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Volumn 9, Issue 17, 2010, Pages 3401-3413

Does Huntingtin play a role in selective macroautophagy?

Author keywords

Autophagy; Huntingtin; Huntington's disease; IKK; Polyglutamine

Indexed keywords

HUNTINGTIN; I KAPPA B KINASE; MUTANT PROTEIN;

EID: 77956408419     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.9.17.12718     Document Type: Review
Times cited : (64)

References (162)
  • 1
    • 72149124383 scopus 로고    scopus 로고
    • IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
    • Thompson LM, Aiken CT, Kaltenbach LS, Agrawal N, Illes K, Khoshnan A, et al. IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome. J Cell Biol 2009; 187:1083-99.
    • (2009) J Cell Biol , vol.187 , pp. 1083-1099
    • Thompson, L.M.1    Aiken, C.T.2    Kaltenbach, L.S.3    Agrawal, N.4    Illes, K.5    Khoshnan, A.6
  • 2
    • 4644307407 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex and nuclear factor-kappaB contributes to mutant huntingtin neurotoxicity
    • DOI 10.1523/JNEUROSCI.2675-04.2004
    • Khoshnan A, Ko J, Watkin EE, Paige LA, Reinhart PH, Patterson PH. Activation of the IkappaB kinase complex and nuclear factor-kappaB contributes to mutant huntingtin neurotoxicity. J Neurosci 2004; 24:7999-8008. (Pubitemid 39280819)
    • (2004) Journal of Neuroscience , vol.24 , Issue.37 , pp. 7999-8008
    • Khoshnan, A.1    Ko, J.2    Watkin, E.E.3    Paige, L.A.4    Reinhart, P.H.5    Patterson, P.H.6
  • 3
    • 49249089029 scopus 로고    scopus 로고
    • A novel pathogenic pathway of immune activation detectable before clinical onset in Huntington's disease
    • Bjorkqvist M, Wild EJ, Thiele J, Silvestroni A, Andre R, Lahiri N, et al. A novel pathogenic pathway of immune activation detectable before clinical onset in Huntington's disease. J Exp Med 2008; 205:1869-77.
    • (2008) J Exp Med , vol.205 , pp. 1869-1877
    • Bjorkqvist, M.1    Wild, E.J.2    Thiele, J.3    Silvestroni, A.4    Andre, R.5    Lahiri, N.6
  • 7
    • 77449089538 scopus 로고    scopus 로고
    • A manually curated network of the PML nuclear body interactome reveals an important role for PMLNBs in SUMOylation dynamics
    • Van Damme E, Laukens K, Dang TH, Van Ostade X. A manually curated network of the PML nuclear body interactome reveals an important role for PMLNBs in SUMOylation dynamics. Int J Biol Sci 2010; 6:51-67.
    • (2010) Int J Biol Sci , vol.6 , pp. 51-67
    • Van Damme, E.1    Laukens, K.2    Dang, T.H.3    Van Ostade, X.4
  • 8
    • 34047248402 scopus 로고    scopus 로고
    • Phosphorylation of CBP by IKKalpha promotes cell growth by switching the binding preference of CBP from p53 to NFkappaB
    • Huang WC, Ju TK, Hung MC, Chen CC. Phosphorylation of CBP by IKKalpha promotes cell growth by switching the binding preference of CBP from p53 to NFkappaB. Mol Cell 2007; 26:75-87.
    • (2007) Mol Cell , vol.26 , pp. 75-87
    • Huang, W.C.1    Ju, T.K.2    Hung, M.C.3    Chen, C.C.4
  • 11
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation Targets Mutant Huntingtin to Autophagosomes for Degradation
    • Jeong H, Then F, Melia TJJ, Mazzulli JR, Cui L, Savas JN, et al. Acetylation Targets Mutant Huntingtin to Autophagosomes for Degradation. Cell 2009; 137:60-72.
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1    Then, F.2    Melia, T.J.J.3    Mazzulli, J.R.4    Cui, L.5    Savas, J.N.6
  • 12
    • 77949324195 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of p62/ SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies
    • Pankiv S, Lamark T, Bruun JA, Overvatn A, Bjorkoy G, Johansen T. Nucleocytoplasmic shuttling of p62/ SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies. J Biol Chem 2010; 285:5941-53.
    • (2010) J Biol Chem , vol.285 , pp. 5941-5953
    • Pankiv, S.1    Lamark, T.2    Bruun, J.A.3    Overvatn, A.4    Bjorkoy, G.5    Johansen, T.6
  • 13
    • 66849129318 scopus 로고    scopus 로고
    • IKKalpha and IKKbeta regulation of DNA damage-induced cleavage of huntingtin
    • Khoshnan A, Ko J, Tescu S, Brundin P, Patterson PH. IKKalpha and IKKbeta regulation of DNA damage-induced cleavage of huntingtin. PLoS One 2009; 45768.
    • (2009) PLoS One , pp. 45768
    • Khoshnan, A.1    Ko, J.2    Tescu, S.3    Brundin, P.4    Patterson, P.H.5
  • 14
    • 49649100923 scopus 로고    scopus 로고
    • SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage
    • Tan JA, Sun Y, Song J, Chen Y, Krontiris TG, Durrin LK. SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage. J Biol Chem 2008; 283:18124-34.
    • (2008) J Biol Chem , vol.283 , pp. 18124-18134
    • Tan, J.A.1    Sun, Y.2    Song, J.3    Chen, Y.4    Krontiris, T.G.5    Durrin, L.K.6
  • 18
    • 58149183257 scopus 로고    scopus 로고
    • Proteasome activation as a novel antiaging strategy
    • Chondrogianni N, Gonos ES. Proteasome activation as a novel antiaging strategy. IUBMB Life 2008; 60:651-5.
    • (2008) IUBMB Life , vol.60 , pp. 651-655
    • Chondrogianni, N.1    Gonos, E.S.2
  • 20
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: When the cleaning crew goes on strike
    • DOI 10.1016/S1474-4422(07)70076-5, PII S1474442207700765
    • Martinez-Vicente M, Cuervo AM. Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol 2007; 6:352-61. (Pubitemid 46367949)
    • (2007) Lancet Neurology , vol.6 , Issue.4 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 21
    • 59449095881 scopus 로고    scopus 로고
    • Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process
    • Tonoki A, Kuranaga E, Tomioka T, Hamazaki J, Murata S, Tanaka K, et al. Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process. Mol Cell Biol 2009; 29:1095-106.
    • (2009) Mol Cell Biol , vol.29 , pp. 1095-1106
    • Tonoki, A.1    Kuranaga, E.2    Tomioka, T.3    Hamazaki, J.4    Murata, S.5    Tanaka, K.6
  • 22
    • 48049092846 scopus 로고    scopus 로고
    • Activated caspase-6 and caspase-6-cleaved fragments of huntingtin specifically colocalize in the nucleus
    • Warby SC, Doty CN, Graham RK, Carroll JB, Yang YZ, Singaraja RR, et al. Activated caspase-6 and caspase-6-cleaved fragments of huntingtin specifically colocalize in the nucleus. Hum Mol Genet 2008; 17:2390-404.
    • (2008) Hum Mol Genet , vol.17 , pp. 2390-2404
    • Warby, S.C.1    Doty, C.N.2    Graham, R.K.3    Carroll, J.B.4    Yang, Y.Z.5    Singaraja, R.R.6
  • 23
    • 72149107077 scopus 로고    scopus 로고
    • Serines 13 and 16 are critical determinants of full-length human mutant Huntingtin induced disease pathogenesis in HD mice
    • Gu X, Greiner ER, Mishra R, Kodali R, Osmand A, Finkbeiner S, et al. Serines 13 and 16 are critical determinants of full-length human mutant Huntingtin induced disease pathogenesis in HD mice. Neuron 2009; 64:828-40.
    • (2009) Neuron , vol.64 , pp. 828-840
    • Gu, X.1    Greiner, E.R.2    Mishra, R.3    Kodali, R.4    Osmand, A.5    Finkbeiner, S.6
  • 24
    • 30744452478 scopus 로고    scopus 로고
    • Dysregulation of receptor interacting protein-2 and caspase recruitment domain only protein mediates aberrant caspase-1 activation in Huntington's disease
    • DOI 10.1523/JNEUROSCI.4181-05.2005
    • Wang X, Wang H, Figueroa BE, Zhang WH, Huo C, Guan Y, et al. Dysregulation of receptor interacting protein-2 and caspase recruitment domain only protein mediates aberrant caspase-1 activation in Huntington's disease. J Neurosci 2005; 25:11645-54. (Pubitemid 43098457)
    • (2005) Journal of Neuroscience , vol.25 , Issue.50 , pp. 11645-11654
    • Wang, X.1    Wang, H.2    Figueroa, B.E.3    Zhang, W.-H.4    Huo, C.5    Guan, Y.6    Zhang, Y.7    Bruey, J.-M.8    Reed, J.C.9    Friedlandery, R.M.10
  • 25
    • 0036850456 scopus 로고    scopus 로고
    • Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila
    • Chan HY, Warrick JM, Andriola I, Merry D, Bonini NM. Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila. Hum Mol Genet 2002; 11:2895-904.
    • (2002) Hum Mol Genet , vol.11 , pp. 2895-2904
    • Chan, H.Y.1    Warrick, J.M.2    Andriola, I.3    Merry, D.4    Bonini, N.M.5
  • 26
    • 77649186048 scopus 로고    scopus 로고
    • SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7
    • Janer A, Werner A, Takahashi-Fujigasaki J, Daret A, Fujigasaki H, Takada K, et al. SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7. Hum Mol Genet 2010; 19:181-95.
    • (2010) Hum Mol Genet , vol.19 , pp. 181-195
    • Janer, A.1    Werner, A.2    Takahashi-Fujigasaki, J.3    Daret, A.4    Fujigasaki, H.5    Takada, K.6
  • 27
    • 66749167799 scopus 로고    scopus 로고
    • Rhes, a striatal specific protein, mediates mutanthuntingtin cytotoxicity
    • Subramaniam S, Sixt KM, Barrow R, Snyder SH. Rhes, a striatal specific protein, mediates mutanthuntingtin cytotoxicity. Science 2009; 324:1327-30.
    • (2009) Science , vol.324 , pp. 1327-1330
    • Subramaniam, S.1    Sixt, K.M.2    Barrow, R.3    Snyder, S.H.4
  • 29
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos J, Bodai L, Lukacsovich T, Purcell JM, Steffan JS, Thompson LM, et al. Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum Mol Genet 2008; 17:3767-75.
    • (2008) Hum Mol Genet , vol.17 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3    Purcell, J.M.4    Steffan, J.S.5    Thompson, L.M.6
  • 30
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • Parker JA, Arango M, Abderrahmane S, Lambert E, Tourette C, Catoire H, et al. Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nat Genet 2005; 37:349-50.
    • (2005) Nat Genet , vol.37 , pp. 349-350
    • Parker, J.A.1    Arango, M.2    Abderrahmane, S.3    Lambert, E.4    Tourette, C.5    Catoire, H.6
  • 31
    • 10344259661 scopus 로고    scopus 로고
    • Degradation of the ghiconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events
    • DOI 10.1074/jbc.M404544200
    • Hung GC, Brown CR, Wolfe AB, Liu J, Chiang HL. Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. J Biol Chem 2004; 279:49138-50. (Pubitemid 39625797)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 49138-49150
    • Hung, G.-C.1    Brown, C.R.2    Wolfe, A.B.3    Liu, J.4    Chiang, H.-L.5
  • 32
    • 0343962235 scopus 로고    scopus 로고
    • The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles
    • Brown CR, McCann JA, Chiang HL. The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles. J Cell Biol 2000; 150:65-76.
    • (2000) J Cell Biol , vol.150 , pp. 65-76
    • Brown, C.R.1    McCann, J.A.2    Chiang, H.L.3
  • 33
    • 54449096709 scopus 로고    scopus 로고
    • The vacuolar import and degradation pathway merges with the endocytic pathway to deliver fructose-1,6-bisphosphatase to the vacuole for degradation
    • Brown CR, Wolfe AB, Cui D, Chiang HL. The vacuolar import and degradation pathway merges with the endocytic pathway to deliver fructose-1,6- bisphosphatase to the vacuole for degradation. J Biol Chem 2008; 283:26116-27.
    • (2008) J Biol Chem , vol.283 , pp. 26116-26127
    • Brown, C.R.1    Wolfe, A.B.2    Cui, D.3    Chiang, H.L.4
  • 34
    • 74049120137 scopus 로고    scopus 로고
    • The vacuole import and degradation pathway utilizes early steps of endocytosis and actin polymerization to deliver cargo proteins to the vacuole for degradation
    • Brown CR, Dunton D, Chiang HL. The vacuole import and degradation pathway utilizes early steps of endocytosis and actin polymerization to deliver cargo proteins to the vacuole for degradation. J Biol Chem 2010; 285:1516-28.
    • (2010) J Biol Chem , vol.285 , pp. 1516-1528
    • Brown, C.R.1    Dunton, D.2    Chiang, H.L.3
  • 35
    • 0034602377 scopus 로고    scopus 로고
    • Targeting of aminopeptidase I to the yeast vacuole is mediated by Ssa1p, a cytosolic member of the 70 kDa stress protein family
    • Silles E, Mazon MJ, Gevaert K, Goethals M, Vandekerckhove J, Leber R, et al. Targeting of aminopeptidase I to the yeast vacuole is mediated by Ssa1p, a cytosolic member of the 70 kDa stress protein family. J Biol Chem 2000; 275:34054-9.
    • (2000) J Biol Chem , vol.275 , pp. 34054-34059
    • Silles, E.1    Mazon, M.J.2    Gevaert, K.3    Goethals, M.4    Vandekerckhove, J.5    Leber, R.6
  • 36
    • 28644447348 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E05-07-0629
    • Reggiori F, Monastyrska I, Shintani T, Klionsky DJ. The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae. Mol Biol Cell 2005; 16:5843-56. (Pubitemid 41752231)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.12 , pp. 5843-5856
    • Reggiori, F.1    Monastyrska, I.2    Shintani, T.3    Klionsky, D.J.4
  • 37
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: Unanswered questions
    • Klionsky DJ. The molecular machinery of autophagy: unanswered questions. J Cell Sci 2005; 118:7-18.
    • (2005) J Cell Sci , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 38
    • 57749173129 scopus 로고    scopus 로고
    • Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae
    • Kageyama T, Suzuki K, Ohsumi Y. Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae. Biochem Biophys Res Commun 2009; 378:551-7.
    • (2009) Biochem Biophys Res Commun , vol.378 , pp. 551-557
    • Kageyama, T.1    Suzuki, K.2    Ohsumi, Y.3
  • 39
    • 33947383050 scopus 로고    scopus 로고
    • ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organism-specific genes
    • Meijer WH, van der Klei IJ, Veenhuis M, Kiel JA. ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organismspecific genes. Autophagy 2007; 3:106-16. (Pubitemid 46449098)
    • (2007) Autophagy , vol.3 , Issue.2 , pp. 106-116
    • Meijer, W.H.1    Van Der Klei, I.J.2    Veenhuis, M.3    Kiel, J.A.K.W.4
  • 40
  • 43
    • 65249106104 scopus 로고    scopus 로고
    • Regulation of autophagy by the p300 acetyltransferase
    • Lee IH, Finkel T. Regulation of autophagy by the p300 acetyltransferase. J Biol Chem 2009; 284:6322-8.
    • (2009) J Biol Chem , vol.284 , pp. 6322-6328
    • Lee, I.H.1    Finkel, T.2
  • 44
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • Yamamoto A, Cremona ML, Rothman JE. Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J Cell Biol 2006; 172:719-31.
    • (2006) J Cell Biol , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 45
    • 34447130222 scopus 로고    scopus 로고
    • Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by DNA damage and regulates wild-type and mutant huntingtin toxicity in neurons
    • DOI 10.1523/JNEUROSCI.1831-07.2007
    • Anne SL, Saudou F, Humbert S. Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by DNA damage and regulates wild-type and mutant huntingtin toxicity in neurons. J Neurosci 2007; 27:7318-28. (Pubitemid 47037570)
    • (2007) Journal of Neuroscience , vol.27 , Issue.27 , pp. 7318-7328
    • Anne, S.L.1    Saudou, F.2    Humbert, S.3
  • 46
    • 22344439156 scopus 로고    scopus 로고
    • Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: Implications for mutant huntingtin toxicity
    • DOI 10.1083/jcb.200412071
    • Luo S, Vacher C, Davies JE, Rubinsztein DC. Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity. J Cell Biol 2005; 169:647-56. (Pubitemid 41002857)
    • (2005) Journal of Cell Biology , vol.169 , Issue.4 , pp. 647-656
    • Luo, S.1    Vacher, C.2    Davies, J.E.3    Rubinsztein, D.C.4
  • 48
    • 44849117768 scopus 로고    scopus 로고
    • Akt-dependent regulation of NF-{kappa}B is controlled by mTOR and Raptor in association with IKK
    • Dan HC, Cooper MJ, Cogswell PC, Duncan JA, Ting JP, Baldwin AS. Akt-dependent regulation of NF-{kappa}B is controlled by mTOR and Raptor in association with IKK. Genes Dev 2008; 22:1490-500.
    • (2008) Genes Dev , vol.22 , pp. 1490-1500
    • Dan, H.C.1    Cooper, M.J.2    Cogswell, P.C.3    Duncan, J.A.4    Ting, J.P.5    Baldwin, A.S.6
  • 49
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 Coordinately Activates Protein Degradation by the Autophagic/Lysosomal and Proteasomal Pathways in Atrophying Muscle Cells
    • DOI 10.1016/j.cmet.2007.11.004, PII S1550413107003397
    • Zhao J, Brault JJ, Schild A, Cao P, Sandri M, Schiaffino S, et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 2007; 6:472-83. (Pubitemid 350163056)
    • (2007) Cell Metabolism , vol.6 , Issue.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6    Lecker, S.H.7    Goldberg, A.L.8
  • 51
    • 0038309329 scopus 로고    scopus 로고
    • The molecular mechanism of autophagy
    • Wang CW, Klionsky DJ. The molecular mechanism of autophagy. Mol Med 2003; 9:65-76.
    • (2003) Mol Med , vol.9 , pp. 65-76
    • Wang, C.W.1    Klionsky, D.J.2
  • 53
    • 33745365931 scopus 로고    scopus 로고
    • Proteolytic and lipolytic responses to starvation
    • Finn PF, Dice JF. Proteolytic and lipolytic responses to starvation. Nutrition 2006; 22:830-44.
    • (2006) Nutrition , vol.22 , pp. 830-844
    • Finn, P.F.1    Dice, J.F.2
  • 54
    • 33947149637 scopus 로고    scopus 로고
    • Atg19 mediates a dual interaction cargo sorting mechanism in selective autophagy
    • Chang CY, Huang WP. Atg19 mediates a dual interaction cargo sorting mechanism in selective autophagy. Mol Biol Cell 2007; 18:919-29.
    • (2007) Mol Biol Cell , vol.18 , pp. 919-929
    • Chang, C.Y.1    Huang, W.P.2
  • 55
    • 77950510302 scopus 로고    scopus 로고
    • The Cvt pathway as a model for selective autophagy
    • Lynch-Day MA, Klionsky DJ. The Cvt pathway as a model for selective autophagy. FEBS Lett 2010.
    • (2010) FEBS Lett
    • Lynch-Day, M.A.1    Klionsky, D.J.2
  • 56
    • 0037119448 scopus 로고    scopus 로고
    • Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy
    • Nice DC, Sato TK, Stromhaug PE, Emr SD, Klionsky DJ. Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy. J Biol Chem 2002; 277:30198-207.
    • (2002) J Biol Chem , vol.277 , pp. 30198-30207
    • Nice, D.C.1    Sato, T.K.2    Stromhaug, P.E.3    Emr, S.D.4    Klionsky, D.J.5
  • 57
    • 16344365254 scopus 로고    scopus 로고
    • Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to vacuole targeting pathway
    • DOI 10.1091/mbc.E04-11-1035
    • Yorimitsu T, Klionsky DJ. Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to vacuole targeting pathway. Mol Biol Cell 2005; 16:1593-605. (Pubitemid 40471933)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.4 , pp. 1593-1605
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 58
    • 34547924464 scopus 로고    scopus 로고
    • Optineurin Negatively Regulates TNFalpha- Induced NF-kappaB Activation by Competing with NEMO for Ubiquitinated RIP
    • DOI 10.1016/j.cub.2007.07.041, PII S0960982207017216
    • Zhu G, Wu CJ, Zhao Y, Ashwell JD. Optineurin negatively regulates TNFalpha- induced NFkappaB activation by competing with NEMO for ubiquitinated RIP. Curr Biol 2007; 17:1438-43. (Pubitemid 47259388)
    • (2007) Current Biology , vol.17 , Issue.16 , pp. 1438-1443
    • Zhu, G.1    Wu, C.-J.2    Zhao, Y.3    Ashwell, J.D.4
  • 59
    • 0034649661 scopus 로고    scopus 로고
    • FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates, cellular morphogenesis
    • DOI 10.1016/S0960-9822(00)00864-2
    • Hattula K, Peranen J. FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis. Curr Biol 2000; 10:1603-6. (Pubitemid 32062664)
    • (2000) Current Biology , vol.10 , Issue.24 , pp. 1603-1606
    • Hattula, K.1    Peranen, J.2
  • 61
    • 77951745194 scopus 로고    scopus 로고
    • Genetic bases for glaucoma
    • Fuse N. Genetic bases for glaucoma. Tohoku J Exp Med 2010; 221:1-10.
    • (2010) Tohoku J Exp Med , vol.221 , pp. 1-10
    • Fuse, N.1
  • 63
    • 10944230901 scopus 로고    scopus 로고
    • The phox homology (PX) domain protein interaction network in yeast
    • DOI 10.1074/mcp.M400081-MCP200
    • Vollert CS, Uetz P. The phox homology (PX) domain protein interaction network in yeast. Mol Cell Proteomics 2004; 3:1053-64. (Pubitemid 40012099)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.11 , pp. 1053-1064
    • Vollert, C.S.1    Uetz, P.2
  • 64
    • 58149473473 scopus 로고    scopus 로고
    • Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism
    • Chan EY, Longatti A, McKnight NC, Tooze SA. Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism. Mol Cell Biol 2009; 29:157-71.
    • (2009) Mol Cell Biol , vol.29 , pp. 157-171
    • Chan, E.Y.1    Longatti, A.2    McKnight, N.C.3    Tooze, S.A.4
  • 66
    • 39749119904 scopus 로고    scopus 로고
    • FIP200, a key signaling node to coordinately regulate various cellular processes
    • DOI 10.1016/j.cellsig.2007.10.021, PII S0898656807003245
    • Gan B, Guan JL. FIP200, a key signaling node to coordinately regulate various cellular processes. Cell Signal 2008; 20:787-94. (Pubitemid 351312869)
    • (2008) Cellular Signalling , vol.20 , Issue.5 , pp. 787-794
    • Gan, B.1    Guan, J.-L.2
  • 67
    • 77950465542 scopus 로고    scopus 로고
    • Current knowledge of the preautophagosomal structure (PAS)
    • Suzuki K, Ohsumi Y. Current knowledge of the preautophagosomal structure (PAS). FEBS Lett 2010; 584:1280-6.
    • (2010) FEBS Lett , vol.584 , pp. 1280-1286
    • Suzuki, K.1    Ohsumi, Y.2
  • 68
    • 0030807624 scopus 로고    scopus 로고
    • A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole
    • DOI 10.1083/jcb.138.3.517
    • Darsow T, Rieder SE, Emr SD. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. J Cell Biol 1997; 138:517-29. (Pubitemid 27349835)
    • (1997) Journal of Cell Biology , vol.138 , Issue.3 , pp. 517-529
    • Darsow, T.1    Rieder, S.E.2    Emr, S.D.3
  • 70
    • 43949112966 scopus 로고    scopus 로고
    • LAMP-2: A control step fot phagosome and autophagosome maturation
    • Saftig P, Beertsen W, Eskelinen EL. LAMP-2: a control step for phagosome and autophagosome maturation. Autophagy 2008; 4:510-2. (Pubitemid 351705148)
    • (2008) Autophagy , vol.4 , Issue.4 , pp. 510-512
    • Saftig, P.1    Beertsen, W.2    Eskelinen, E.-L.3
  • 71
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R, et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006; 441:885-9.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 72
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006; 441:880-4.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 73
    • 77449094358 scopus 로고    scopus 로고
    • Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration
    • Liang CC, Wang C, Peng X, Gan B, Guan JL. Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration. J Biol Chem 2010; 285:3499-509.
    • (2010) J Biol Chem , vol.285 , pp. 3499-3509
    • Liang, C.C.1    Wang, C.2    Peng, X.3    Gan, B.4    Guan, J.L.5
  • 74
    • 77649219699 scopus 로고    scopus 로고
    • Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice
    • Zheng S, Clabough EB, Sarkar S, Futter M, Rubinsztein DC, Zeitlin SO. Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice. PLoS Genet 2010; 6:1000838.
    • (2010) PLoS Genet , vol.6 , pp. 1000838
    • Zheng, S.1    Clabough, E.B.2    Sarkar, S.3    Futter, M.4    Rubinsztein, D.C.5    Zeitlin, S.O.6
  • 75
    • 77951665859 scopus 로고    scopus 로고
    • Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease
    • Martinez-Vicente M, Talloczy Z, Wong E, Tang G, Koga H, Kaushik S, et al. Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease. Nat Neurosci 2010; 13:567-76.
    • (2010) Nat Neurosci , vol.13 , pp. 567-576
    • Martinez-Vicente, M.1    Talloczy, Z.2    Wong, E.3    Tang, G.4    Koga, H.5    Kaushik, S.6
  • 76
    • 34548082024 scopus 로고    scopus 로고
    • A cycling protein complex required for selective autophagy
    • Legakis JE, Yen WL, Klionsky DJ. A cycling protein complex required for selective autophagy. Autophagy 2007; 3:422-32.
    • (2007) Autophagy , vol.3 , pp. 422-432
    • Legakis, J.E.1    Yen, W.L.2    Klionsky, D.J.3
  • 77
    • 49149112606 scopus 로고    scopus 로고
    • Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons
    • Colin E, Zala D, Liot G, Rangone H, Borrell-Pages M, Li XJ, et al. Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons. EMBO J 2008; 27:2124-34.
    • (2008) EMBO J , vol.27 , pp. 2124-2134
    • Colin, E.1    Zala, D.2    Liot, G.3    Rangone, H.4    Borrell-Pages, M.5    Li, X.J.6
  • 78
    • 57049184027 scopus 로고    scopus 로고
    • Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons
    • DOI 10.1093/hmg/ddn281
    • Zala D, Colin E, Rangone H, Liot G, Humbert S, Saudou F. Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons. Hum Mol Genet 2008; 17:3837-46. (Pubitemid 352762847)
    • (2008) Human Molecular Genetics , vol.17 , Issue.24 , pp. 3837-3846
    • Zala, D.1    Colin, E.2    Rangone, H.3    Liot, G.4    Humbert, S.5    Saudou, F.6
  • 79
    • 0032498794 scopus 로고    scopus 로고
    • Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole
    • Wang YX, Catlett NL, Weisman LS. Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. J Cell Biol 1998; 140:1063-74.
    • (1998) J Cell Biol , vol.140 , pp. 1063-1074
    • Wang, Y.X.1    Catlett, N.L.2    Weisman, L.S.3
  • 80
    • 33748433784 scopus 로고    scopus 로고
    • Early and late molecular events of glucose-induced pexophagy in Pichia pastoris require Vac8
    • Fry MR, Thomson JM, Tomasini AJ, Dunn WA Jr. Early and late molecular events of glucose-induced pexophagy in Pichia pastoris require Vac8. Autophagy 2006; 2:280-8.
    • (2006) Autophagy , vol.2 , pp. 280-288
    • Fry, M.R.1    Thomson, J.M.2    Tomasini, A.J.3    Dunn Jr., W.A.4
  • 81
    • 33748527156 scopus 로고    scopus 로고
    • Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with multiple vacuolar processes
    • DOI 10.1111/j.1600-0854.2006.00458.x
    • Tang F, Peng Y, Nau JJ, Kauffman EJ, Weisman LS. Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with multiple vacuolar processes. Traffic 2006; 7:1368-77. (Pubitemid 44364174)
    • (2006) Traffic , vol.7 , Issue.10 , pp. 1368-1377
    • Tang, F.1    Peng, Y.2    Nau, J.J.3    Kauffman, E.J.4    Weisman, L.S.5
  • 84
    • 33745627659 scopus 로고    scopus 로고
    • Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function
    • Yanai A, Huang K, Kang R, Singaraja RR, Arstikaitis P, Gan L, et al. Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function. Nat Neurosci 2006; 9:824-31.
    • (2006) Nat Neurosci , vol.9 , pp. 824-831
    • Yanai, A.1    Huang, K.2    Kang, R.3    Singaraja, R.R.4    Arstikaitis, P.5    Gan, L.6
  • 85
    • 77949412662 scopus 로고    scopus 로고
    • F-actin binding regions on the androgen receptor and huntingtin increase aggregation and alter aggregate characteristics
    • Angeli S, Shao J, Diamond MI. F-actin binding regions on the androgen receptor and huntingtin increase aggregation and alter aggregate characteristics. PLoS One 2010; 5:9053.
    • (2010) PLoS One , vol.5 , pp. 9053
    • Angeli, S.1    Shao, J.2    Diamond, M.I.3
  • 87
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin Has a Membrane Association Signal that Can Modulate Huntingtin Aggregation, Nuclear Entry and Toxicity
    • Atwal RS, Xia J, Pinchev D, Taylor J, Epand RM, Truant R. Huntingtin Has a Membrane Association Signal that Can Modulate Huntingtin Aggregation, Nuclear Entry and Toxicity. Hum Mol Genet 2007; 16:2600-15.
    • (2007) Hum Mol Genet , vol.16 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Pinchev, D.3    Taylor, J.4    Epand, R.M.5    Truant, R.6
  • 88
    • 53549131963 scopus 로고    scopus 로고
    • A life-span extending form of autophagy employs the vacuole-vacuole fusion machinery
    • Tang F, Watkins JW, Bermudez M, Gray R, Gaban A, Portie K, et al. A life-span extending form of autophagy employs the vacuole-vacuole fusion machinery. Autophagy 2008; 4:874-86.
    • (2008) Autophagy , vol.4 , pp. 874-886
    • Tang, F.1    Watkins, J.W.2    Bermudez, M.3    Gray, R.4    Gaban, A.5    Portie, K.6
  • 89
    • 32644434386 scopus 로고    scopus 로고
    • Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington's disease
    • DOI 10.1083/jcb.200509091
    • Pal A, Severin F, Lommer B, Shevchenko A, Zerial M. Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is upregulated in Huntington's disease. J Cell Biol 2006; 172:605-18. (Pubitemid 43243880)
    • (2006) Journal of Cell Biology , vol.172 , Issue.4 , pp. 605-618
    • Pal, A.1    Severin, F.2    Lommer, B.3    Shevchenko, A.4    Zerial, M.5
  • 91
    • 57249083972 scopus 로고    scopus 로고
    • Structural basis of target recognition by Atg8/LC3 during selective autophagy
    • Noda NN, Kumeta H, Nakatogawa H, Satoo K, Adachi W, Ishii J, et al. Structural basis of target recognition by Atg8/LC3 during selective autophagy. Genes Cells 2008; 13:1211-8.
    • (2008) Genes Cells , vol.13 , pp. 1211-1218
    • Noda, N.N.1    Kumeta, H.2    Nakatogawa, H.3    Satoo, K.4    Adachi, W.5    Ishii, J.6
  • 92
    • 38049053467 scopus 로고    scopus 로고
    • A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy
    • Atwal RS, Truant R. A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy. Autophagy 2008; 4:91-3.
    • (2008) Autophagy , vol.4 , pp. 91-93
    • Atwal, R.S.1    Truant, R.2
  • 93
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • DOI 10.1083/jcb.200507002
    • Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A, et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005; 171:603-14. (Pubitemid 41668720)
    • (2005) Journal of Cell Biology , vol.171 , Issue.4 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 95
    • 0442325388 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis
    • DOI 10.1016/S1534-5807(03)00403-9, PII S1534580703004039
    • Duran A, Serrano M, Leitges M, Flores JM, Picard S, Brown JP, et al. The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis. Dev Cell 2004; 6:303-9. (Pubitemid 38190368)
    • (2004) Developmental Cell , vol.6 , Issue.2 , pp. 303-309
    • Duran, A.1    Serrano, M.2    Leitges, M.3    Flores, J.M.4    Picard, S.5    Brown, J.P.6    Moscat, J.7    Diaz-Meco, M.T.8
  • 97
    • 70349334586 scopus 로고    scopus 로고
    • Peroxisome size provides insights into the function of autophagy-related proteins
    • Nazarko TY, Farre JC, Subramani S. Peroxisome size provides insights into the function of autophagy-related proteins. Mol Biol Cell 2009; 20:3828-39.
    • (2009) Mol Biol Cell , vol.20 , pp. 3828-3839
    • Nazarko, T.Y.1    Farre, J.C.2    Subramani, S.3
  • 98
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice JF. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 1990; 15:305-9.
    • (1990) Trends Biochem Sci , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 99
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin- Like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • Sampson DA, Wang M, Matunis MJ. The small ubiquitin- like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J Biol Chem 2001; 276:21664-9.
    • (2001) J Biol Chem , vol.276 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 100
    • 58149215720 scopus 로고    scopus 로고
    • Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy
    • Yang Q, She H, Gearing M, Colla E, Lee M, Shacka JJ, et al. Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy. Science 2009; 323:124-7.
    • (2009) Science , vol.323 , pp. 124-127
    • Yang, Q.1    She, H.2    Gearing, M.3    Colla, E.4    Lee, M.5    Shacka, J.J.6
  • 101
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • DOI 10.1042/BJ20030282
    • Fuertes G, Martin De Llano JJ, Villarroya A, Rivett AJ, Knecht E. Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem J 2003; 375:75-86. (Pubitemid 37255383)
    • (2003) Biochemical Journal , vol.375 , Issue.1 , pp. 75-86
    • Fuertes, G.1    Martin De Llano, J.J.2    Villarroya, A.3    Rivett, A.J.4    Knecht, E.5
  • 102
    • 77950495123 scopus 로고    scopus 로고
    • Physiological significance of selective degradation of p62 by autophagy
    • Komatsu M, Ichimura Y. Physiological significance of selective degradation of p62 by autophagy. FEBS Lett 2010; 584:1374-8.
    • (2010) FEBS Lett , vol.584 , pp. 1374-1378
    • Komatsu, M.1    Ichimura, Y.2
  • 103
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • DOI 10.1128/MCB.24.18.8055-8068.2004
    • Seibenhener ML, Babu JR, Geetha T, Wong HC, Krishna NR, Wooten MW. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol 2004; 24:8055-68. (Pubitemid 39167456)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.18 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3    Wong, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 104
    • 77951248828 scopus 로고    scopus 로고
    • Autophagy: Links with the proteasome
    • Lamark T, Johansen T. Autophagy: links with the proteasome. Curr Opin Cell Biol 2010; 22:192-8.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 192-198
    • Lamark, T.1    Johansen, T.2
  • 109
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transcriptional activator Sp1
    • DOI 10.1128/MCB.22.5.1277-1287.2002
    • Li SH, Cheng AL, Zhou H, Lam S, Rao M, Li H, et al. Interaction of Huntington disease protein with transcriptional activator Sp1. Mol Cell Biol 2002; 22:1277-87. (Pubitemid 34150765)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.5 , pp. 1277-1287
    • Li, S.-H.1    Cheng, A.L.2    Zhou, H.3    Lam, S.4    Rao, M.5    Li, H.6    Li, X.-J.7
  • 110
    • 0742287915 scopus 로고    scopus 로고
    • CRE-Mediated Transcription Is Increased in Huntington's Disease Transgenic Mice
    • DOI 10.1523/JNEUROSCI.3493-03.2004
    • Obrietan K, Hoyt KR. CRE-mediated transcription is increased in Huntington's disease transgenic mice. J Neurosci 2004; 24:791-6. (Pubitemid 38146589)
    • (2004) Journal of Neuroscience , vol.24 , Issue.4 , pp. 791-796
    • Obrietan, K.1    Hoyt, K.R.2
  • 111
    • 33745200299 scopus 로고    scopus 로고
    • Sp1 is upregulated in cellular and transgenic models of Huntington disease, and its reduction is neuroprotective
    • Qiu Z, Norflus F, Singh B, Swindell MK, Buzescu R, Bejarano M, et al. Sp1 is upregulated in cellular and transgenic models of Huntington disease, and its reduction is neuroprotective. J Biol Chem 2006; 281:16672-80.
    • (2006) J Biol Chem , vol.281 , pp. 16672-16680
    • Qiu, Z.1    Norflus, F.2    Singh, B.3    Swindell, M.K.4    Buzescu, R.5    Bejarano, M.6
  • 112
    • 0033818112 scopus 로고    scopus 로고
    • Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription
    • Shimohata T, Nakajima T, Yamada M, Uchida C, Onodera O, Naruse S, et al. Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription. Nat Genet 2000; 26:29-36.
    • (2000) Nat Genet , vol.26 , pp. 29-36
    • Shimohata, T.1    Nakajima, T.2    Yamada, M.3    Uchida, C.4    Onodera, O.5    Naruse, S.6
  • 113
    • 1042289730 scopus 로고    scopus 로고
    • Decreased cAMP response element-mediated transcription. An early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis
    • DOI 10.1074/jbc.M310226200
    • Sugars KL, Brown R, Cook LJ, Swartz J, Rubinsztein DC. Decreased cAMP response element-mediated transcription: an early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis. J Biol Chem 2004; 279:4988-99. (Pubitemid 38199095)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4988-4999
    • Sugars, K.L.1    Brown, R.2    Cook, L.J.3    Swartz, J.4    Rubinsztein, D.C.5
  • 117
    • 77950903972 scopus 로고    scopus 로고
    • The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy
    • Filimonenko M, Isakson P, Finley KD, Anderson M, Jeong H, Melia TJ, et al. The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy. Mol Cell 2010; 38:265-79.
    • (2010) Mol Cell , vol.38 , pp. 265-279
    • Filimonenko, M.1    Isakson, P.2    Finley, K.D.3    Anderson, M.4    Jeong, H.5    Melia, T.J.6
  • 118
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NFkappaB
    • Hayden MS, Ghosh S. Signaling to NFkappaB. Genes Dev 2004; 18:2195-224.
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 119
    • 33750523632 scopus 로고    scopus 로고
    • NF-kappaB activation by reactive oxygen species: Fifteen years later
    • DOI 10.1016/j.bcp.2006.04.011, PII S0006295206002255, Cell Signalling, Transcription and Translation as Therapeutic Tergets
    • Gloire G, Legrand-Poels S, Piette J. NFkappaB activation by reactive oxygen species: fifteen years later. Biochem Pharmacol 2006; 72:1493-505. (Pubitemid 44666727)
    • (2006) Biochemical Pharmacology , vol.72 , Issue.11 , pp. 1493-1505
    • Gloire, G.1    Legrand-Poels, S.2    Piette, J.3
  • 120
    • 33644538632 scopus 로고    scopus 로고
    • Molecular linkage between the kinase ATM and NFkappaB signaling in response to genotoxic stimuli
    • Wu ZH, Shi Y, Tibbetts RS, Miyamoto S. Molecular linkage between the kinase ATM and NFkappaB signaling in response to genotoxic stimuli. Science 2006; 311:1141-6.
    • (2006) Science , vol.311 , pp. 1141-1146
    • Wu, Z.H.1    Shi, Y.2    Tibbetts, R.S.3    Miyamoto, S.4
  • 121
    • 0042817922 scopus 로고    scopus 로고
    • Cyclin-dependent kinase-5 is involved in neuregulin-dependent activation of phosphatidylinositol 3-kinase and Akt activity mediating neuronal survival
    • DOI 10.1074/jbc.M302004200
    • Li BS, Ma W, Jaffe H, Zheng Y, Takahashi S, Zhang L, et al. Cyclin-dependent kinase-5 is involved in neuregulin-dependent activation of phosphatidylinositol 3-kinase and Akt activity mediating neuronal survival. J Biol Chem 2003; 278:35702-9. (Pubitemid 37102345)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 35702-35709
    • Li, B.-S.1    Ma, W.2    Jaffe, H.3    Zheng, Y.4    Takahashi, S.5    Zhang, L.6    Kulkarni, A.B.7    Pant, H.C.8
  • 123
    • 0037846441 scopus 로고    scopus 로고
    • Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice
    • DOI 10.1016/S0896-6273(03)00258-7
    • Emamian ES, Kaytor MD, Duvick LA, Zu T, Tousey SK, Zoghbi HY, et al. Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice. Neuron 2003; 38:375-87. (Pubitemid 36579141)
    • (2003) Neuron , vol.38 , Issue.3 , pp. 375-387
    • Emamian, E.S.1    Kaytor, M.D.2    Duvick, L.A.3    Zu, T.4    Tousey, S.K.5    Zoghbi, H.Y.6    Clark, H.B.7    Orr, H.T.8
  • 125
    • 71449108913 scopus 로고    scopus 로고
    • Reduced IGF-1 signaling delays age-associated proteotoxicity in mice
    • Cohen E, Paulsson JF, Blinder P, Burstyn-Cohen T, Du D, Estepa G, et al. Reduced IGF-1 signaling delays age-associated proteotoxicity in mice. Cell 2009; 139:1157-69.
    • (2009) Cell , vol.139 , pp. 1157-1169
    • Cohen, E.1    Paulsson, J.F.2    Blinder, P.3    Burstyn-Cohen, T.4    Du, D.5    Estepa, G.6
  • 126
    • 70349672704 scopus 로고    scopus 로고
    • Neuronal IGF-1 resistance reduces Abeta accumulation and protects against premature death in a model of Alzheimer's disease
    • Freude S, Hettich MM, Schumann C, Stohr O, Koch L, Kohler C, et al. Neuronal IGF-1 resistance reduces Abeta accumulation and protects against premature death in a model of Alzheimer's disease. Faseb J 2009; 23:3315-24.
    • (2009) Faseb J , vol.23 , pp. 3315-3324
    • Freude, S.1    Hettich, M.M.2    Schumann, C.3    Stohr, O.4    Koch, L.5    Kohler, C.6
  • 127
    • 67649224051 scopus 로고    scopus 로고
    • Deletion of Irs2 reduces amyloid deposition and rescues behavioural deficits in APP transgenic mice
    • Killick R, Scales G, Leroy K, Causevic M, Hooper C, Irvine EE, et al. Deletion of Irs2 reduces amyloid deposition and rescues behavioural deficits in APP transgenic mice. Biochem Biophys Res Commun 2009; 386:257-62.
    • (2009) Biochem Biophys Res Commun , vol.386 , pp. 257-262
    • Killick, R.1    Scales, G.2    Leroy, K.3    Causevic, M.4    Hooper, C.5    Irvine, E.E.6
  • 128
    • 68149180778 scopus 로고    scopus 로고
    • Overexpression of IGF-1 in muscle attenuates disease in a mouse model of spinal and bulbar muscular atrophy
    • Palazzolo I, Stack C, Kong L, Musaro A, Adachi H, Katsuno M, et al. Overexpression of IGF-1 in muscle attenuates disease in a mouse model of spinal and bulbar muscular atrophy. Neuron 2009; 63:316-28.
    • (2009) Neuron , vol.63 , pp. 316-328
    • Palazzolo, I.1    Stack, C.2    Kong, L.3    Musaro, A.4    Adachi, H.5    Katsuno, M.6
  • 131
    • 33646010041 scopus 로고    scopus 로고
    • Roles for NFkappaB in nerve cell survival, plasticity and disease
    • Mattson MP, Meffert MK. Roles for NFkappaB in nerve cell survival, plasticity and disease. Cell Death Differ 2006; 13:852-60.
    • (2006) Cell Death Differ , vol.13 , pp. 852-860
    • Mattson, M.P.1    Meffert, M.K.2
  • 132
  • 135
    • 0041733096 scopus 로고    scopus 로고
    • Improved reversal learning and altered fear conditioning in transgenic mice with regionally restricted p25 expression
    • DOI 10.1046/j.1460-9568.2003.02746.x
    • Angelo M, Plattner F, Irvine EE, Giese KP. Improved reversal learning and altered fear conditioning in transgenic mice with regionally restricted p25 expression. Eur J Neurosci 2003; 18:423-31. (Pubitemid 36999943)
    • (2003) European Journal of Neuroscience , vol.18 , Issue.2 , pp. 423-431
    • Angelo, M.1    Plattner, F.2    Irvine, E.E.3    Giese, K.P.4
  • 136
    • 28744449248 scopus 로고    scopus 로고
    • Opposing roles of transient and prolonged expression of p25 in synaptic plasticity and hippocampus-dependent memory
    • DOI 10.1016/j.neuron.2005.10.033, PII S0896627305009517
    • Fischer A, Sananbenesi F, Pang PT, Lu B, Tsai LH. Opposing roles of transient and prolonged expression of p25 in synaptic plasticity and hippocampusdependent memory. Neuron 2005; 48:825-38. (Pubitemid 41759432)
    • (2005) Neuron , vol.48 , Issue.5 , pp. 825-838
    • Fischer, A.1    Sananbenesi, F.2    Pang, P.T.3    Lu, B.4    Tsai, L.-H.5
  • 137
    • 58149267462 scopus 로고    scopus 로고
    • Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau
    • Green KN, Steffan JS, Martinez-Coria H, Sun X, Schreiber SS, Thompson LM, et al. Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau. J Neurosci 2008; 28:11500-10.
    • (2008) J Neurosci , vol.28 , pp. 11500-11510
    • Green, K.N.1    Steffan, J.S.2    Martinez-Coria, H.3    Sun, X.4    Schreiber, S.S.5    Thompson, L.M.6
  • 138
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q, Zhang Y, Yang C, Xiong H, Lin Y, Yao J, et al. Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 2010; 327:1004-7.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5    Yao, J.6
  • 139
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, et al. Regulation of cellular metabolism by protein lysine acetylation. Science 2010; 327:1000-4.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3    Yu, W.4    Lin, Y.5    Zhang, T.6
  • 142
    • 74549133523 scopus 로고    scopus 로고
    • Chaperone-assisted selective autophagy is essential for muscle maintenance
    • Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D, Hesse M, et al. Chaperone-assisted selective autophagy is essential for muscle maintenance. Curr Biol 2010; 20:143-8.
    • (2010) Curr Biol , vol.20 , pp. 143-148
    • Arndt, V.1    Dick, N.2    Tawo, R.3    Dreiseidler, M.4    Wenzel, D.5    Hesse, M.6
  • 143
    • 77649337122 scopus 로고    scopus 로고
    • HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy
    • Lee JY, Koga H, Kawaguchi Y, Tang W, Wong E, Gao YS, et al. HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy. EMBO J 2010; 29:969-80.
    • (2010) EMBO J , vol.29 , pp. 969-980
    • Lee, J.Y.1    Koga, H.2    Kawaguchi, Y.3    Tang, W.4    Wong, E.5    Gao, Y.S.6
  • 145
    • 33847191686 scopus 로고    scopus 로고
    • Parkin mediates neuroprotection through activation of IkappaB kinase/ nuclear factor-kappaB signaling
    • Henn IH, Bouman L, Schlehe JS, Schlierf A, Schramm JE, Wegener E, et al. Parkin mediates neuroprotection through activation of IkappaB kinase/ nuclear factor-kappaB signaling. J Neurosci 2007; 27:1868-78.
    • (2007) J Neurosci , vol.27 , pp. 1868-1878
    • Henn, I.H.1    Bouman, L.2    Schlehe, J.S.3    Schlierf, A.4    Schramm, J.E.5    Wegener, E.6
  • 146
    • 77949478474 scopus 로고    scopus 로고
    • Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NFkappaB signaling
    • Sha D, Chin LS, Li L. Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NFkappaB signaling. Hum Mol Genet 2010; 19:352-63.
    • (2010) Hum Mol Genet , vol.19 , pp. 352-363
    • Sha, D.1    Chin, L.S.2    Li, L.3
  • 148
    • 76249124608 scopus 로고    scopus 로고
    • Resveratrol promotes autophagic cell death in chronic myelogenous leukemia cells via JNK-mediated p62/SQSTM1 expression and AMPK activation
    • Puissant A, Robert G, Fenouille N, Luciano F, Cassuto JP, Raynaud S, et al. Resveratrol promotes autophagic cell death in chronic myelogenous leukemia cells via JNK-mediated p62/SQSTM1 expression and AMPK activation. Cancer Res 2010; 70:1042-52.
    • (2010) Cancer Res , vol.70 , pp. 1042-1052
    • Puissant, A.1    Robert, G.2    Fenouille, N.3    Luciano, F.4    Cassuto, J.P.5    Raynaud, S.6
  • 149
    • 0942298113 scopus 로고    scopus 로고
    • Nuclear Role of IkappaB Kinase-gamma/NF-kappaB Essential Modulator (IKKgamma/NEMO) in NF-kappaB-dependent Gene Expression
    • DOI 10.1074/jbc.M309300200
    • Verma UN, Yamamoto Y, Prajapati S, Gaynor RB. Nuclear role of IkappaB Kinase-gamma/NFkappa B essential modulator (IKKgamma/NEMO) in NFkappaB-dependent gene expression. J Biol Chem 2004; 279:3509-15. (Pubitemid 38140590)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3509-3515
    • Verma, U.N.1    Yamamoto, Y.2    Prajapati, S.3    Gaynor, R.B.4
  • 150
    • 77955789211 scopus 로고    scopus 로고
    • Altered lipid content inhibits autophagic vesicular fusion
    • Koga H, Kaushik S, Cuervo AM. Altered lipid content inhibits autophagic vesicular fusion. Faseb J 2010.
    • (2010) Faseb J
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 151
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo AM, Dice JF. Age-related decline in chaperone-mediated autophagy. J Biol Chem 2000; 275:31505-13.
    • (2000) J Biol Chem , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 152
    • 33746278194 scopus 로고    scopus 로고
    • Chapter 7: The selfish brain: competition for energy resources
    • DOI 10.1016/S0079-6123(06)53007-9, PII S0079612306530079, Hypothalmic Integration of Energy Metabolism
    • Fehm HL, Kern W, Peters A. The selfish brain: competition for energy resources. Prog Brain Res 2006; 153:129-40. (Pubitemid 44107413)
    • (2006) Progress in Brain Research , vol.153 , pp. 129-140
    • Fehm, H.L.1    Kern, W.2    Peters, A.3
  • 153
    • 70350418625 scopus 로고    scopus 로고
    • mTOR signaling at a glance
    • Laplante M, Sabatini DM. mTOR signaling at a glance. J Cell Sci 2009; 122:3589-94.
    • (2009) J Cell Sci , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 154
    • 38549084725 scopus 로고    scopus 로고
    • A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation
    • DOI 10.1038/sj.emboj.7601962, PII 7601962
    • Hasegawa M, Fujimoto Y, Lucas PC, Nakano H, Fukase K, Nunez G, et al. A critical role of RICK/ RIP2 polyubiquitination in Nod-induced NFkappaB activation. EMBO J 2008; 27:373-83. (Pubitemid 351161652)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 373-383
    • Hasegawa, M.1    Fujimoto, Y.2    Lucas, P.C.3    Nakano, H.4    Fukase, K.5    Nunez, G.6    Inohara, N.7
  • 155
    • 44449161481 scopus 로고    scopus 로고
    • The TSC1-TSC2 complex: A molecular switchboard controlling cell growth
    • DOI 10.1042/BJ20080281
    • Huang J, Manning BD. The TSC1-TSC2 complex: a molecular switchboard controlling cell growth. Biochem J 2008; 412:179-90. (Pubitemid 351758225)
    • (2008) Biochemical Journal , vol.412 , Issue.2 , pp. 179-190
    • Huang, J.1    Manning, B.D.2
  • 157
    • 58149473435 scopus 로고    scopus 로고
    • Role of ULK-FIP200 complex in mammalian autophagy: FIP200, a counterpart of yeast Atg17?
    • Hara T, Mizushima N. Role of ULK-FIP200 complex in mammalian autophagy: FIP200, a counterpart of yeast Atg17? Autophagy 2009; 5:85-7.
    • (2009) Autophagy , vol.5 , pp. 85-87
    • Hara, T.1    Mizushima, N.2
  • 159
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • DOI 10.1038/ncb1007-1102, PII NCB1007-1102
    • Xie Z, Klionsky DJ. Autophagosome formation: core machinery and adaptations. Nat Cell Biol 2007; 9:1102-9. (Pubitemid 47500484)
    • (2007) Nature Cell Biology , vol.9 , Issue.10 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 160
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • DOI 10.1016/S0968-0004(03)00168-3
    • Harjes P, Wanker EE. The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem Sci 2003; 28:425-33. (Pubitemid 36976745)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.8 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 161
    • 0032540437 scopus 로고    scopus 로고
    • HAP1-huntingtin interactions do not contribute to the molecular pathology in Huntington's disease transgenic mice
    • DOI 10.1016/S0014-5793(98)00352-4, PII S0014579398003524
    • Bertaux F, Sharp AH, Ross CA, Lehrach H, Bates GP, Wanker E. HAP1-huntingtin interactions do not contribute to the molecular pathology in Huntington's disease transgenic mice. FEBS Lett 1998; 426:229-32. (Pubitemid 28198132)
    • (1998) FEBS Letters , vol.426 , Issue.2 , pp. 229-232
    • Bertaux, F.1    Sharp, A.H.2    Ross, C.A.3    Lehrach, H.4    Bates, G.P.5    Wanker, E.6
  • 162
    • 53049101345 scopus 로고    scopus 로고
    • Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy
    • Kabuta T, Furuta A, Aoki S, Furuta K, Wada K. Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy. J Biol Chem 2008; 283:23731-8.
    • (2008) J Biol Chem , vol.283 , pp. 23731-23738
    • Kabuta, T.1    Furuta, A.2    Aoki, S.3    Furuta, K.4    Wada, K.5


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