메뉴 건너뛰기




Volumn 34, Issue 1, 2014, Pages 19-26

ALS-associated protein FIG4 is localized in Pick and Lewy bodies, and also neuronal nuclear inclusions, in polyglutamine and intranuclear inclusion body diseases

Author keywords

Endosomal lysosomal pathway; FIG4; Lewy body; Nuclear inclusion; Pick body

Indexed keywords

ALPHA SYNUCLEIN; FIG4 PROTEIN; PHOSPHATASE; POLYGLUTAMINE; UNCLASSIFIED DRUG;

EID: 84892802771     PISSN: 09196544     EISSN: 14401789     Source Type: Journal    
DOI: 10.1111/neup.12056     Document Type: Article
Times cited : (23)

References (44)
  • 1
    • 0030608273 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain
    • Nagase T, Seki N, Ishikawa K etal. Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res 1996; 3: 321-329.
    • (1996) DNA Res , vol.3 , pp. 321-329
    • Nagase, T.1    Seki, N.2    Ishikawa, K.3
  • 2
    • 0032498622 scopus 로고    scopus 로고
    • Pheromone-regulated genes required for yeast mating differentiation
    • Erdman S, Lin L, Malczynski M, Snyder M. Pheromone-regulated genes required for yeast mating differentiation. J Cell Biol 1998; 140: 461-483.
    • (1998) J Cell Biol , vol.140 , pp. 461-483
    • Erdman, S.1    Lin, L.2    Malczynski, M.3    Snyder, M.4
  • 3
    • 82555200841 scopus 로고    scopus 로고
    • Congenital CNS hypomyelination in the Fig4 null mouse is rescued by neuronal expression of the PI(3,5)P phosphatase Fig4
    • Winters JJ, Ferguson CJ, Lenk GM etal. Congenital CNS hypomyelination in the Fig4 null mouse is rescued by neuronal expression of the PI(3, 5)P phosphatase Fig4. J Neurosci 2011; 31: 17736-17751.
    • (2011) J Neurosci , vol.31 , pp. 17736-17751
    • Winters, J.J.1    Ferguson, C.J.2    Lenk, G.M.3
  • 4
    • 84655163880 scopus 로고    scopus 로고
    • Fig4 expression in the rodent nervous system and its potential role in preventing abnormal lysosomal accumulation
    • Guo J, Ma YH, Yan Q etal. Fig4 expression in the rodent nervous system and its potential role in preventing abnormal lysosomal accumulation. J Neuropathol Exp Neurol 2012; 71: 28-39.
    • (2012) J Neuropathol Exp Neurol , vol.71 , pp. 28-39
    • Guo, J.1    Ma, Y.H.2    Yan, Q.3
  • 5
    • 84865089799 scopus 로고    scopus 로고
    • Neuronal expression of Fig4 is both necessary and sufficient to prevent spongiform neurodegeneration
    • Ferguson CJ, Lenk GM, Jones JM etal. Neuronal expression of Fig4 is both necessary and sufficient to prevent spongiform neurodegeneration. Hum Mol Genet 2012; 21: 3525-3534.
    • (2012) Hum Mol Genet , vol.21 , pp. 3525-3534
    • Ferguson, C.J.1    Lenk, G.M.2    Jones, J.M.3
  • 6
    • 34447133038 scopus 로고    scopus 로고
    • Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J
    • Chow CY, Zhang Y, Dowling JJ etal. Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J. Nature 2007; 448: 68-72.
    • (2007) Nature , vol.448 , pp. 68-72
    • Chow, C.Y.1    Zhang, Y.2    Dowling, J.J.3
  • 7
    • 49449098975 scopus 로고    scopus 로고
    • Mutation of FIG4 causes a rapidly progressive, asymmetric neuronal degeneration
    • Zhang X, Chow CY, Sahenk Z, Shy ME, Meisler MH, Li J. Mutation of FIG4 causes a rapidly progressive, asymmetric neuronal degeneration. Brain 2008; 131: 1990-2001.
    • (2008) Brain , vol.131 , pp. 1990-2001
    • Zhang, X.1    Chow, C.Y.2    Sahenk, Z.3    Shy, M.E.4    Meisler, M.H.5    Li, J.6
  • 8
    • 58049192812 scopus 로고    scopus 로고
    • Deleterious variants of FIG4, a phosphoinositide phosphatase, in patients with ALS
    • Chow CY, Landers JE, Bergren SK etal. Deleterious variants of FIG4, a phosphoinositide phosphatase, in patients with ALS. Am J Hum Genet 2009; 84: 85-88.
    • (2009) Am J Hum Genet , vol.84 , pp. 85-88
    • Chow, C.Y.1    Landers, J.E.2    Bergren, S.K.3
  • 10
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: when the cleaning crew goes on strike
    • Martinez-Vicente M, Cuervo AM. Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol 2007; 6: 352-361.
    • (2007) Lancet Neurol , vol.6 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 11
    • 59249097160 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies
    • Arai T, Mackenzie IR, Hasegawa M etal. Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies. Acta Neuropathol 2009; 117: 125-136.
    • (2009) Acta Neuropathol , vol.117 , pp. 125-136
    • Arai, T.1    Mackenzie, I.R.2    Hasegawa, M.3
  • 12
    • 69949174325 scopus 로고    scopus 로고
    • Selective occurrence of TDP-43-immunoreactive inclusions in the lower motor neurons in Machado-Joseph disease
    • Tan C-F, Yamada M, Toyoshima Y etal. Selective occurrence of TDP-43-immunoreactive inclusions in the lower motor neurons in Machado-Joseph disease. Acta Neuropathol 2009; 118: 553-560.
    • (2009) Acta Neuropathol , vol.118 , pp. 553-560
    • Tan, C.-F.1    Yamada, M.2    Toyoshima, Y.3
  • 13
    • 80054715358 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 2 (SCA2) is associated with TDP-43 pathology
    • Toyoshima Y, Tanaka H, Shimohata M etal. Spinocerebellar ataxia type 2 (SCA2) is associated with TDP-43 pathology. Acta Neuropathol 2011; 122: 375-378.
    • (2011) Acta Neuropathol , vol.122 , pp. 375-378
    • Toyoshima, Y.1    Tanaka, H.2    Shimohata, M.3
  • 15
    • 77950788517 scopus 로고    scopus 로고
    • FUS-immunoreactive intranuclear inclusions in neurodegenerative disease
    • Woulfe J, Gray DA, Mackenzie IR. FUS-immunoreactive intranuclear inclusions in neurodegenerative disease. Brain Pathol 2010; 20: 589-597.
    • (2010) Brain Pathol , vol.20 , pp. 589-597
    • Woulfe, J.1    Gray, D.A.2    Mackenzie, I.R.3
  • 16
    • 84860901797 scopus 로고    scopus 로고
    • FUS immunoreactivity of neuronal and glial intranuclear inclusions in intranuclear inclusion body disease
    • Mori F, Tanji K, Kon T etal. FUS immunoreactivity of neuronal and glial intranuclear inclusions in intranuclear inclusion body disease. Neuropathol Appl Neurobiol 2012; 38: 322-328.
    • (2012) Neuropathol Appl Neurobiol , vol.38 , pp. 322-328
    • Mori, F.1    Tanji, K.2    Kon, T.3
  • 18
    • 84862679022 scopus 로고    scopus 로고
    • Optineurin immunoreactivity in neuronal nuclear inclusions of polyglutamine diseases (Huntington's, DRPLA, SCA2, SCA3) and intranuclear inclusion body disease
    • Mori F, Tanji K, Toyoshima Y etal. Optineurin immunoreactivity in neuronal nuclear inclusions of polyglutamine diseases (Huntington's, DRPLA, SCA2, SCA3) and intranuclear inclusion body disease. Acta Neuropathol 2012; 123: 747-749.
    • (2012) Acta Neuropathol , vol.123 , pp. 747-749
    • Mori, F.1    Tanji, K.2    Toyoshima, Y.3
  • 19
    • 84862756869 scopus 로고    scopus 로고
    • Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion
    • Brettschneider J, Van Deerlin VM, Robinson JL etal. Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion. Acta Neuropathol 2012; 123: 825-839.
    • (2012) Acta Neuropathol , vol.123 , pp. 825-839
    • Brettschneider, J.1    Van Deerlin, V.M.2    Robinson, J.L.3
  • 20
    • 84862765926 scopus 로고    scopus 로고
    • Ubiquilin immunoreactivity in cytoplasmic and nuclear inclusions in synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease
    • Mori F, Tanji K, Odagiri S etal. Ubiquilin immunoreactivity in cytoplasmic and nuclear inclusions in synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease. Acta Neuropathol 2012; 124: 149-151.
    • (2012) Acta Neuropathol , vol.124 , pp. 149-151
    • Mori, F.1    Tanji, K.2    Odagiri, S.3
  • 21
    • 84866491973 scopus 로고    scopus 로고
    • Endosomal sorting related protein CHMP2B is localized in Lewy bodies and glial cytoplasmic inclusions in α-synucleinopathy
    • Tanikawa S, Mori F, Tanji K, Kakita A, Takahashi H, Wakabayashi K. Endosomal sorting related protein CHMP2B is localized in Lewy bodies and glial cytoplasmic inclusions in α-synucleinopathy. Neurosci Lett 2012; 527: 16-21.
    • (2012) Neurosci Lett , vol.527 , pp. 16-21
    • Tanikawa, S.1    Mori, F.2    Tanji, K.3    Kakita, A.4    Takahashi, H.5    Wakabayashi, K.6
  • 22
    • 84878664294 scopus 로고    scopus 로고
    • Localization of CHMP2B-immunoreactivity in the brainstem of Lewy body disease
    • Kurashige T, Takahashi T, Yamazaki Y etal. Localization of CHMP2B-immunoreactivity in the brainstem of Lewy body disease. Neuropathology 2013; 33: 237-245.
    • (2013) Neuropathology , vol.33 , pp. 237-245
    • Kurashige, T.1    Takahashi, T.2    Yamazaki, Y.3
  • 23
    • 84897077024 scopus 로고    scopus 로고
    • Valosin-containing protein immunoreactivity in tauopathies, synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease
    • Mori F, Tanji K, Toyoshima Y etal. Valosin-containing protein immunoreactivity in tauopathies, synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease. Neuropathology 2013; 33: 637-644.
    • (2013) Neuropathology , vol.33 , pp. 637-644
    • Mori, F.1    Tanji, K.2    Toyoshima, Y.3
  • 24
    • 79959599081 scopus 로고    scopus 로고
    • A harmonized classification system for FTLD-TDP pathology
    • Mackenzie IR, Neumann M, Baborie A etal. A harmonized classification system for FTLD-TDP pathology. Acta Neuropathol 2011; 122: 111-113.
    • (2011) Acta Neuropathol , vol.122 , pp. 111-113
    • Mackenzie, I.R.1    Neumann, M.2    Baborie, A.3
  • 25
    • 0031715399 scopus 로고    scopus 로고
    • Accumulation of α-synuclein/NACP is a cytopathological feature common to Lewy body disease and multiple system atrophy
    • Wakabayashi K, Hayashi S, Kakita A etal. Accumulation of α-synuclein/NACP is a cytopathological feature common to Lewy body disease and multiple system atrophy. Acta Neuropathol 1998; 96: 445-452.
    • (1998) Acta Neuropathol , vol.96 , pp. 445-452
    • Wakabayashi, K.1    Hayashi, S.2    Kakita, A.3
  • 26
    • 1842789766 scopus 로고    scopus 로고
    • Accumulation of phosphorylated α-synuclein in the brain and peripheral ganglia of patients with multiple system atrophy
    • Nishie M, Mori F, Fujiwara H etal. Accumulation of phosphorylated α-synuclein in the brain and peripheral ganglia of patients with multiple system atrophy. Acta Neuropathol 2004; 107: 292-298.
    • (2004) Acta Neuropathol , vol.107 , pp. 292-298
    • Nishie, M.1    Mori, F.2    Fujiwara, H.3
  • 27
    • 0018645615 scopus 로고
    • Regular arrangements of tubular structures in Pick bodies formed in an autopsied case of Pick's disease (in Japanese with English abstract)
    • Oyanagi S, Tanaka M, Omori T, Matsushita M, Ishii T. Regular arrangements of tubular structures in Pick bodies formed in an autopsied case of Pick's disease (in Japanese with English abstract). Shinkei Simpo 1979; 23: 441-451.
    • (1979) Shinkei Simpo , vol.23 , pp. 441-451
    • Oyanagi, S.1    Tanaka, M.2    Omori, T.3    Matsushita, M.4    Ishii, T.5
  • 29
    • 0036942389 scopus 로고    scopus 로고
    • Pick's disease: α- and β-synuclein-immunoreactive Pick bodies in the dentate gyrus
    • Mori F, Hayashi S, Yamagishi S etal. Pick's disease: α- and β-synuclein-immunoreactive Pick bodies in the dentate gyrus. Acta Neuropathol 2002; 104: 455-461.
    • (2002) Acta Neuropathol , vol.104 , pp. 455-461
    • Mori, F.1    Hayashi, S.2    Yamagishi, S.3
  • 30
    • 84937088414 scopus 로고
    • Phase and electron microscopic observations of Lewy bodies and melanin granules in the substantia nigra and locus caeruleus in Parkinson's disease
    • Duffy PE, Tennyson VM. Phase and electron microscopic observations of Lewy bodies and melanin granules in the substantia nigra and locus caeruleus in Parkinson's disease. J Neuropathol Exp Neurol 1965; 24: 398-414.
    • (1965) J Neuropathol Exp Neurol , vol.24 , pp. 398-414
    • Duffy, P.E.1    Tennyson, V.M.2
  • 31
    • 12944269063 scopus 로고    scopus 로고
    • SAC3 may link nuclear protein export to cell cycle progression
    • Jones AL, Quimby BB, Hood JK etal. SAC3 may link nuclear protein export to cell cycle progression. Proc Natl Acad Sci USA 2000; 97: 3224-3229.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3224-3229
    • Jones, A.L.1    Quimby, B.B.2    Hood, J.K.3
  • 32
    • 78049430399 scopus 로고    scopus 로고
    • Polyglutamine diseases: where does toxicity come from? What is toxicity? Where are we going?
    • Takahashi T, Katada S, Onodera O. Polyglutamine diseases: where does toxicity come from? What is toxicity? Where are we going? J Mol Cell Biol 2010; 2: 180-191.
    • (2010) J Mol Cell Biol , vol.2 , pp. 180-191
    • Takahashi, T.1    Katada, S.2    Onodera, O.3
  • 33
    • 1842563060 scopus 로고    scopus 로고
    • Substantia nigra Marinesco bodies are associated with decreased striatal expression of dopaminergic markers
    • Beach TG, Walker DG, Sue LL, Newell A, Adler CC, Joyce JN. Substantia nigra Marinesco bodies are associated with decreased striatal expression of dopaminergic markers. J Neuropathol Exp Neurol 2004; 63: 329-337.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 329-337
    • Beach, T.G.1    Walker, D.G.2    Sue, L.L.3    Newell, A.4    Adler, C.C.5    Joyce, J.N.6
  • 34
    • 0016402119 scopus 로고
    • A study of the Marinesco body in monkey (Macaca fuscata). A comparative study to the Marinesco body in man (in Japanese with English abstract)
    • Ikeda K. A study of the Marinesco body in monkey (Macaca fuscata). A comparative study to the Marinesco body in man (in Japanese with English abstract). Seishin Shinkeigaku Zasshi 1974; 76: 778-792.
    • (1974) Seishin Shinkeigaku Zasshi , vol.76 , pp. 778-792
    • Ikeda, K.1
  • 35
    • 84861531546 scopus 로고    scopus 로고
    • Immunohistochemical analysis of Marinesco bodies, using antibodies against proteins implicated in the ubiquitin-proteasome system, autophagy and aggresome formation
    • Odagiri S, Tanji K, Mori F etal. Immunohistochemical analysis of Marinesco bodies, using antibodies against proteins implicated in the ubiquitin-proteasome system, autophagy and aggresome formation. Neuropathology 2012; 32: 261-266.
    • (2012) Neuropathology , vol.32 , pp. 261-266
    • Odagiri, S.1    Tanji, K.2    Mori, F.3
  • 36
    • 34248139628 scopus 로고    scopus 로고
    • Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae
    • Suzuki K, Ohsumi Y. Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae. FEBS Lett 2007; 581: 2156-2161.
    • (2007) FEBS Lett , vol.581 , pp. 2156-2161
    • Suzuki, K.1    Ohsumi, Y.2
  • 37
    • 34447116281 scopus 로고    scopus 로고
    • Phosphoinositides link to neurodegeneration
    • Volpicelli-Daley L, De Camilli P. Phosphoinositides link to neurodegeneration. Nat Med 2007; 13: 784-786.
    • (2007) Nat Med , vol.13 , pp. 784-786
    • Volpicelli-Daley, L.1    De Camilli, P.2
  • 38
    • 48249115147 scopus 로고    scopus 로고
    • Clearance of a Hirano body-like F-actin aggresome generated by jasplakinolide
    • Lázaro-Diéguez F, Knecht E, Egea G. Clearance of a Hirano body-like F-actin aggresome generated by jasplakinolide. Autophagy 2008; 4: 717-720.
    • (2008) Autophagy , vol.4 , pp. 717-720
    • Lázaro-Diéguez, F.1    Knecht, E.2    Egea, G.3
  • 39
    • 84884660504 scopus 로고    scopus 로고
    • Ubiquilin-1 immunoreactivity is concentrated on Hirano bodies and dystrophic neuritis in Alzhermer's disease brains
    • doi: 10.1111/nan.12036
    • Satoh J, Tabunoki H, Ishida T, Saito Y, Arima K. Ubiquilin-1 immunoreactivity is concentrated on Hirano bodies and dystrophic neuritis in Alzhermer's disease brains. Neuropathol Appl Neurobiol 2013. doi: 10.1111/nan.12036
    • (2013) Neuropathol Appl Neurobiol
    • Satoh, J.1    Tabunoki, H.2    Ishida, T.3    Saito, Y.4    Arima, K.5
  • 41
    • 79751480230 scopus 로고    scopus 로고
    • Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1 accumulation and aggresome formation
    • Viswanathan J, Haapasalo A, Böttcher C etal. Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1 accumulation and aggresome formation. Traffic 2011; 12: 330-348.
    • (2011) Traffic , vol.12 , pp. 330-348
    • Viswanathan, J.1    Haapasalo, A.2    Böttcher, C.3
  • 42
    • 77955023765 scopus 로고    scopus 로고
    • Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
    • Rothenberg C, Srinivasan D, Mah L etal. Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy. Hum Mol Genet 2010; 19: 3219-3232.
    • (2010) Hum Mol Genet , vol.19 , pp. 3219-3232
    • Rothenberg, C.1    Srinivasan, D.2    Mah, L.3
  • 43
    • 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
  • 44
    • 59649110865 scopus 로고    scopus 로고
    • PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation
    • N'Diaye EN, Kajihara KK, Hsieh I, Morisaki H, Debnath J, Brown EJ. PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation. EMBO Rep 2009; 10: 173-179.
    • (2009) EMBO Rep , vol.10 , pp. 173-179
    • N'Diaye, E.N.1    Kajihara, K.K.2    Hsieh, I.3    Morisaki, H.4    Debnath, J.5    Brown, E.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.