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Volumn 62, Issue 1, 2017, Pages 114-122

Neuron-to-Neuron Transfer of FUS in Drosophila Primary Neuronal Culture Is Enhanced by ALS-Associated Mutations

Author keywords

Drosophila primary neuronal culture; FACS; FUS; Mutations; Spreading

Indexed keywords

DROSOPHILA PROTEIN; RED FLUORESCENT PROTEIN; RNA BINDING PROTEIN FUS; TRANSCRIPTION FACTOR GAL4; FUS PROTEIN, HUMAN;

EID: 85018498350     PISSN: 08958696     EISSN: 15591166     Source Type: Journal    
DOI: 10.1007/s12031-017-0908-y     Document Type: Article
Times cited : (12)

References (38)
  • 1
    • 0029964391 scopus 로고    scopus 로고
    • A nuclear protein regulated during the transition from active to quiescent phenotype in cultured endothelial cells
    • COI: 1:CAS:528:DyaK28XhvVSgsbo%3D, PID: 8631501
    • Alliegro MC, Alliegro MA (1996) A nuclear protein regulated during the transition from active to quiescent phenotype in cultured endothelial cells. Dev Biol 174:288–297
    • (1996) Dev Biol , vol.174 , pp. 288-297
    • Alliegro, M.C.1    Alliegro, M.A.2
  • 2
    • 84970004962 scopus 로고    scopus 로고
    • Molecular mechanism of prion-like tau-induced neurodegeneration
    • PID: 27126544
    • Alonso AD, Beharry C, Corbo CP, Cohen LS (2016) Molecular mechanism of prion-like tau-induced neurodegeneration. Alzheimers Dement 12:1090–1097
    • (2016) Alzheimers Dement , vol.12 , pp. 1090-1097
    • Alonso, A.D.1    Beharry, C.2    Corbo, C.P.3    Cohen, L.S.4
  • 3
    • 30344449514 scopus 로고    scopus 로고
    • Synaptic protein synthesis associated with memory is regulated by the RISC pathway in Drosophila
    • COI: 1:CAS:528:DC%2BD28XntVGkuw%3D%3D, PID: 16413491
    • Ashraf SI, McLoon AL, Sclarsic SM, Kunes S (2006) Synaptic protein synthesis associated with memory is regulated by the RISC pathway in Drosophila. Cell 124:191–205
    • (2006) Cell , vol.124 , pp. 191-205
    • Ashraf, S.I.1    McLoon, A.L.2    Sclarsic, S.M.3    Kunes, S.4
  • 5
    • 84926226703 scopus 로고    scopus 로고
    • A fruitful endeavor: modeling ALS in the fruit fly
    • COI: 1:CAS:528:DC%2BC2cXhslehu7nL, PID: 25289585
    • Casci I, Pandey UB (2015) A fruitful endeavor: modeling ALS in the fruit fly. Brain Res 1607:47–74
    • (2015) Brain Res , vol.1607 , pp. 47-74
    • Casci, I.1    Pandey, U.B.2
  • 6
    • 80053087977 scopus 로고    scopus 로고
    • Expression of human FUS protein in Drosophila leads to progressive neurodegeneration
    • COI: 1:CAS:528:DC%2BC3MXovFehsLs%3D, PID: 21748598
    • Chen Y, Yang M, Deng J, Chen X, Ye Y, Zhu L, Liu J, Ye H, Shen Y, Li Y et al (2011) Expression of human FUS protein in Drosophila leads to progressive neurodegeneration. Protein Cell 2:477–486
    • (2011) Protein Cell , vol.2 , pp. 477-486
    • Chen, Y.1    Yang, M.2    Deng, J.3    Chen, X.4    Ye, Y.5    Zhu, L.6    Liu, J.7    Ye, H.8    Shen, Y.9    Li, Y.10
  • 9
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: blurring the divide between transmissibility and infectivity
    • COI: 1:CAS:528:DC%2BC3cXmsFeksLo%3D, PID: 20356930
    • Cushman M, Johnson BS, King OD, Gitler AD, Shorter J (2010) Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 123:1191–1201
    • (2010) J Cell Sci , vol.123 , pp. 1191-1201
    • Cushman, M.1    Johnson, B.S.2    King, O.D.3    Gitler, A.D.4    Shorter, J.5
  • 12
    • 79959865166 scopus 로고    scopus 로고
    • TDP-43 and FUS: a nuclear affair
    • COI: 1:CAS:528:DC%2BC3MXoslalu7w%3D, PID: 21700347
    • Dormann D, Haass C (2011) TDP-43 and FUS: a nuclear affair. Trends Neurosci 34:339–348
    • (2011) Trends Neurosci , vol.34 , pp. 339-348
    • Dormann, D.1    Haass, C.2
  • 14
    • 30544448358 scopus 로고    scopus 로고
    • TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
    • COI: 1:CAS:528:DC%2BD28XosFelsw%3D%3D, PID: 16317045
    • Fujii R, Takumi T (2005) TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines. J Cell Sci 118:5755–5765
    • (2005) J Cell Sci , vol.118 , pp. 5755-5765
    • Fujii, R.1    Takumi, T.2
  • 15
    • 15744378126 scopus 로고    scopus 로고
    • The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology
    • COI: 1:CAS:528:DC%2BD2MXis1Kmtbc%3D, PID: 15797031
    • Fujii R, Okabe S, Urushido T, Inoue K, Yoshimura A, Tachibana T, Nishikawa T, Hicks GG, Takumi T (2005) The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology. Curr Biol 15:587–593
    • (2005) Curr Biol , vol.15 , pp. 587-593
    • Fujii, R.1    Okabe, S.2    Urushido, T.3    Inoue, K.4    Yoshimura, A.5    Tachibana, T.6    Nishikawa, T.7    Hicks, G.G.8    Takumi, T.9
  • 16
    • 85012066425 scopus 로고    scopus 로고
    • Molecular mechanisms in the pathogenesis of Alzheimer’s disease and tauopathies-prion-like seeded aggregation and phosphorylation
    • Hasegawa M (2016) Molecular mechanisms in the pathogenesis of Alzheimer’s disease and tauopathies-prion-like seeded aggregation and phosphorylation. Biomol Ther 6
    • (2016) Biomol Ther , pp. 6
    • Hasegawa, M.1
  • 18
    • 84981352019 scopus 로고    scopus 로고
    • Proteomic analysis of FUS interacting proteins provides insights into FUS function and its role in ALS
    • COI: 1:CAS:528:DC%2BC28Xht1Ghtr7K, PID: 27460707
    • Kamelgarn M, Chen J, Kuang L, Arenas A, Zhai J, Zhu H, Gal J (2016) Proteomic analysis of FUS interacting proteins provides insights into FUS function and its role in ALS. Biochim Biophys Acta 1862:2004–2014
    • (2016) Biochim Biophys Acta , vol.1862 , pp. 2004-2014
    • Kamelgarn, M.1    Chen, J.2    Kuang, L.3    Arenas, A.4    Zhai, J.5    Zhu, H.6    Gal, J.7
  • 19
    • 79954616116 scopus 로고    scopus 로고
    • Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations
    • COI: 1:CAS:528:DC%2BC3MXkvFansrw%3D, PID: 21109527
    • Kino Y, Washizu C, Aquilanti E, Okuno M, Kurosawa M, Yamada M, Doi H, Nukina N (2011) Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations. Nucleic Acids Res 39:2781–2798
    • (2011) Nucleic Acids Res , vol.39 , pp. 2781-2798
    • Kino, Y.1    Washizu, C.2    Aquilanti, E.3    Okuno, M.4    Kurosawa, M.5    Yamada, M.6    Doi, H.7    Nukina, N.8
  • 21
    • 33749501976 scopus 로고    scopus 로고
    • Solubility and dissolution rate of progesterone-cyclodextrin-polymer systems
    • COI: 1:CAS:528:DC%2BD28XhtFemsLzN, PID: 17012117
    • Lahiani-Skiba M, Barbot C, Bounoure F, Joudieh S, Skiba M (2006) Solubility and dissolution rate of progesterone-cyclodextrin-polymer systems. Drug Dev Ind Pharm 32:1043–1058
    • (2006) Drug Dev Ind Pharm , vol.32 , pp. 1043-1058
    • Lahiani-Skiba, M.1    Barbot, C.2    Bounoure, F.3    Joudieh, S.4    Skiba, M.5
  • 22
    • 84941785675 scopus 로고    scopus 로고
    • Prion-like mechanism in amyotrophic lateral sclerosis: are protein aggregates the key?
    • PID: 25792864
    • Lee S, Kim HJ (2015) Prion-like mechanism in amyotrophic lateral sclerosis: are protein aggregates the key? Exp Neurobiol 24:1–7
    • (2015) Exp Neurobiol , vol.24 , pp. 1-7
    • Lee, S.1    Kim, H.J.2
  • 23
    • 0344407006 scopus 로고    scopus 로고
    • Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins
    • COI: 1:CAS:528:DC%2BD3sXhtVequrg%3D, PID: 12581738
    • Meissner M, Lopato S, Gotzmann J, Sauermann G, Barta A (2003) Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins. Exp Cell Res 283:184–195
    • (2003) Exp Cell Res , vol.283 , pp. 184-195
    • Meissner, M.1    Lopato, S.2    Gotzmann, J.3    Sauermann, G.4    Barta, A.5
  • 25
    • 84891947306 scopus 로고    scopus 로고
    • Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC2cXns1ajsQ%3D%3D, PID: 24280224
    • Nomura T, Watanabe S, Kaneko K, Yamanaka K, Nukina N, Furukawa Y (2014) Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis. J Biol Chem 289:1192–1202
    • (2014) J Biol Chem , vol.289 , pp. 1192-1202
    • Nomura, T.1    Watanabe, S.2    Kaneko, K.3    Yamanaka, K.4    Nukina, N.5    Furukawa, Y.6
  • 26
    • 0035940416 scopus 로고    scopus 로고
    • A conditional tissue-specific transgene expression system using inducible GAL4
    • COI: 1:CAS:528:DC%2BD3MXotFaiurs%3D, PID: 11675495
    • Osterwalder T, Yoon KS, White BH, Keshishian H (2001) A conditional tissue-specific transgene expression system using inducible GAL4. Proc Natl Acad Sci U S A 98:12596–12601
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12596-12601
    • Osterwalder, T.1    Yoon, K.S.2    White, B.H.3    Keshishian, H.4
  • 27
    • 84981188324 scopus 로고    scopus 로고
    • Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins
    • COI: 1:CAS:528:DC%2BC28XpvFChsbs%3D, PID: 27015757
    • Ratti A, Buratti E (2016) Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins. J Neurochem 138(Suppl 1):95–111
    • (2016) J Neurochem , vol.138 , pp. 95-111
    • Ratti, A.1    Buratti, E.2
  • 29
    • 84908304881 scopus 로고    scopus 로고
    • Stain-free detection as loading control alternative to ponceau and housekeeping protein immunodetection in Western blotting
    • PID: 25193447
    • Rivero-Gutiérrez B, Anzola A, Martínez-Augustin O, de Medina FS (2014) Stain-free detection as loading control alternative to ponceau and housekeeping protein immunodetection in Western blotting. Anal Biochem 467:1–3
    • (2014) Anal Biochem , vol.467 , pp. 1-3
    • Rivero-Gutiérrez, B.1    Anzola, A.2    Martínez-Augustin, O.3    de Medina, F.S.4
  • 31
    • 84949096416 scopus 로고    scopus 로고
    • Review: Prion-like mechanisms of transactive response DNA binding protein of 43 kDa (TDP-43) in amyotrophic lateral sclerosis (ALS)
    • COI: 1:CAS:528:DC%2BC2MXht1SrsbnP, PID: 25487060
    • Smethurst P, Sidle KC, Hardy J (2015) Review: Prion-like mechanisms of transactive response DNA binding protein of 43 kDa (TDP-43) in amyotrophic lateral sclerosis (ALS). Neuropathol Appl Neurobiol 41:578–597
    • (2015) Neuropathol Appl Neurobiol , vol.41 , pp. 578-597
    • Smethurst, P.1    Sidle, K.C.2    Hardy, J.3
  • 32
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • COI: 1:CAS:528:DC%2BC3MXls1Kks7c%3D, PID: 21541367
    • Sun Z, Diaz Z, Fang X, Hart MP, Chesi A, Shorter J, Gitler AD (2011) Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol 9:e1000614
    • (2011) PLoS Biol , vol.9
    • Sun, Z.1    Diaz, Z.2    Fang, X.3    Hart, M.P.4    Chesi, A.5    Shorter, J.6    Gitler, A.D.7
  • 34
    • 85028261236 scopus 로고    scopus 로고
    • Sorting out release, uptake and processing of alpha-synuclein during prion-like spread of pathology
    • Tyson T, Steiner JA, Brundin P (2015) Sorting out release, uptake and processing of alpha-synuclein during prion-like spread of pathology. J Neurochem 139(Suppl 1):275–289
    • (2015) J Neurochem , vol.139 , pp. 275-289
    • Tyson, T.1    Steiner, J.A.2    Brundin, P.3
  • 37
    • 80054840008 scopus 로고    scopus 로고
    • Genetic manipulation of genes and cells in the nervous system of the fruit fly
    • COI: 1:CAS:528:DC%2BC3MXhtlKrtL%2FN, PID: 22017985
    • Venken KJ, Simpson JH, Bellen HJ (2011) Genetic manipulation of genes and cells in the nervous system of the fruit fly. Neuron 72:202–230
    • (2011) Neuron , vol.72 , pp. 202-230
    • Venken, K.J.1    Simpson, J.H.2    Bellen, H.J.3
  • 38
    • 84977588048 scopus 로고    scopus 로고
    • The prion-like properties of amyloid-beta assemblies: implications for Alzheimer’s disease
    • Walker LC, Schelle J, Jucker M (2016) The prion-like properties of amyloid-beta assemblies: implications for Alzheimer’s disease. Cold Spring Harb Perspect Med 6
    • (2016) Cold Spring Harb Perspect Med , pp. 6
    • Walker, L.C.1    Schelle, J.2    Jucker, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.