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Volumn 52, Issue , 2013, Pages 219-228

Brain region- and age-dependent dysregulation of p62 and NBR1 in a mouse model of Huntington's disease

Author keywords

Aggregates; Autophagy; Humans; R6 1 mouse

Indexed keywords

NEIGHBOR OF BRCA1 PROTEIN; NUCLEAR PROTEIN; PROTEIN P62; UNCLASSIFIED DRUG;

EID: 84873569630     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2012.12.008     Document Type: Article
Times cited : (44)

References (60)
  • 1
    • 84860837080 scopus 로고    scopus 로고
    • Light and electron microscopic characterization of the evolution of cellular pathology in the R6/1 Huntington's disease transgenic mice
    • Bayram-Weston Z., Jones L., Dunnett S.B., Brooks S.P. Light and electron microscopic characterization of the evolution of cellular pathology in the R6/1 Huntington's disease transgenic mice. Brain Res. Bull. 2012, 88:104-112.
    • (2012) Brain Res. Bull. , vol.88 , pp. 104-112
    • Bayram-Weston, Z.1    Jones, L.2    Dunnett, S.B.3    Brooks, S.P.4
  • 2
    • 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., Lamark T., Brech A., Outzen H., Perander M., Overvatn A., Stenmark H., Johansen T. 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    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 4
    • 33745862719 scopus 로고    scopus 로고
    • Potential compensatory responses through autophagic/lysosomal pathways in neurodegenerative diseases
    • Butler D., Nixon R.A., Bahr B.A. Potential compensatory responses through autophagic/lysosomal pathways in neurodegenerative diseases. Autophagy 2006, 2:234-237.
    • (2006) Autophagy , vol.2 , pp. 234-237
    • Butler, D.1    Nixon, R.A.2    Bahr, B.A.3
  • 5
    • 84858153178 scopus 로고    scopus 로고
    • Induced pluripotent stem cell lines from Huntington's disease mice undergo neuronal differentiation while showing alterations in the lysosomal pathway
    • Castiglioni V., Onorati M., Rochon C., Cattaneo E. Induced pluripotent stem cell lines from Huntington's disease mice undergo neuronal differentiation while showing alterations in the lysosomal pathway. Neurobiol. Dis. 2012, 46:30-40.
    • (2012) Neurobiol. Dis. , vol.46 , pp. 30-40
    • Castiglioni, V.1    Onorati, M.2    Rochon, C.3    Cattaneo, E.4
  • 6
    • 79954464577 scopus 로고    scopus 로고
    • Expanded polyglutamine domain possesses nuclear export activity which modulates subcellular localization and toxicity of polyQ disease protein via exportin-1
    • Chan W.M., Tsoi H., Wu C.C., Wong C.H., Cheng T.C., Li H.Y., Lau K.F., Shaw P.C., Perrimon N., Chan H.Y. Expanded polyglutamine domain possesses nuclear export activity which modulates subcellular localization and toxicity of polyQ disease protein via exportin-1. Hum. Mol. Genet. 2011, 20:1738-1750.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1738-1750
    • Chan, W.M.1    Tsoi, H.2    Wu, C.C.3    Wong, C.H.4    Cheng, T.C.5    Li, H.Y.6    Lau, K.F.7    Shaw, P.C.8    Perrimon, N.9    Chan, H.Y.10
  • 7
    • 79551655290 scopus 로고    scopus 로고
    • Huntington's disease: can mice lead the way to treatment?
    • Crook Z.R., Housman D. Huntington's disease: can mice lead the way to treatment?. Neuron 2011, 69:423-435.
    • (2011) Neuron , vol.69 , pp. 423-435
    • Crook, Z.R.1    Housman, D.2
  • 9
    • 82355175806 scopus 로고    scopus 로고
    • Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis
    • D'Agostino C., Nogalska A., Cacciottolo M., King E.W., Askanas V. Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis. Acta Neuropathol. 2011, 122:627-636.
    • (2011) Acta Neuropathol. , vol.122 , pp. 627-636
    • D'Agostino, C.1    Nogalska, A.2    Cacciottolo, M.3    King, E.W.4    Askanas, V.5
  • 10
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997, 277:1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 13
    • 80053960641 scopus 로고    scopus 로고
    • Increased PKA signaling disrupts recognition memory and spatial memory: role in Huntington's disease
    • Giralt A., Saavedra A., Carreton O., Xifro X., Alberch J., Perez-Navarro E. Increased PKA signaling disrupts recognition memory and spatial memory: role in Huntington's disease. Hum. Mol. Genet. 2011, 20:4232-4247.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4232-4247
    • Giralt, A.1    Saavedra, A.2    Carreton, O.3    Xifro, X.4    Alberch, J.5    Perez-Navarro, E.6
  • 16
    • 0030582370 scopus 로고    scopus 로고
    • Murine peritoneal macrophages induce a novel 60-kDa protein with structural similarity to a tyrosine kinase p56lck-associated protein in response to oxidative stress
    • Ishii T., Yanagawa T., Kawane T., Yuki K., Seita J., Yoshida H., Bannai S. Murine peritoneal macrophages induce a novel 60-kDa protein with structural similarity to a tyrosine kinase p56lck-associated protein in response to oxidative stress. Biochem. Biophys. Res. Commun. 1996, 226:456-460.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 456-460
    • Ishii, T.1    Yanagawa, T.2    Kawane, T.3    Yuki, K.4    Seita, J.5    Yoshida, H.6    Bannai, S.7
  • 17
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • Ishii T., Itoh K., Takahashi S., Sato H., Yanagawa T., Katoh Y., Bannai S., Yamamoto M. Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. J. Biol. Chem. 2000, 275:16023-16029.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6    Bannai, S.7    Yamamoto, M.8
  • 18
    • 78651282673 scopus 로고    scopus 로고
    • P62 Targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding
    • Itakura E., Mizushima N. p62 Targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding. J. Cell Biol. 2011, 192:17-27.
    • (2011) J. Cell Biol. , vol.192 , pp. 17-27
    • Itakura, E.1    Mizushima, N.2
  • 20
    • 77954599053 scopus 로고    scopus 로고
    • P62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • Jain A., Lamark T., Sjottem E., Larsen K.B., Awuh J.A., Overvatn A., McMahon M., Hayes J.D., Johansen T. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J. Biol. Chem. 2010, 285:22576-22591.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22576-22591
    • Jain, A.1    Lamark, T.2    Sjottem, E.3    Larsen, K.B.4    Awuh, J.A.5    Overvatn, A.6    McMahon, M.7    Hayes, J.D.8    Johansen, T.9
  • 21
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T., Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy 2011, 7:279-296.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 22
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel K.B., Kim M., Sapp E., McIntyre C., Castano J.G., Aronin N., DiFiglia M. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J. Neurosci. 2000, 20:7268-7278.
    • (2000) J. Neurosci. , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6    DiFiglia, M.7
  • 27
    • 0034805395 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells
    • Kuusisto E., Suuronen T., Salminen A. Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells. Biochem. Biophys. Res. Commun. 2001, 280:223-228.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 223-228
    • Kuusisto, E.1    Suuronen, T.2    Salminen, A.3
  • 29
    • 83455169115 scopus 로고    scopus 로고
    • IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux
    • Lee H., Noh J.Y., Oh Y., Kim Y., Chang J.W., Chung C.W., Lee S.T., Kim M., Ryu H., Jung Y.K. IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux. Hum. Mol. Genet. 2012, 21:101-114.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 101-114
    • Lee, H.1    Noh, J.Y.2    Oh, Y.3    Kim, Y.4    Chang, J.W.5    Chung, C.W.6    Lee, S.T.7    Kim, M.8    Ryu, H.9    Jung, Y.K.10
  • 30
    • 0022876328 scopus 로고
    • Huntington's disease. Pathogenesis and management
    • Martin J.B., Gusella J.F. Huntington's disease. Pathogenesis and management. N. Engl. J. Med. 1986, 315:1267-1276.
    • (1986) N. Engl. J. Med. , vol.315 , pp. 1267-1276
    • Martin, J.B.1    Gusella, J.F.2
  • 33
    • 78650706363 scopus 로고    scopus 로고
    • Continuous and periodic expansion of CAG repeats in Huntington's disease R6/1 mice
    • Mollersen L., Rowe A.D., Larsen E., Rognes T., Klungland A. Continuous and periodic expansion of CAG repeats in Huntington's disease R6/1 mice. PLoS Genet. 2010, 6:e1001242.
    • (2010) PLoS Genet. , vol.6
    • Mollersen, L.1    Rowe, A.D.2    Larsen, E.3    Rognes, T.4    Klungland, A.5
  • 34
  • 35
    • 66449114033 scopus 로고    scopus 로고
    • P62 at the crossroads of autophagy, apoptosis, and cancer
    • Moscat J., Diaz-Meco M.T. p62 at the crossroads of autophagy, apoptosis, and cancer. Cell 2009, 137:1001-1004.
    • (2009) Cell , vol.137 , pp. 1001-1004
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 36
    • 79959364986 scopus 로고    scopus 로고
    • Dynamics of the degradation of ubiquitinated proteins by proteasomes and autophagy: association with sequestosome 1/p62
    • Myeku N., Figueiredo-Pereira M.E. Dynamics of the degradation of ubiquitinated proteins by proteasomes and autophagy: association with sequestosome 1/p62. J. Biol. Chem. 2011, 286:22426-22440.
    • (2011) J. Biol. Chem. , vol.286 , pp. 22426-22440
    • Myeku, N.1    Figueiredo-Pereira, M.E.2
  • 37
    • 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., Nukina N. Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions. J. Neurochem. 2004, 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
  • 38
    • 68349097450 scopus 로고    scopus 로고
    • P62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis
    • Nogalska A., Terracciano C., D'Agostino C., King E.W., Askanas V. p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis. Acta Neuropathol. 2009, 118:407-413.
    • (2009) Acta Neuropathol. , vol.118 , pp. 407-413
    • Nogalska, A.1    Terracciano, C.2    D'Agostino, C.3    King, E.W.4    Askanas, V.5
  • 39
    • 84865863969 scopus 로고    scopus 로고
    • Autophagic adapter protein NBR1 is localized in Lewy bodies and glial cytoplasmic inclusions and is involved in aggregate formation in alpha-synucleinopathy
    • Odagiri S., Tanji K., Mori F., Kakita A., Takahashi H., Wakabayashi K. Autophagic adapter protein NBR1 is localized in Lewy bodies and glial cytoplasmic inclusions and is involved in aggregate formation in alpha-synucleinopathy. Acta Neuropathol. 2012, 124:173-186.
    • (2012) Acta Neuropathol. , vol.124 , pp. 173-186
    • Odagiri, S.1    Tanji, K.2    Mori, F.3    Kakita, A.4    Takahashi, H.5    Wakabayashi, K.6
  • 40
    • 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 J.A., 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, 285:5941-5953.
    • (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
  • 41
    • 0342635463 scopus 로고    scopus 로고
    • Striatal oxidative damage parallels the expression of a neurological phenotype in mice transgenic for the mutation of Huntington's disease
    • Perez-Severiano F., Rios C., Segovia J. Striatal oxidative damage parallels the expression of a neurological phenotype in mice transgenic for the mutation of Huntington's disease. Brain Res. 2000, 862:234-237.
    • (2000) Brain Res. , vol.862 , pp. 234-237
    • Perez-Severiano, F.1    Rios, C.2    Segovia, J.3
  • 44
    • 29244480602 scopus 로고    scopus 로고
    • Proteasomes degrade proteins in focal subdomains of the human cell nucleus
    • Rockel T.D., Stuhlmann D., von M.A. Proteasomes degrade proteins in focal subdomains of the human cell nucleus. J. Cell Sci. 2005, 118:5231-5242.
    • (2005) J. Cell Sci. , vol.118 , pp. 5231-5242
    • Rockel, T.D.1    Stuhlmann, D.2    von, M.A.3
  • 49
    • 49349090155 scopus 로고    scopus 로고
    • Huntington's disease: degradation of mutant huntingtin by autophagy
    • Sarkar S., Rubinsztein D.C. Huntington's disease: degradation of mutant huntingtin by autophagy. FEBS J. 2008, 275:4263-4270.
    • (2008) FEBS J. , vol.275 , pp. 4263-4270
    • Sarkar, S.1    Rubinsztein, D.C.2
  • 50
    • 57649227693 scopus 로고    scopus 로고
    • Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies
    • Sarkar S., Ravikumar B., Floto R.A., Rubinsztein D.C. Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell Death Differ. 2009, 16:46-56.
    • (2009) Cell Death Differ. , vol.16 , pp. 46-56
    • Sarkar, S.1    Ravikumar, B.2    Floto, R.A.3    Rubinsztein, D.C.4
  • 52
    • 44149110574 scopus 로고    scopus 로고
    • Intermediate filament cytoskeleton of the liver in health and disease
    • Strnad P., Stumptner C., Zatloukal K., Denk H. Intermediate filament cytoskeleton of the liver in health and disease. Histochem. Cell Biol. 2008, 129:735-749.
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 735-749
    • Strnad, P.1    Stumptner, C.2    Zatloukal, K.3    Denk, H.4
  • 53
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993, 72:971-983. The Huntington's Disease Collaborative Research Group.
    • (1993) Cell , vol.72 , pp. 971-983
  • 54
    • 0037994340 scopus 로고    scopus 로고
    • P62 overexpression in breast tumors and regulation by prostate-derived Ets factor in breast cancer cells
    • Thompson H.G., Harris J.W., Wold B.J., Lin F., Brody J.P. p62 overexpression in breast tumors and regulation by prostate-derived Ets factor in breast cancer cells. Oncogene 2003, 22:2322-2333.
    • (2003) Oncogene , vol.22 , pp. 2322-2333
    • Thompson, H.G.1    Harris, J.W.2    Wold, B.J.3    Lin, F.4    Brody, J.P.5
  • 55
    • 0029809134 scopus 로고    scopus 로고
    • P62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins
    • Vadlamudi R.K., Joung I., Strominger J.L., Shin J. p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. J. Biol. Chem. 1996, 271:20235-20237.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20235-20237
    • Vadlamudi, R.K.1    Joung, I.2    Strominger, J.L.3    Shin, J.4
  • 57
    • 67349216078 scopus 로고    scopus 로고
    • Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover
    • Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M. Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover. FEBS Lett. 2009, 583:1846-1852.
    • (2009) FEBS Lett. , vol.583 , pp. 1846-1852
    • Waters, S.1    Marchbank, K.2    Solomon, E.3    Whitehouse, C.4    Gautel, M.5
  • 58
    • 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., Regulier E., Bates G.P., Paganetti P. Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease. J. Neurochem. 2008, 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    Regulier, E.6    Bates, G.P.7    Paganetti, P.8
  • 59
    • 79952585579 scopus 로고    scopus 로고
    • Integration of clearance mechanisms: the proteasome and autophagy
    • Wong E., Cuervo A.M. Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb. Perspect. Biol. 2010, 2:a006734.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2
    • Wong, E.1    Cuervo, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.