메뉴 건너뛰기




Volumn 7, Issue 1, 2011, Pages 51-60

Binding preference of p62 towards LC3-II during dopaminergic neurotoxin-induced impairment of autophagic flux

Author keywords

Autophagic flux; Autophagy; LC3 II; Neurodegeneration; p62 sequestosome 1; Parkinson disease

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; CELL PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 1 LIGHT CHAIN 3; NEUROTOXIN; PROTEIN; PROTEIN ATG4B; PROTEIN ATG4B C74A; PROTEIN P62; TRITON X 100; UBIQUITINATED PROTEIN; UNCLASSIFIED DRUG;

EID: 78650831133     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.7.1.13909     Document Type: Article
Times cited : (70)

References (47)
  • 1
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008; 132:27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 2
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • Cuervo AM. Autophagy: in sickness and in health. Trends Cell Biol 2004; 14:70-7.
    • (2004) Trends Cell Biol , vol.14 , pp. 70-77
    • Cuervo, A.M.1
  • 3
    • 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
  • 4
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C, Klionsky DJ. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 2009; 43:67-93.
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 5
    • 51049118332 scopus 로고    scopus 로고
    • The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. 'Protein modifications: Beyond the usual suspects' review series
    • Geng J, Klionsky DJ. The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. 'Protein modifications: beyond the usual suspects' review series. EMBO Rep 2008; 9:859-64.
    • (2008) EMBO Rep , vol.9 , pp. 859-864
    • Geng, J.1    Klionsky, D.J.2
  • 6
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19:5720-8.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6
  • 7
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv S, Clausen TH, Lamark T, Brech A, Bruun JA, Outzen H, et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282:24131-45.
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3    Brech, A.4    Bruun, J.A.5    Outzen, H.6
  • 8
    • 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
  • 9
    • 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
  • 10
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V, McEwan DG, Novak I, Dikic I. A role for ubiquitin in selective autophagy. Mol Cell 2009; 34:259-69.
    • (2009) Mol Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 12
    • 77950484269 scopus 로고    scopus 로고
    • Atg8-family interacting motif crucial for selective autophagy
    • Noda NN, Ohsumi Y, Inagaki F. Atg8-family interacting motif crucial for selective autophagy. FEBS Lett 2010; 584:1379-85.
    • (2010) FEBS Lett , vol.584 , pp. 1379-1385
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 13
    • 52649121942 scopus 로고    scopus 로고
    • The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes
    • Shvets E, Fass E, Scherz-Shouval R, Elazar Z. The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes. J Cell Sci 2008; 121:2685-95.
    • (2008) J Cell Sci , vol.121 , pp. 2685-2695
    • Shvets, E.1    Fass, E.2    Scherz-Shouval, R.3    Elazar, Z.4
  • 15
    • 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
  • 17
    • 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
  • 18
    • 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
  • 19
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451:1069-75.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 20
    • 38949096081 scopus 로고    scopus 로고
    • Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome
    • Ding WX, Yin XM. Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy 2008; 4:141-50.
    • (2008) Autophagy , vol.4 , pp. 141-150
    • Ding, W.X.1    Yin, X.M.2
  • 21
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006; 443:780-6.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 22
    • 68349161234 scopus 로고    scopus 로고
    • Autophagy in neurodegeneration: Two sides of the same coin
    • Lee JA. Autophagy in neurodegeneration: two sides of the same coin. BMB Rep 2009; 42:324-30.
    • (2009) BMB Rep , vol.42 , pp. 324-330
    • Lee, J.A.1
  • 23
    • 0033168508 scopus 로고    scopus 로고
    • Two distinct mechanisms are involved in 6-hydroxydopamine-and MPP+-induced dopaminergic neuronal cell death: Role of caspases, ROS and JNK
    • Choi WS, Yoon SY, Oh TH, Choi EJ, O'Malley KL, Oh YJ. Two distinct mechanisms are involved in 6-hydroxydopamine-and MPP+-induced dopaminergic neuronal cell death: role of caspases, ROS and JNK. J Neurosci Res 1999; 57:86-94.
    • (1999) J Neurosci Res , vol.57 , pp. 86-94
    • Choi, W.S.1    Yoon, S.Y.2    Oh, T.H.3    Choi, E.J.4    O'Malley, K.L.5    Oh, Y.J.6
  • 24
    • 0038790330 scopus 로고    scopus 로고
    • Caspase-dependent and -independent cell death pathways in primary cultures of mesencephalic dopaminergic neurons after neurotoxin treatment
    • Han BS, Hong HS, Choi WS, Markelonis GJ, Oh TH, Oh YJ. Caspase-dependent and -independent cell death pathways in primary cultures of mesencephalic dopaminergic neurons after neurotoxin treatment. J Neurosci 2003; 23:5069-78.
    • (2003) J Neurosci , vol.23 , pp. 5069-5078
    • Han, B.S.1    Hong, H.S.2    Choi, W.S.3    Markelonis, G.J.4    Oh, T.H.5    Oh, Y.J.6
  • 25
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • Komatsu M, Waguri S, Koike M, Sou YS, Ueno T, Hara T, et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 2007; 131:1149-63.
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1    Waguri, S.2    Koike, M.3    Sou, Y.S.4    Ueno, T.5    Hara, T.6
  • 26
    • 58149083873 scopus 로고    scopus 로고
    • Selective turnover of p62/A170/SQSTM1 by autophagy
    • Ichimura Y, Kominami E, Tanaka K, Komatsu M. Selective turnover of p62/A170/SQSTM1 by autophagy. Autophagy 2008; 4:1063-6.
    • (2008) Autophagy , vol.4 , pp. 1063-1066
    • Ichimura, Y.1    Kominami, E.2    Tanaka, K.3    Komatsu, M.4
  • 27
    • 77956314467 scopus 로고    scopus 로고
    • Parkinson Disease: A Role for Autophagy?
    • Yang Q, Mao Z. Parkinson Disease: A Role for Autophagy? Neuroscientist 2010.
    • (2010) Neuroscientist
    • Yang, Q.1    Mao, Z.2
  • 28
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death
    • DOI 10.2353/ajpath.2007.060524
    • Zhu JH, Horbinski C, Guo F, Watkins S, Uchiyama Y, Chu CT. Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death. Am J Pathol 2007; 170:75-86. (Pubitemid 47339191)
    • (2007) American Journal of Pathology , vol.170 , Issue.1 , pp. 75-86
    • Zhu, J.-H.1    Horbinski, C.2    Guo, F.3    Watkins, S.4    Uchiyama, Y.5    Chu, C.T.6
  • 31
    • 65449117176 scopus 로고    scopus 로고
    • Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
    • Gamerdinger M, Hajieva P, Kaya AM, Wolfrum U, Hartl FU, Behl C. Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3. EMBO J 2009; 28:889-901.
    • (2009) EMBO J , vol.28 , pp. 889-901
    • Gamerdinger, M.1    Hajieva, P.2    Kaya, A.M.3    Wolfrum, U.4    Hartl, F.U.5    Behl, C.6
  • 32
    • 58149290220 scopus 로고    scopus 로고
    • An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure
    • Fujita N, Hayashi-Nishino M, Fukumoto H, Omori H, Yamamoto A, Noda T, et al. An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure. Mol Biol Cell 2008; 19:4651-9.
    • (2008) Mol Biol Cell , vol.19 , pp. 4651-4659
    • Fujita, N.1    Hayashi-Nishino, M.2    Fukumoto, H.3    Omori, H.4    Yamamoto, A.5    Noda, T.6
  • 33
    • 29144517659 scopus 로고    scopus 로고
    • The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers
    • Kumanomidou T, Mizushima T, Komatsu M, Suzuki A, Tanida I, Sou YS, et al. The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers. J Mol Biol 2006; 355:612-8.
    • (2006) J Mol Biol , vol.355 , pp. 612-618
    • Kumanomidou, T.1    Mizushima, T.2    Komatsu, M.3    Suzuki, A.4    Tanida, I.5    Sou, Y.S.6
  • 34
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W, Przedborski S. Parkinson's disease: mechanisms and models. Neuron 2003; 39:889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 35
    • 26844505808 scopus 로고    scopus 로고
    • Toxin-induced models of Parkinson's disease
    • Bove J, Prou D, Perier C, Przedborski S. Toxin-induced models of Parkinson's disease. NeuroRx 2005; 2:484-94.
    • (2005) NeuroRx , vol.2 , pp. 484-494
    • Bove, J.1    Prou, D.2    Perier, C.3    Przedborski, S.4
  • 36
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease
    • Anglade P, Vyas S, Javoy-Agid F, Herrero MT, Michel PP, Marquez J, et al. Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol Histopathol 1997; 12:25-31. (Pubitemid 27106916)
    • (1997) Histology and Histopathology , vol.12 , Issue.1 , pp. 25-31
    • Anglade, P.1
  • 37
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • Vogiatzi T, Xilouri M, Vekrellis K, Stefanis L. Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J Biol Chem 2008; 283:23542-56.
    • (2008) J Biol Chem , vol.283 , pp. 23542-23556
    • Vogiatzi, T.1    Xilouri, M.2    Vekrellis, K.3    Stefanis, L.4
  • 38
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • DOI 10.1126/science.1101738
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004; 305:1292-5. (Pubitemid 39129234)
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stafanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 39
    • 70350630733 scopus 로고    scopus 로고
    • The emerging role of autophagy in Parkinson's disease
    • Cheung ZH, Ip NY. The emerging role of autophagy in Parkinson's disease. Mol Brain 2009; 2:29.
    • (2009) Mol Brain , vol.2 , pp. 29
    • Cheung, Z.H.1    Ip, N.Y.2
  • 41
    • 70350131893 scopus 로고    scopus 로고
    • Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism
    • Gal J, Strom AL, Kwinter DM, Kilty R, Zhang J, Shi P, et al. Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism. J Neurochem 2009; 111:1062-73.
    • (2009) J Neurochem , vol.111 , pp. 1062-1073
    • Gal, J.1    Strom, A.L.2    Kwinter, D.M.3    Kilty, R.4    Zhang, J.5    Shi, P.6
  • 42
    • 77956268597 scopus 로고    scopus 로고
    • The evolutionarily conserved interaction between LC3 and p62 selectively mediates autophagy-dependent degradation of mutant huntingtin
    • Tung YT, Hsu WM, Lee H, Huang WP, Liao YF. The evolutionarily conserved interaction between LC3 and p62 selectively mediates autophagy-dependent degradation of mutant huntingtin. Cell Mol Neurobiol 2010; 30:795-806.
    • (2010) Cell Mol Neurobiol , vol.30 , pp. 795-806
    • Tung, Y.T.1    Hsu, W.M.2    Lee, H.3    Huang, W.P.4    Liao, Y.F.5
  • 43
    • 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
  • 44
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita N, Itoh T, Omori H, Fukuda M, Noda T, Yoshimori T. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol Biol Cell 2008; 19:2092-100.
    • (2008) Mol Biol Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 45
    • 74049106190 scopus 로고    scopus 로고
    • Biochemical isolation and characterization of the tubulovesicular LC3-positive autophagosomal compartment
    • Gao W, Kang JH, Liao Y, Ding WX, Gambotto AA, Watkins SC, et al. Biochemical isolation and characterization of the tubulovesicular LC3-positive autophagosomal compartment. J Biol Chem 2010; 285:1371-83.
    • (2010) J Biol Chem , vol.285 , pp. 1371-1383
    • Gao, W.1    Kang, J.H.2    Liao, Y.3    Ding, W.X.4    Gambotto, A.A.5    Watkins, S.C.6
  • 46
    • 73649130269 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: Emerging role of molecular chaperones
    • Bandopadhyay R, de Belleroche J. Pathogenesis of Parkinson's disease: emerging role of molecular chaperones. Trends Mol Med 2010; 16:27-36.
    • (2010) Trends Mol Med , vol.16 , pp. 27-36
    • Bandopadhyay, R.1    De Belleroche, J.2
  • 47
    • 0033049149 scopus 로고    scopus 로고
    • Sequential cleavage of poly(ADP-ribose)polymerase and appearance of a small Bax-immunoreactive protein are blocked by Bcl-X(L) and caspase inhibitors during staurosporine-induced dopaminergic neuronal apoptosis
    • Kim JE, Oh JH, Choi WS, Chang II, Sohn S, Krajewski S, et al. Sequential cleavage of poly(ADP-ribose)polymerase and appearance of a small Bax-immunoreactive protein are blocked by Bcl-X(L) and caspase inhibitors during staurosporine-induced dopaminergic neuronal apoptosis. J Neurochem 1999; 72:2456-63.
    • (1999) J Neurochem , vol.72 , pp. 2456-2463
    • Kim, J.E.1    Oh, J.H.2    Choi, W.S.3    Chang, I.I.4    Sohn, S.5    Krajewski, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.