메뉴 건너뛰기




Volumn 111, Issue 44, 2014, Pages E4769-E4778

Activity-dependent FUS dysregulation disrupts

Author keywords

Amyotrophic lateral sclerosis; Frontotemporal lobar degeneration; FUS; Metabotropic glutamate receptors; Synaptic homeostasis

Indexed keywords

CRE RECOMBINASE; FUSED IN SARCOMA PROTEIN; METABOTROPIC RECEPTOR 1; METABOTROPIC RECEPTOR 5; RNA BINDING PROTEIN;

EID: 84914696708     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1406162111     Document Type: Article
Times cited : (101)

References (51)
  • 1
    • 0037044240 scopus 로고    scopus 로고
    • The overlap of amyotrophic lateral sclerosis and frontotemporal dementia
    • Lomen-Hoerth C, Anderson T, Miller B (2002) The overlap of amyotrophic lateral sclerosis and frontotemporal dementia. Neurology 59(7):1077-1079.
    • (2002) Neurology , vol.59 , Issue.7 , pp. 1077-1079
    • Lomen-Hoerth, C.1    Anderson, T.2    Miller, B.3
  • 2
    • 77649187519 scopus 로고    scopus 로고
    • Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: An update
    • Mackenzie IR, et al. (2010) Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: An update. Acta Neuropathol 119(1):1-4.
    • (2010) Acta Neuropathol , vol.119 , Issue.1 , pp. 1-4
    • Mackenzie, I.R.1
  • 3
    • 84884821327 scopus 로고    scopus 로고
    • Fused in sarcoma (FUS): An oncogene goes awry in neurodegeneration
    • Dormann D, Haass C (2013) Fused in sarcoma (FUS): An oncogene goes awry in neurodegeneration. Mol Cell Neurosci 56:475-486.
    • (2013) Mol Cell Neurosci , vol.56 , pp. 475-486
    • Dormann, D.1    Haass, C.2
  • 4
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee EB, Lee VM, Trojanowski JQ (2012) Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci 13(1):38-50.
    • (2012) Nat Rev Neurosci , vol.13 , Issue.1 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 5
    • 77449136874 scopus 로고    scopus 로고
    • The TET family of proteins: Functions and roles in disease
    • Tan AY, Manley JL (2009) The TET family of proteins: Functions and roles in disease. J Mol Cell Biol 1(2):82-92.
    • (2009) J Mol Cell Biol , vol.1 , Issue.2 , pp. 82-92
    • Tan, A.Y.1    Manley, J.L.2
  • 6
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNAbinding proteins
    • Burd CG, Dreyfuss G (1994) Conserved structures and diversity of functions of RNAbinding proteins. Science 265(5172):615-621.
    • (1994) Science , vol.265 , Issue.5172 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 7
    • 0035794162 scopus 로고    scopus 로고
    • Identification of an RNA binding specificity for the potential splicing factor TLS
    • Lerga A, et al. (2001) Identification of an RNA binding specificity for the potential splicing factor TLS. J Biol Chem 276(9):6807-6816.
    • (2001) J Biol Chem , vol.276 , Issue.9 , pp. 6807-6816
    • Lerga, A.1
  • 8
    • 7244242399 scopus 로고    scopus 로고
    • Domain architectures and characterization of an RNA-binding protein, TLS
    • Iko Y, et al. (2004) Domain architectures and characterization of an RNA-binding protein, TLS. J Biol Chem 279(43):44834-44840.
    • (2004) J Biol Chem , vol.279 , Issue.43 , pp. 44834-44840
    • Iko, Y.1
  • 9
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • Kato M, et al. (2012) Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels. Cell 149(4):753-767.
    • (2012) Cell , vol.149 , Issue.4 , pp. 753-767
    • Kato, M.1
  • 10
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee BJ, et al. (2006) Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 126(3):543-558.
    • (2006) Cell , vol.126 , Issue.3 , pp. 543-558
    • Lee, B.J.1
  • 11
    • 84869237956 scopus 로고    scopus 로고
    • Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS
    • Dormann D, et al. (2012) Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS. EMBO J 31(22):4258-4275.
    • (2012) EMBO J , vol.31 , Issue.22 , pp. 4258-4275
    • Dormann, D.1
  • 12
    • 79959865166 scopus 로고    scopus 로고
    • TDP-43 and FUS: A nuclear affair
    • Dormann D, Haass C (2011) TDP-43 and FUS: A nuclear affair. Trends Neurosci 34(7): 339-348.
    • (2011) Trends Neurosci , vol.34 , Issue.7 , pp. 339-348
    • Dormann, D.1    Haass, C.2
  • 13
    • 84863309952 scopus 로고    scopus 로고
    • Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43)
    • Bentmann E, et al. (2012) Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43). J Biol Chem 287(27): 23079-23094.
    • (2012) J Biol Chem , vol.287 , Issue.27 , pp. 23079-23094
    • Bentmann, E.1
  • 14
    • 15744378126 scopus 로고    scopus 로고
    • The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology
    • Fujii R, et al. (2005) The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology. Curr Biol 15(6):587-593.
    • (2005) Curr Biol , vol.15 , Issue.6 , pp. 587-593
    • Fujii, R.1
  • 15
    • 84887510924 scopus 로고    scopus 로고
    • Mutations in the 3? Untranslated region of FUS causing FUS overexpression are associated with amyotrophic lateral sclerosis
    • Sabatelli M, et al. (2013) Mutations in the 3? untranslated region of FUS causing FUS overexpression are associated with amyotrophic lateral sclerosis. Hum Mol Genet 22(23):4748-4755.
    • (2013) Hum Mol Genet , vol.22 , Issue.23 , pp. 4748-4755
    • Sabatelli, M.1
  • 16
    • 70449528427 scopus 로고    scopus 로고
    • TARDBP 3?-UTR variant in autopsy-confirmed frontotemporal lobar degeneration with TDP-43 proteinopathy
    • Gitcho MA, et al. (2009) TARDBP 3?-UTR variant in autopsy-confirmed frontotemporal lobar degeneration with TDP-43 proteinopathy. Acta Neuropathol 118(5):633-645.
    • (2009) Acta Neuropathol , vol.118 , Issue.5 , pp. 633-645
    • Gitcho, M.A.1
  • 17
    • 29444442794 scopus 로고    scopus 로고
    • APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy
    • Rovelet-Lecrux A, et al. (2006) APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy. Nat Genet 38(1): 24-26.
    • (2006) Nat Genet , vol.38 , Issue.1 , pp. 24-26
    • Rovelet-Lecrux, A.1
  • 18
    • 4644290985 scopus 로고    scopus 로고
    • Alpha-synuclein locus duplication as a cause of familial Parkinson's disease
    • Chartier-Harlin MC, et al. (2004) Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364(9440):1167-1169.
    • (2004) Lancet , vol.364 , Issue.9440 , pp. 1167-1169
    • Chartier-Harlin, M.C.1
  • 19
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski TJ, Jr, et al. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323(5918):1205-1208.
    • (2009) Science , vol.323 , Issue.5918 , pp. 1205-1208
    • Kwiatkowski, T.J.1
  • 20
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, et al. (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323(5918):1208-1211.
    • (2009) Science , vol.323 , Issue.5918 , pp. 1208-1211
    • Vance, C.1
  • 21
    • 84871590658 scopus 로고    scopus 로고
    • FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2
    • Schwartz JC, et al. (2012) FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2. Genes Dev 26(24):2690-2695.
    • (2012) Genes Dev , vol.26 , Issue.24 , pp. 2690-2695
    • Schwartz, J.C.1
  • 22
    • 84864448921 scopus 로고    scopus 로고
    • Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions
    • Ishigaki S, et al. (2012) Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions. Sci Rep 2:529.
    • (2012) Sci Rep , vol.2 , pp. 529
    • Ishigaki, S.1
  • 23
    • 84866126892 scopus 로고    scopus 로고
    • Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain
    • Rogelj B, et al. (2012) Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain. Sci Rep 2:603.
    • (2012) Sci Rep , vol.2 , pp. 603
    • Rogelj, B.1
  • 24
    • 82955236089 scopus 로고    scopus 로고
    • RNA targets of wild-type and mutant FET family proteins
    • Hoell JI, et al. (2011) RNA targets of wild-type and mutant FET family proteins. Nat Struct Mol Biol 18(12):1428-1431.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.12 , pp. 1428-1431
    • Hoell, J.I.1
  • 25
    • 84868152371 scopus 로고    scopus 로고
    • Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs
    • Lagier-Tourenne C, et al. (2012) Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs. Nat Neurosci 15(11):1488-1497.
    • (2012) Nat Neurosci , vol.15 , Issue.11 , pp. 1488-1497
    • Lagier-Tourenne, C.1
  • 26
    • 84888440451 scopus 로고    scopus 로고
    • Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains
    • Kwon I, et al. (2013) Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains. Cell 155(5):1049-1060.
    • (2013) Cell , vol.155 , Issue.5 , pp. 1049-1060
    • Kwon, I.1
  • 27
    • 17444381645 scopus 로고    scopus 로고
    • Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: Exclusion from the nucleus and accumulation in dendritic granules and spine heads
    • Belly A, Moreau-Gachelin F, Sadoul R, Goldberg Y (2005) Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: Exclusion from the nucleus and accumulation in dendritic granules and spine heads. Neurosci Lett 379(3): 152-157.
    • (2005) Neurosci Lett , vol.379 , Issue.3 , pp. 152-157
    • Belly, A.1    Moreau-Gachelin, F.2    Sadoul, R.3    Goldberg, Y.4
  • 28
    • 0037022346 scopus 로고    scopus 로고
    • Dendritic spines elongate after stimulation of group 1 metabotropic glutamate receptors in cultured hippocampal neurons
    • Vanderklish PW, Edelman GM (2002) Dendritic spines elongate after stimulation of group 1 metabotropic glutamate receptors in cultured hippocampal neurons. Proc Natl Acad Sci USA 99(3):1639-1644.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.3 , pp. 1639-1644
    • Vanderklish, P.W.1    Edelman, G.M.2
  • 29
    • 84855993931 scopus 로고    scopus 로고
    • P525L FUS mutation is consistently associated with a severe form of juvenile amyotrophic lateral sclerosis
    • Conte A, et al. (2012) P525L FUS mutation is consistently associated with a severe form of juvenile amyotrophic lateral sclerosis. Neuromuscul Disord 22(1):73-75.
    • (2012) Neuromuscul Disord , vol.22 , Issue.1 , pp. 73-75
    • Conte, A.1
  • 30
    • 84860904002 scopus 로고    scopus 로고
    • Novel FUS deletion in a patient with juvenile amyotrophic lateral sclerosis
    • Belzil VV, et al. (2012) Novel FUS deletion in a patient with juvenile amyotrophic lateral sclerosis. Arch Neurol 69(5):653-656.
    • (2012) Arch Neurol , vol.69 , Issue.5 , pp. 653-656
    • Belzil, V.V.1
  • 31
    • 84872327415 scopus 로고    scopus 로고
    • De novo FUS gene mutations are associated with juvenile-onset sporadic amyotrophic lateral sclerosis in China
    • 1312 e8
    • Zou ZY, et al. (2013) De novo FUS gene mutations are associated with juvenile-onset sporadic amyotrophic lateral sclerosis in China. Neurobiol Aging 34(4):1312.e1-1312. e8.
    • (2013) Neurobiol Aging , vol.34 , Issue.4 , pp. e1-e1312
    • Zou, Z.Y.1
  • 32
    • 84902276700 scopus 로고    scopus 로고
    • Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U
    • Lee EB, et al. (2013) Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U. Acta Neuropathologica Comm 1(9):1-11.
    • (2013) Acta Neuropathologica Comm , vol.1 , Issue.9 , pp. 1-11
    • Lee, E.B.1
  • 33
    • 84891904592 scopus 로고    scopus 로고
    • R521C mutation in the FUS/TLS gene presenting as juvenile onset flail leg syndrome
    • Taieb G, et al. (2013) R521C mutation in the FUS/TLS gene presenting as juvenile onset flail leg syndrome. Muscle Nerve 48(6):993-994.
    • (2013) Muscle Nerve , vol.48 , Issue.6 , pp. 993-994
    • Taieb, G.1
  • 34
    • 77955127561 scopus 로고    scopus 로고
    • Fus gene mutations in familial and sporadic amyotrophic lateral sclerosis
    • Rademakers R, et al. (2010) Fus gene mutations in familial and sporadic amyotrophic lateral sclerosis. Muscle Nerve 42(2):170-176.
    • (2010) Muscle Nerve , vol.42 , Issue.2 , pp. 170-176
    • Rademakers, R.1
  • 35
    • 77949760219 scopus 로고    scopus 로고
    • Mutations of FUS gene in sporadic amyotrophic lateral sclerosis
    • Corrado L, et al. (2010) Mutations of FUS gene in sporadic amyotrophic lateral sclerosis. J Med Genet 47(3):190-194.
    • (2010) J Med Genet , vol.47 , Issue.3 , pp. 190-194
    • Corrado, L.1
  • 36
    • 84855791444 scopus 로고    scopus 로고
    • Synaptic dysfunction in progranulin-deficient mice
    • Petkau TL, et al. (2012) Synaptic dysfunction in progranulin-deficient mice. Neurobiol Dis 45(2):711-722.
    • (2012) Neurobiol Dis , vol.45 , Issue.2 , pp. 711-722
    • Petkau, T.L.1
  • 37
    • 84864366184 scopus 로고    scopus 로고
    • Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)
    • Zhang ZC, Chook YM (2012) Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS). Proc Natl Acad Sci USA 109(30):12017-12021.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.30 , pp. 12017-12021
    • Zhang, Z.C.1    Chook, Y.M.2
  • 38
    • 79958720175 scopus 로고    scopus 로고
    • A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43
    • Lanson NA, Jr, et al. (2011) A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43. Hum Mol Genet 20(13): 2510-2523.
    • (2011) Hum Mol Genet , vol.20 , Issue.13 , pp. 2510-2523
    • Lanson, N.A.1
  • 39
    • 83455213568 scopus 로고    scopus 로고
    • ALS mutations in FUS cause neuronal dysfunction and death in Caenorhabditis elegans by a dominant gain-of-function mechanism
    • Murakami T, et al. (2012) ALS mutations in FUS cause neuronal dysfunction and death in Caenorhabditis elegans by a dominant gain-of-function mechanism. Hum Mol Genet 21(1):1-9.
    • (2012) Hum Mol Genet , vol.21 , Issue.1 , pp. 1-9
    • Murakami, T.1
  • 40
    • 79953743204 scopus 로고    scopus 로고
    • FUS transgenic rats develop the phenotypes of amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • Huang C, et al. (2011) FUS transgenic rats develop the phenotypes of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. PLoS Genet 7(3):e1002011.
    • (2011) PLoS Genet , vol.7 , Issue.3 , pp. e1002011
    • Huang, C.1
  • 41
    • 84875427900 scopus 로고    scopus 로고
    • Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashion
    • Mitchell JC, et al. (2013) Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashion. Acta Neuropathol 125(2):273-288.
    • (2013) Acta Neuropathol , vol.125 , Issue.2 , pp. 273-288
    • Mitchell, J.C.1
  • 42
    • 74049164709 scopus 로고    scopus 로고
    • Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond
    • Ilieva H, Polymenidou M, Cleveland DW (2009) Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond. J Cell Biol 187(6):761-772.
    • (2009) J Cell Biol , vol.187 , Issue.6 , pp. 761-772
    • Ilieva, H.1    Polymenidou, M.2    Cleveland, D.W.3
  • 43
    • 84896799718 scopus 로고    scopus 로고
    • ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects
    • Qiu H, et al. (2014) ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects. J Clin Invest 124(3):981-999.
    • (2014) J Clin Invest , vol.124 , Issue.3 , pp. 981-999
    • Qiu, H.1
  • 44
    • 0033946468 scopus 로고    scopus 로고
    • Proteomic analysis of NMDA receptor-adhesion protein signaling complexes
    • Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG (2000) Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat Neurosci 3(7):661-669.
    • (2000) Nat Neurosci , vol.3 , Issue.7 , pp. 661-669
    • Husi, H.1    Ward, M.A.2    Choudhary, J.S.3    Blackstock, W.P.4    Grant, S.G.5
  • 45
    • 84886953546 scopus 로고    scopus 로고
    • The translation of translational control by FMRP: Therapeutic targets for FXS
    • Darnell JC, Klann E (2013) The translation of translational control by FMRP: Therapeutic targets for FXS. Nat Neurosci 16(11):1530-1536.
    • (2013) Nat Neurosci , vol.16 , Issue.11 , pp. 1530-1536
    • Darnell, J.C.1    Klann, E.2
  • 46
    • 0033797832 scopus 로고    scopus 로고
    • Dendritic spine structural anomalies in fragile-X mental retardation syndrome
    • Irwin SA, Galvez R, Greenough WT (2000) Dendritic spine structural anomalies in fragile-X mental retardation syndrome. Cereb Cortex 10(10):1038-1044.
    • (2000) Cereb Cortex , vol.10 , Issue.10 , pp. 1038-1044
    • Irwin, S.A.1    Galvez, R.2    Greenough, W.T.3
  • 47
    • 77949878273 scopus 로고    scopus 로고
    • TDP-43 is a developmentally regulated protein essential for early embryonic development
    • Sephton CF, et al. (2010) TDP-43 is a developmentally regulated protein essential for early embryonic development. J Biol Chem 285(9):6826-6834.
    • (2010) J Biol Chem , vol.285 , Issue.9 , pp. 6826-6834
    • Sephton, C.F.1
  • 48
    • 79953158803 scopus 로고    scopus 로고
    • The role of synaptobrevin1/VAMP1 in Ca2+-triggered neurotransmitter release at the mouse neuromuscular junction
    • Liu Y, Sugiura Y, Lin W (2011) The role of synaptobrevin1/VAMP1 in Ca2+-triggered neurotransmitter release at the mouse neuromuscular junction. J Physiol 589(Pt 7): 1603-1618.
    • (2011) J Physiol , vol.589 , Issue.7 , pp. 1603-1618
    • Liu, Y.1    Sugiura, Y.2    Lin, W.3
  • 49
    • 79952268025 scopus 로고    scopus 로고
    • TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor
    • Dewey CM, et al. (2011) TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor. Mol Cell Biol 31(5):1098-1108.
    • (2011) Mol Cell Biol , vol.31 , Issue.5 , pp. 1098-1108
    • Dewey, C.M.1
  • 50
    • 78651408754 scopus 로고    scopus 로고
    • Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes
    • Sephton CF, et al. (2011) Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes. J Biol Chem 286(2):1204-1215.
    • (2011) J Biol Chem , vol.286 , Issue.2 , pp. 1204-1215
    • Sephton, C.F.1
  • 51
    • 80053900558 scopus 로고    scopus 로고
    • Preparation of synaptoneurosomes from mouse cortex using a discontinuous percoll-sucrose density gradient
    • Westmark PR, Westmark CJ, Jeevananthan A, Malter JS (2011) Preparation of synaptoneurosomes from mouse cortex using a discontinuous percoll-sucrose density gradient. J Vis Exp, 10.3791/3196.
    • (2011) J Vis Exp
    • Westmark, P.R.1    Westmark, C.J.2    Jeevananthan, A.3    Malter, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.