • 11
    • 33845600006 scopus 로고    scopus 로고
    • Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities
    • Crosas B., et al. Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 2006, 127:1401-1413.
    • (2006) Cell , vol.127 , pp. 1401-1413
    • Crosas, B.1
  • 12
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda R.K., et al. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J. Biol. Chem. 2009, 284:13843-13855.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13843-13855
    • Dagda, R.K.1
  • 13
    • 76949087985 scopus 로고    scopus 로고
    • Mitochondrial quality control: insights on how Parkinson's disease related genes PINK1, parkin, and Omi/HtrA2 interact to maintain mitochondrial homeostasis
    • Dagda R.K., Chu C.T. Mitochondrial quality control: insights on how Parkinson's disease related genes PINK1, parkin, and Omi/HtrA2 interact to maintain mitochondrial homeostasis. J. Bioenerg. Biomembr. 2009, 41:473-479.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 473-479
    • Dagda, R.K.1    Chu, C.T.2
  • 14
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L., et al. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000, 103:351-361.
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1
  • 15
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • Dickey C.A., et al. The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J. Clin. Invest. 2007, 117:648-658.
    • (2007) J. Clin. Invest. , vol.117 , pp. 648-658
    • Dickey, C.A.1
  • 16
    • 20444450523 scopus 로고    scopus 로고
    • Alpha-synuclein and parkin contribute to the assembly of ubiquitin lysine 63-linked multiubiquitin chains
    • Doss-Pepe E.W., et al. Alpha-synuclein and parkin contribute to the assembly of ubiquitin lysine 63-linked multiubiquitin chains. J. Biol. Chem. 2005, 280:16619-16624.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16619-16624
    • Doss-Pepe, E.W.1
  • 17
    • 33646147146 scopus 로고    scopus 로고
    • Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules
    • Duncan L.M., et al. Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules. EMBO J. 2006, 25:1635-1645.
    • (2006) EMBO J. , vol.25 , pp. 1635-1645
    • Duncan, L.M.1
  • 18
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • Fisk H.A., Yaffe M.P. A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 1999, 145:1199-1208.
    • (1999) J. Cell Biol. , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 19
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan J.M., Haguenauer-Tsapis R. Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 1997, 16:5847-5854.
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 20
    • 26944484011 scopus 로고    scopus 로고
    • Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling
    • Geetha T., et al. Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling. Mol. Cell 2005, 20:301-312.
    • (2005) Mol. Cell , vol.20 , pp. 301-312
    • Geetha, T.1
  • 21
    • 75949130828 scopus 로고    scopus 로고
    • PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
    • Geisler S., et al. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat. Cell Biol. 2010, 12:119-131.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 119-131
    • Geisler, S.1
  • 22
    • 3242732994 scopus 로고    scopus 로고
    • Protective effects of mutant ubiquitin in transgenic mice
    • Gray D.A., et al. Protective effects of mutant ubiquitin in transgenic mice. Ann. NY Acad. Sci. 2004, 1019:215-218.
    • (2004) Ann. NY Acad. Sci. , vol.1019 , pp. 215-218
    • Gray, D.A.1
  • 23
    • 33745280651 scopus 로고    scopus 로고
    • Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity
    • Hampe C., et al. Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity. Hum. Mol. Genet. 2006, 15:2059-2075.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2059-2075
    • Hampe, C.1
  • 24
    • 33749049581 scopus 로고    scopus 로고
    • Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation
    • Hanna J., et al. Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 2006, 127:99-111.
    • (2006) Cell , vol.127 , pp. 99-111
    • Hanna, J.1
  • 25
    • 33847191686 scopus 로고    scopus 로고
    • Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling
    • Henn I.H., et al. Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling. J. Neurosci. 2007, 27:1868-1878.
    • (2007) J. Neurosci. , vol.27 , pp. 1868-1878
    • Henn, I.H.1
  • 26
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann R.M., Pickart C.M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 1999, 96:645-653.
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 27
    • 0041430614 scopus 로고    scopus 로고
    • Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease
    • Hoglinger G.U., et al. Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease. J. Neurochem. 2003, 86:1297-1307.
    • (2003) J. Neurochem. , vol.86 , pp. 1297-1307
    • Hoglinger, G.U.1
  • 28
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y., et al. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 2001, 105:891-902.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1
  • 29
    • 72149130935 scopus 로고    scopus 로고
    • The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26s proteasome
    • Jacobson A.D., et al. The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26s proteasome. J. Biol. Chem. 2009, 284:35485-35494.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35485-35494
    • Jacobson, A.D.1
  • 30
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • Jana N.R., et al. Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J. Biol. Chem. 2005, 280:11635-11640.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1
  • 31
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi Y., et al. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 2003, 115:727-738.
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1
  • 32
    • 34547130325 scopus 로고    scopus 로고
    • Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages
    • Kim H.T., et al. Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J. Biol. Chem. 2007, 282:17375-17386.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17375-17386
    • Kim, H.T.1
  • 33
    • 67650427174 scopus 로고    scopus 로고
    • S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains
    • Kim H.T., et al. S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains. EMBO J. 2009, 28:1867-1877.
    • (2009) EMBO J. , vol.28 , pp. 1867-1877
    • Kim, H.T.1
  • 34
    • 56049091236 scopus 로고    scopus 로고
    • PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
    • Kim Y., et al. PINK1 controls mitochondrial localization of Parkin through direct phosphorylation. Biochem. Biophys. Res. Commun. 2008, 377:975-980.
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 975-980
    • Kim, Y.1
  • 35
    • 60849099049 scopus 로고    scopus 로고
    • A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
    • Kirkin V., et al. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol. Cell 2009, 33:505-516.
    • (2009) Mol. Cell , vol.33 , pp. 505-516
    • Kirkin, V.1
  • 36
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V., et al. A role for ubiquitin in selective autophagy. Mol. Cell 2009, 34:259-269.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1
  • 37
    • 62449124769 scopus 로고    scopus 로고
    • CHIP regulates leucine-rich repeat kinase-2 ubiquitination, degradation, and toxicity
    • Ko H.S., et al. CHIP regulates leucine-rich repeat kinase-2 ubiquitination, degradation, and toxicity. Proc. Natl Acad. Sci. USA 2009, 106:2897-2902.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 2897-2902
    • Ko, H.S.1
  • 38
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000, 10:524-530.
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 39
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • Kovalenko A., et al. The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 2003, 424:801-805.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1
  • 40
    • 77649337122 scopus 로고    scopus 로고
    • HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy
    • Lee J.Y., et al. HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy. EMBO J. 2010, 29:969-980.
    • (2010) EMBO J. , vol.29 , pp. 969-980
    • Lee, J.Y.1
  • 41
    • 77952326081 scopus 로고    scopus 로고
    • Disease-causing mutations in Parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy
    • Lee J.Y., et al. Disease-causing mutations in Parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J. Cell Biol. 2010, 189:671-679.
    • (2010) J. Cell Biol. , vol.189 , pp. 671-679
    • Lee, J.Y.1
  • 42
    • 20044386298 scopus 로고    scopus 로고
    • Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation
    • Lim K.L., et al. Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J. Neurosci. 2005, 25:2002-2009.
    • (2005) J. Neurosci. , vol.25 , pp. 2002-2009
    • Lim, K.L.1
  • 43
    • 33344456519 scopus 로고    scopus 로고
    • Parkin-mediated lysine 63-linked polyubiquitination: a link to protein inclusions formation in Parkinson's and other conformational diseases?
    • Lim K.L., et al. Parkin-mediated lysine 63-linked polyubiquitination: a link to protein inclusions formation in Parkinson's and other conformational diseases?. Neurobiol. Aging 2006, 27:524-529.
    • (2006) Neurobiol. Aging , vol.27 , pp. 524-529
    • Lim, K.L.1
  • 44
    • 34347260686 scopus 로고    scopus 로고
    • Assembly of lysine 63-linked ubiquitin conjugates by phosphorylated alpha-synuclein implies Lewy body biogenesis
    • Liu C., et al. Assembly of lysine 63-linked ubiquitin conjugates by phosphorylated alpha-synuclein implies Lewy body biogenesis. J. Biol. Chem. 2007, 282:14558-14566.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14558-14566
    • Liu, C.1
  • 45
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
    • Liu Y., et al. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility. Cell 2002, 111:209-218.
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1
  • 46
    • 33645635706 scopus 로고    scopus 로고
    • Diverse effects of pathogenic mutations of Parkin that catalyze multiple monoubiquitylation in vitro
    • Matsuda N., et al. Diverse effects of pathogenic mutations of Parkin that catalyze multiple monoubiquitylation in vitro. J. Biol. Chem. 2006, 281:3204-3209.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3204-3209
    • Matsuda, N.1
  • 47
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda N., et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J. Cell Biol. 2010, 189:211-221.
    • (2010) J. Cell Biol. , vol.189 , pp. 211-221
    • Matsuda, N.1
  • 48
    • 69549131138 scopus 로고    scopus 로고
    • Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment
    • Maynard C.J., et al. Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment. Proc. Natl Acad. Sci. USA 2009, 106:13986-13991.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13986-13991
    • Maynard, C.J.1
  • 49
    • 0035955731 scopus 로고    scopus 로고
    • Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination
    • McKenna S., et al. Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination. J. Biol. Chem. 2001, 276:40120-40126.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40120-40126
    • McKenna, S.1
  • 50
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N., et al. Autophagy fights disease through cellular self-digestion. Nature 2008, 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1
  • 51
    • 0346434141 scopus 로고    scopus 로고
    • A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization
    • Moore D.J., et al. A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization. J. Neurochem. 2003, 87:1558-1567.
    • (2003) J. Neurochem. , vol.87 , pp. 1558-1567
    • Moore, D.J.1
  • 52
    • 50449092205 scopus 로고    scopus 로고
    • Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks
    • Motegi A., et al. Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks. Proc. Natl Acad. Sci. USA 2008, 105:12411-12416.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 12411-12416
    • Motegi, A.1
  • 53
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D., et al. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 2008, 183:795-803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1
  • 54
    • 1542349213 scopus 로고    scopus 로고
    • Familial Parkinson's disease-associated L166P mutation disrupts DJ-1 protein folding and function
    • Olzmann J.A., et al. Familial Parkinson's disease-associated L166P mutation disrupts DJ-1 protein folding and function. J. Biol. Chem. 2004, 279:8506-8515.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8506-8515
    • Olzmann, J.A.1
  • 55
    • 34548851476 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6
    • Olzmann J.A., et al. Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J. Cell Biol. 2007, 178:1025-1038.
    • (2007) J. Cell Biol. , vol.178 , pp. 1025-1038
    • Olzmann, J.A.1
  • 56
    • 77949352928 scopus 로고    scopus 로고
    • Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation
    • Ortega Z., et al. Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation. J. Neurosci. 2010, 30:3675-3688.
    • (2010) J. Neurosci. , vol.30 , pp. 3675-3688
    • Ortega, Z.1
  • 57
    • 67449131894 scopus 로고    scopus 로고
    • Immunoreactivity to Lys63-linked polyubiquitin is a feature of neurodegeneration
    • Paine S., et al. Immunoreactivity to Lys63-linked polyubiquitin is a feature of neurodegeneration. Neurosci. Lett. 2009, 460:205-208.
    • (2009) Neurosci. Lett. , vol.460 , pp. 205-208
    • Paine, S.1
  • 58
    • 34548259958 scopus 로고    scopus 로고
    • P62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv S., et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J. Biol. Chem. 2007, 282:24131-24145.
    • (2007) J. Biol. Chem. , vol.282 , pp. 24131-24145
    • Pankiv, S.1
  • 59
    • 0041706156 scopus 로고    scopus 로고
    • A proteomics approach to understanding protein ubiquitination
    • Peng J., et al. A proteomics approach to understanding protein ubiquitination. Nat. Biotechnol. 2003, 21:921-926.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 921-926
    • Peng, J.1
  • 60
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli L., et al. Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron 2002, 36:1007-1019.
    • (2002) Neuron , vol.36 , pp. 1007-1019
    • Petrucelli, L.1
  • 61
  • 62
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, 10(Suppl):S10-S17.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 63
    • 41249090880 scopus 로고    scopus 로고
    • Monoubiquitylation of alpha-synuclein by seven in absentia homolog (SIAH) promotes its aggregation in dopaminergic cells
    • Rott R., et al. Monoubiquitylation of alpha-synuclein by seven in absentia homolog (SIAH) promotes its aggregation in dopaminergic cells. J. Biol. Chem. 2008, 283:3316-3328.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3316-3328
    • Rott, R.1
  • 64
    • 60549107173 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
    • Saeki Y., et al. Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. EMBO J. 2009, 28:359-371.
    • (2009) EMBO J. , vol.28 , pp. 359-371
    • Saeki, Y.1
  • 65
    • 52149103164 scopus 로고    scopus 로고
    • Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains
    • Sato Y., et al. Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains. Nature 2008, 455:358-362.
    • (2008) Nature , vol.455 , pp. 358-362
    • Sato, Y.1
  • 66
    • 77950658888 scopus 로고    scopus 로고
    • Multiplex SILAC analysis of a cellular TDP-43 proteinopathy model reveals protein inclusions associated with SUMOylation and diverse polyubiquitin chains
    • Seyfried N.T., et al. Multiplex SILAC analysis of a cellular TDP-43 proteinopathy model reveals protein inclusions associated with SUMOylation and diverse polyubiquitin chains. Mol. Cell. Proteomics 2010, 9:705-718.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 705-718
    • Seyfried, N.T.1
  • 67
    • 77949478474 scopus 로고    scopus 로고
    • Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling
    • Sha D., et al. Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Hum. Mol. Genet. 2010, 19:352-363.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 352-363
    • Sha, D.1
  • 68
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H., et al. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat. Genet. 2000, 25:302-305.
    • (2000) Nat. Genet. , vol.25 , pp. 302-305
    • Shimura, H.1
  • 69
    • 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., et al. The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways. J. Biol. Chem. 2005, 280:23727-23734.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23727-23734
    • Shin, Y.1
  • 70
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence J., et al. Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell 2000, 102:67-76.
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1
  • 71
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J., et al. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 1995, 15:1265-1273.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1
  • 72
    • 2442645048 scopus 로고    scopus 로고
    • Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover
    • Sullivan P.G., et al. Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover. J. Biol. Chem. 2004, 279:20699-20707.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20699-20707
    • Sullivan, P.G.1
  • 73
    • 70349252765 scopus 로고    scopus 로고
    • Mitochondrial accumulation of polyubiquitinated proteins and differential regulation of apoptosis by polyubiquitination sites Lys-48 and -63
    • Sun F., et al. Mitochondrial accumulation of polyubiquitinated proteins and differential regulation of apoptosis by polyubiquitination sites Lys-48 and -63. J. Cell. Mol. Med. 2009, 13:1632-1643.
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 1632-1643
    • Sun, F.1
  • 74
    • 38949162988 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy
    • Tan J.M., et al. Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy. Autophagy 2008, 4:251-253.
    • (2008) Autophagy , vol.4 , pp. 251-253
    • Tan, J.M.1
  • 75
    • 38349114036 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
    • Tan J.M., et al. Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum. Mol. Genet. 2008, 17:431-439.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 431-439
    • Tan, J.M.1
  • 76
    • 67649374865 scopus 로고    scopus 로고
    • Protein misfolding and aggregation in Parkinson's disease
    • Tan J.M., et al. Protein misfolding and aggregation in Parkinson's disease. Antioxid. Redox Signal. 2009, 11:2119-2134.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2119-2134
    • Tan, J.M.1
  • 77
    • 68149170034 scopus 로고    scopus 로고
    • ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways
    • Tao M., et al. ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways. Curr. Biol. 2009, 19:1255-1263.
    • (2009) Curr. Biol. , vol.19 , pp. 1255-1263
    • Tao, M.1
  • 78
    • 5644259751 scopus 로고    scopus 로고
    • Structural basis for distinct roles of Lys63- and Lys48-linked polyubiquitin chains
    • Tenno T., et al. Structural basis for distinct roles of Lys63- and Lys48-linked polyubiquitin chains. Genes Cells 2004, 9:865-875.
    • (2004) Genes Cells , vol.9 , pp. 865-875
    • Tenno, T.1
  • 79
    • 60549100850 scopus 로고    scopus 로고
    • Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3
    • Todi S.V., et al. Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3. EMBO J. 2009, 28:372-382.
    • (2009) EMBO J. , vol.28 , pp. 372-382
    • Todi, S.V.1
  • 80
    • 0242666359 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function
    • Tofaris G.K., et al. Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function. J. Biol. Chem. 2003, 278:44405-44411.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44405-44411
    • Tofaris, G.K.1
  • 81
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E., et al. CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 2003, 424:793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1
  • 82
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai Y.C., et al. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J. Biol. Chem. 2003, 278:22044-22055.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1
  • 83
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer
    • VanDemark A.P., et al. Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. Cell 2001, 105:711-720.
    • (2001) Cell , vol.105 , pp. 711-720
    • VanDemark, A.P.1
  • 84
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling
    • Varadan R., et al. Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. J. Biol. Chem. 2004, 279:7055-7063.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7055-7063
    • Varadan, R.1
  • 85
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman P., et al. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol. Cell 2004, 14:95-104.
    • (2004) Mol. Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1
  • 86
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef L.G., et al. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 2002, 11:2689-2700.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1
  • 87
    • 77951221830 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitination of the dopamine transporter requires WW3 and WW4 domains of Nedd4-2 and UBE2D ubiquitin-conjugating enzymes
    • Vina-Vilaseca A., Sorkin A. Lysine 63-linked polyubiquitination of the dopamine transporter requires WW3 and WW4 domains of Nedd4-2 and UBE2D ubiquitin-conjugating enzymes. J. Biol. Chem. 2010, 285:7645-7656.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7645-7656
    • Vina-Vilaseca, A.1    Sorkin, A.2
  • 88
    • 75949098487 scopus 로고    scopus 로고
    • PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
    • Vives-Bauza C., et al. PINK1-dependent recruitment of Parkin to mitochondria in mitophagy. Proc. Natl Acad. Sci. USA 2010, 107:378-383.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 378-383
    • Vives-Bauza, C.1
  • 89
    • 28544453333 scopus 로고    scopus 로고
    • Chromosome alignment and segregation regulated by ubiquitination of survivin
    • Vong Q.P., et al. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science 2005, 310:1499-1504.
    • (2005) Science , vol.310 , pp. 1499-1504
    • Vong, Q.P.1
  • 90
    • 29644448325 scopus 로고    scopus 로고
    • Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function
    • Wang C., et al. Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function. Hum. Mol. Genet. 2005, 14:3885-3897.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3885-3897
    • Wang, C.1
  • 91
    • 29644448325 scopus 로고    scopus 로고
    • Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function
    • Wang C., et al. Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function. Hum. Mol. Genet. 2005, 14:3885-3897.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3885-3897
    • Wang, C.1
  • 92
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling
    • Wertz I.E., et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. Nature 2004, 430:694-699.
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1
  • 93
    • 55549086868 scopus 로고    scopus 로고
    • The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains
    • Winborn B.J., et al. The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains. J. Biol. Chem. 2008, 283:26436-26443.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26436-26443
    • Winborn, B.J.1
  • 94
    • 77953487481 scopus 로고    scopus 로고
    • Dynamic role of ubiquitination in the management of misfolded proteins associated with neurodegenerative diseases
    • J. Ovadi, F. Orosz (Eds.)
    • Wong E.S., et al. Dynamic role of ubiquitination in the management of misfolded proteins associated with neurodegenerative diseases. Protein Folding and Misfolding: Neurodegenerative Diseases 2009, J. Ovadi, F. Orosz (Eds.).
    • (2009) Protein Folding and Misfolding: Neurodegenerative Diseases
    • Wong, E.S.1
  • 95
    • 48249084875 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of aggresomes is not a universal phenomenon
    • Wong E.S., et al. Autophagy-mediated clearance of aggresomes is not a universal phenomenon. Hum. Mol. Genet. 2008, 17:2570-2582.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2570-2582
    • Wong, E.S.1
  • 96
    • 42049100859 scopus 로고    scopus 로고
    • Essential role of sequestosome 1/p62 in regulating accumulation of Lys63-ubiquitinated proteins
    • Wooten M.W., et al. Essential role of sequestosome 1/p62 in regulating accumulation of Lys63-ubiquitinated proteins. J. Biol. Chem. 2008, 283:6783-6789.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6783-6789
    • Wooten, M.W.1
  • 97
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu P., et al. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 2009, 137:133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1
  • 98
    • 0036144410 scopus 로고    scopus 로고
    • P62 Is a common component of cytoplasmic inclusions in protein aggregation diseases
    • Zatloukal K., et al. p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases. Am. J. Pathol. 2002, 160:255-263.
    • (2002) Am. J. Pathol. , vol.160 , pp. 255-263
    • Zatloukal, K.1
  • 99
    • 0037663945 scopus 로고    scopus 로고
    • Effects of mutant ubiquitin on ts1 retrovirus-mediated neuropathology
    • Zhang M., et al. Effects of mutant ubiquitin on ts1 retrovirus-mediated neuropathology. J. Virol. 2003, 77:7193-7201.
    • (2003) J. Virol. , vol.77 , pp. 7193-7201
    • Zhang, M.1
  • 100
    • 27944495299 scopus 로고    scopus 로고
    • Chaperoned ubiquitylation-crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex
    • Zhang M., et al. Chaperoned ubiquitylation-crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. Mol. Cell 2005, 20:525-538.
    • (2005) Mol. Cell , vol.20 , pp. 525-538
    • Zhang, M.1
  • 101
    • 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., et al. 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, 97:13354-13359.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1
  • 102
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E., et al. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl Acad. Sci. USA 2010, 107:5018-5023.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 5018-5023
    • Ziviani, E.1


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