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Volumn 290, Issue 3, 2015, Pages 1442-1453

p62 plays a protective role in the autophagic degradation of polyglutamine protein oligomers in polyglutamine disease model flies

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; BIODEGRADATION; OLIGOMERS; PROTEINS;

EID: 84961290118     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.590281     Document Type: Article
Times cited : (49)

References (45)
  • 1
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: Mechanisms and common principles
    • Gatchel, J. R., and Zoghbi, H. Y. (2005) Diseases of unstable repeat expansion: mechanisms and common principles. Nat. Rev. Genet. 6, 743-755
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 4
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., and Finkbeiner, S. (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 6
    • 38349158062 scopus 로고    scopus 로고
    • Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic
    • Takahashi, T., Kikuchi, S., Katada, S., Nagai, Y., Nishizawa, M., and Onodera, O. (2008) Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic. Hum. Mol. Genet. 17, 345-356
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 345-356
    • Takahashi, T.1    Kikuchi, S.2    Katada, S.3    Nagai, Y.4    Nishizawa, M.5    Onodera, O.6
  • 7
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D. C. (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443, 780-786
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 8
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef, L. G., Lindsten, K., Masucci, M. G., and Dantuma, N. P. (2002) Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 11, 2689-2700
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 9
    • 9144223729 scopus 로고    scopus 로고
    • Inefficient degradation of truncated polyglutamine proteins by the proteasome
    • Holmberg, C. I., Staniszewski, K. E., Mensah, K. N., Matouschek, A., and Morimoto, R. I. (2004) Inefficient degradation of truncated polyglutamine proteins by the proteasome. EMBO J. 23, 4307-4318
    • (2004) EMBO J , vol.23 , pp. 4307-4318
    • Holmberg, C.I.1    Staniszewski, K.E.2    Mensah, K.N.3    Matouschek, A.4    Morimoto, R.I.5
  • 10
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman, P., Wetzel, R., Tanaka, M., Nukina, N., and Goldberg, A. L. (2004) Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol. Cell 14, 95-104
    • (2004) Mol. Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 11
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar, B., Duden, R., and Rubinsztein, D. C. (2002) Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 11, 1107-1117
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 12
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen, T., and Lamark, T. (2011) Selective autophagy mediated by autophagic adapter proteins. Autophagy 7, 279-296
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 15
    • 0035919837 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies
    • Kuusisto, E., Salminen, A., and Alafuzoff, I. (2001) Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. Neuroreport 12, 2085-2090
    • (2001) Neuroreport , vol.12 , pp. 2085-2090
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 17
    • 0033581953 scopus 로고    scopus 로고
    • Ectopic expression of human p53 inhibits entry into S phase and induces apoptosis in the Drosophila eye imaginal disc
    • Yamaguchi, M., Hirose, F., Inoue, Y. H., Shiraki, M., Hayashi, Y., Nishi, Y., and Matsukage, A. (1999) Ectopic expression of human p53 inhibits entry into S phase and induces apoptosis in the Drosophila eye imaginal disc. Oncogene 18, 6767-6775
    • (1999) Oncogene , vol.18 , pp. 6767-6775
    • Yamaguchi, M.1    Hirose, F.2    Inoue, Y.H.3    Shiraki, M.4    Hayashi, Y.5    Nishi, Y.6    Matsukage, A.7
  • 18
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • Warrick, J. M., Paulson, H. L., Gray-Board, G. L., Bui, Q. T., Fischbeck, K. H., Pittman, R. N., and Bonini, N. M. (1998) Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Cell 93, 939-949
    • (1998) Cell , vol.93 , pp. 939-949
    • Warrick, J.M.1    Paulson, H.L.2    Gray-Board, G.L.3    Bui, Q.T.4    Fischbeck, K.H.5    Pittman, R.N.6    Bonini, N.M.7
  • 20
    • 15044339964 scopus 로고    scopus 로고
    • Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease
    • Crowther, D. C., Kinghorn, K. J., Miranda, E., Page, R., Curry, J. A., Duthie, F. A., Gubb, D. C., and Lomas, D. A. (2005) Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease. Neuroscience 132, 123-135
    • (2005) Neuroscience , vol.132 , pp. 123-135
    • Crowther, D.C.1    Kinghorn, K.J.2    Miranda, E.3    Page, R.4    Curry, J.A.5    Duthie, F.A.6    Gubb, D.C.7    Lomas, D.A.8
  • 22
    • 0029014415 scopus 로고
    • Localization of domains within the Drosophila Ref(2)P protein involved in the intracellular control of σ rhabdovirus multiplication
    • Wyers, F., Petitjean, A. M., Dru, P., Gay, P., and Contamine, D. (1995) Localization of domains within the Drosophila Ref(2)P protein involved in the intracellular control of σ rhabdovirus multiplication. J. Virol. 69, 4463-4470
    • (1995) J. Virol. , vol.69 , pp. 4463-4470
    • Wyers, F.1    Petitjean, A.M.2    Dru, P.3    Gay, P.4    Contamine, D.5
  • 23
    • 44449154449 scopus 로고    scopus 로고
    • Functional analysis of proteoglycan galactosyltransferase II RNA interference mutant flies
    • Ueyama, M., Takemae, H., Ohmae, Y., Yoshida, H., Toyoda, H., Ueda, R., and Nishihara, S. (2008) Functional analysis of proteoglycan galactosyltransferase II RNA interference mutant flies. J. Biol. Chem. 283, 6076-6084
    • (2008) J. Biol. Chem. , vol.283 , pp. 6076-6084
    • Ueyama, M.1    Takemae, H.2    Ohmae, Y.3    Yoshida, H.4    Toyoda, H.5    Ueda, R.6    Nishihara, S.7
  • 25
    • 38049139425 scopus 로고    scopus 로고
    • Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease
    • Weiss, A., Klein, C., Woodman, B., Sathasivam, K., Bibel, M., Régulier, E., Bates, G. P., and Paganetti, P. (2008) Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease. J. Neurochem. 104, 846-858
    • (2008) J. Neurochem. , vol.104 , pp. 846-858
    • Weiss, A.1    Klein, C.2    Woodman, B.3    Sathasivam, K.4    Bibel, M.5    Régulier, E.6    Bates, G.P.7    Paganetti, P.8
  • 26
    • 77951988103 scopus 로고    scopus 로고
    • Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo
    • Legleiter, J., Mitchell, E., Lotz, G. P., Sapp, E., Ng, C., DiFiglia, M., Thompson, L. M., and Muchowski, P. J. (2010) Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo. J. Biol. Chem. 285, 14777-14790
    • (2010) J. Biol. Chem. , vol.285 , pp. 14777-14790
    • Legleiter, J.1    Mitchell, E.2    Lotz, G.P.3    Sapp, E.4    Ng, C.5    DiFiglia, M.6    Thompson, L.M.7    Muchowski, P.J.8
  • 27
  • 28
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., Stenmark, H., and Johansen, T. (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603-614
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 30
    • 0036743869 scopus 로고    scopus 로고
    • Conditional expression of UAS-transgenes in the adult eye with a new gene-switch vector system
    • Roman, G., and Davis, R. L. (2002) Conditional expression of UAS-transgenes in the adult eye with a new gene-switch vector system. Genesis 34, 127-131
    • (2002) Genesis , vol.34 , pp. 127-131
    • Roman, G.1    Davis, R.L.2
  • 31
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk, V. I., Mansilla, A., Menzies, F. M., and Rubinsztein, D. C. (2009) Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol. Cell 33, 517-527
    • (2009) Mol. Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 32
    • 4744349602 scopus 로고    scopus 로고
    • Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions
    • Nagaoka, U., Kim, K., Jana, N. R., Doi, H., Maruyama, M., Mitsui, K., Oyama, F., and Nukina, N. (2004) Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions. J. Neurochem. 91, 57-68
    • (2004) J. Neurochem. , vol.91 , pp. 57-68
    • Nagaoka, U.1    Kim, K.2    Jana, N.R.3    Doi, H.4    Maruyama, M.5    Mitsui, K.6    Oyama, F.7    Nukina, N.8
  • 33
    • 82455172117 scopus 로고    scopus 로고
    • Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins
    • Matsumoto, G., Wada, K., Okuno, M., Kurosawa, M., and Nukina, N. (2011) Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. Mol. Cell 44, 279-289
    • (2011) Mol. Cell , vol.44 , pp. 279-289
    • Matsumoto, G.1    Wada, K.2    Okuno, M.3    Kurosawa, M.4    Nukina, N.5
  • 36
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 38
  • 39
    • 78650680776 scopus 로고    scopus 로고
    • Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1
    • Brady, O. A., Meng, P., Zheng, Y., Mao, Y., and Hu, F. (2011) Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1. J. Neurochem. 116, 248-259
    • (2011) J. Neurochem. , vol.116 , pp. 248-259
    • Brady, O.A.1    Meng, P.2    Zheng, Y.3    Mao, Y.4    Hu, F.5
  • 42
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated Tau and enhances cell survival
    • Shimura, H., Schwartz, D., Gygi, S. P., and Kosik, K. S. (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated Tau and enhances cell survival. J. Biol. Chem. 279, 4869-4876
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 43
    • 84878114130 scopus 로고    scopus 로고
    • Tau degradation: The ubiquitin-proteasome system versus the autophagy-lysosome system
    • Lee, M. J., Lee, J. H., and Rubinsztein, D. C. (2013) Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system. Prog. Neurobiol. 105, 49-59
    • (2013) Prog. Neurobiol. , vol.105 , pp. 49-59
    • Lee, M.J.1    Lee, J.H.2    Rubinsztein, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.