메뉴 건너뛰기




Volumn 7, Issue 10, 2012, Pages

FUS-NLS/Transportin 1 Complex Structure Provides Insights into the Nuclear Targeting Mechanism of FUS and the Implications in ALS

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; FUSED IN SARCOMA PROTEIN; MUTANT PROTEIN; TRANSPORTIN 1; UNCLASSIFIED DRUG;

EID: 84867290759     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047056     Document Type: Article
Times cited : (52)

References (38)
  • 1
    • 15744378126 scopus 로고    scopus 로고
    • The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology
    • Fujii R, Okabe S, Urushido T, Inoue K, Yoshimura A, et al. (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
  • 2
    • 30544448358 scopus 로고    scopus 로고
    • TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
    • 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
  • 3
    • 77957317483 scopus 로고    scopus 로고
    • The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation
    • Buratti E, Baralle FE, (2010) The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation. RNA Biol 7: 420-429.
    • (2010) RNA Biol , vol.7 , pp. 420-429
    • Buratti, E.1    Baralle, F.E.2
  • 4
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C, Polymenidou M, Cleveland DW, (2010) TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum Mol Genet 19: R46-64.
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 5
    • 0030746523 scopus 로고    scopus 로고
    • TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
    • Zinszner H, Sok J, Immanuel D, Yin Y, Ron D, (1997) TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling. J Cell Sci 110 (Pt 15): 1741-1750.
    • (1997) J Cell Sci , vol.110 , Issue.Pt 15 , pp. 1741-1750
    • Zinszner, H.1    Sok, J.2    Immanuel, D.3    Yin, Y.4    Ron, D.5
  • 6
    • 0031035765 scopus 로고    scopus 로고
    • A topogenic role for the oncogenic N-terminus of TLS: nucleolar localization when transcription is inhibited
    • Zinszner H, Immanuel D, Yin Y, Liang FX, Ron D, (1997) A topogenic role for the oncogenic N-terminus of TLS: nucleolar localization when transcription is inhibited. Oncogene 14: 451-461.
    • (1997) Oncogene , vol.14 , pp. 451-461
    • Zinszner, H.1    Immanuel, D.2    Yin, Y.3    Liang, F.X.4    Ron, D.5
  • 7
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, et al. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323: 1205-1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski Jr., T.J.1    Bosco, D.A.2    Leclerc, A.L.3    Tamrazian, E.4    Vanderburg, C.R.5
  • 8
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, Rogelj B, Hortobagyi T, De Vos KJ, Nishimura AL, et al. (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323: 1208-1211.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3    De Vos, K.J.4    Nishimura, A.L.5
  • 9
    • 70449521091 scopus 로고    scopus 로고
    • Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease
    • Neumann M, Roeber S, Kretzschmar HA, Rademakers R, Baker M, et al. (2009) Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease. Acta Neuropathol 118: 605-616.
    • (2009) Acta Neuropathol , vol.118 , pp. 605-616
    • Neumann, M.1    Roeber, S.2    Kretzschmar, H.A.3    Rademakers, R.4    Baker, M.5
  • 10
    • 80053646130 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • Gal J, Zhang J, Kwinter DM, Zhai J, Jia H, et al. (2011) Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol Aging 32: 2323 e2327-2340.
    • (2011) Neurobiol Aging , vol.32
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5
  • 11
    • 77955792022 scopus 로고    scopus 로고
    • ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import
    • Dormann D, Rodde R, Edbauer D, Bentmann E, Fischer I, et al. (2010) ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J 29: 2841-2857.
    • (2010) EMBO J , vol.29 , pp. 2841-2857
    • Dormann, D.1    Rodde, R.2    Edbauer, D.3    Bentmann, E.4    Fischer, I.5
  • 12
    • 77957867303 scopus 로고    scopus 로고
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • Bosco DA, Lemay N, Ko HK, Zhou H, Burke C, et al. (2010) Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum Mol Genet 19: 4160-4175.
    • (2010) Hum Mol Genet , vol.19 , pp. 4160-4175
    • Bosco, D.A.1    Lemay, N.2    Ko, H.K.3    Zhou, H.4    Burke, C.5
  • 13
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee BJ, Cansizoglu AE, Suel KE, Louis TH, Zhang Z, et al. (2006) Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 126: 543-558.
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Suel, K.E.3    Louis, T.H.4    Zhang, Z.5
  • 15
    • 34948857985 scopus 로고    scopus 로고
    • Structural basis for substrate recognition and dissociation by human transportin 1
    • Imasaki T, Shimizu T, Hashimoto H, Hidaka Y, Kose S, et al. (2007) Structural basis for substrate recognition and dissociation by human transportin 1. Mol Cell 28: 57-67.
    • (2007) Mol Cell , vol.28 , pp. 57-67
    • Imasaki, T.1    Shimizu, T.2    Hashimoto, H.3    Hidaka, Y.4    Kose, S.5
  • 16
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp
    • Chook YM, Blobel G, (1999) Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Nature 399: 230-237.
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 18
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 19
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 24
    • 34249679116 scopus 로고    scopus 로고
    • p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis
    • Gal J, Strom AL, Kilty R, Zhang F, Zhu H, (2007) p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis. J Biol Chem 282: 11068-11077.
    • (2007) J Biol Chem , vol.282 , pp. 11068-11077
    • Gal, J.1    Strom, A.L.2    Kilty, R.3    Zhang, F.4    Zhu, H.5
  • 25
    • 67349155310 scopus 로고    scopus 로고
    • Two Italian kindreds with familial amyotrophic lateral sclerosis due to FUS mutation
    • Chiò A, Restagno G, Brunetti M, Ossola I, Calvo A, et al. (2009) Two Italian kindreds with familial amyotrophic lateral sclerosis due to FUS mutation. Neurobiol Aging 30: 1272-1275.
    • (2009) Neurobiol Aging , vol.30 , pp. 1272-1275
    • Chiò, A.1    Restagno, G.2    Brunetti, M.3    Ossola, I.4    Calvo, A.5
  • 26
    • 77955897545 scopus 로고    scopus 로고
    • Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations
    • Bäumer D, Hilton D, Paine SML, Turner MR, Lowe J, et al. (2010) Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations. Neurology 75: 611-618.
    • (2010) Neurology , vol.75 , pp. 611-618
    • Bäumer, D.1    Hilton, D.2    Paine, S.M.L.3    Turner, M.R.4    Lowe, J.5
  • 27
    • 78449287318 scopus 로고    scopus 로고
    • Extensive FUS-Immunoreactive Pathology in Juvenile Amyotrophic Lateral Sclerosis with Basophilic Inclusions
    • Huang EJ, Zhang J, Geser F, Trojanowski JQ, Strober JB, et al. (2010) Extensive FUS-Immunoreactive Pathology in Juvenile Amyotrophic Lateral Sclerosis with Basophilic Inclusions. Brain Pathology 20: 1069-1076.
    • (2010) Brain Pathology , vol.20 , pp. 1069-1076
    • Huang, E.J.1    Zhang, J.2    Geser, F.3    Trojanowski, J.Q.4    Strober, J.B.5
  • 28
    • 77956357112 scopus 로고    scopus 로고
    • Frameshift and novel mutations in FUS in familial amyotrophic lateral sclerosis and ALS/dementia
    • Yan J, Deng H-X, Siddique N, Fecto F, Chen W, et al. (2010) Frameshift and novel mutations in FUS in familial amyotrophic lateral sclerosis and ALS/dementia. Neurology 75: 807-814.
    • (2010) Neurology , vol.75 , pp. 807-814
    • Yan, J.1    Deng, H.-X.2    Siddique, N.3    Fecto, F.4    Chen, W.5
  • 29
    • 84859986072 scopus 로고    scopus 로고
    • TLS/FUS (translocated in liposarcoma/fused in sarcoma) regulates target gene transcription via single-stranded DNA response elements
    • Tan AY, Riley TR, Coady T, Bussemaker HJ, Manley JL, (2012) TLS/FUS (translocated in liposarcoma/fused in sarcoma) regulates target gene transcription via single-stranded DNA response elements. Proceedings of the National Academy of Sciences 109: 6030-6035.
    • (2012) Proceedings of the National Academy of Sciences , vol.109 , pp. 6030-6035
    • Tan, A.Y.1    Riley, T.R.2    Coady, T.3    Bussemaker, H.J.4    Manley, J.L.5
  • 31
    • 77951712967 scopus 로고    scopus 로고
    • FALS with FUS mutation in Japan, with early onset, rapid progress and basophilic inclusion
    • Suzuki N, Aoki M, Warita H, Kato M, Mizuno H, et al. (2010) FALS with FUS mutation in Japan, with early onset, rapid progress and basophilic inclusion. J Hum Genet 55: 252-254.
    • (2010) J Hum Genet , vol.55 , pp. 252-254
    • Suzuki, N.1    Aoki, M.2    Warita, H.3    Kato, M.4    Mizuno, H.5
  • 32
    • 33744798774 scopus 로고    scopus 로고
    • Onset and Progression in Inherited ALS Determined by Motor Neurons and Microglia
    • Boillée S, Yamanaka K, Lobsiger CS, Copeland NG, Jenkins NA, et al. (2006) Onset and Progression in Inherited ALS Determined by Motor Neurons and Microglia. Science 312: 1389-1392.
    • (2006) Science , vol.312 , pp. 1389-1392
    • Boillée, S.1    Yamanaka, K.2    Lobsiger, C.S.3    Copeland, N.G.4    Jenkins, N.A.5
  • 33
    • 39749188753 scopus 로고    scopus 로고
    • Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis
    • Yamanaka K, Chun SJ, Boillee S, Fujimori-Tonou N, Yamashita H, et al. (2008) Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis. Nat Neurosci 11: 251-253.
    • (2008) Nat Neurosci , vol.11 , pp. 251-253
    • Yamanaka, K.1    Chun, S.J.2    Boillee, S.3    Fujimori-Tonou, N.4    Yamashita, H.5
  • 36
    • 84858726202 scopus 로고    scopus 로고
    • Motor neuron apoptosis and neuromuscular junction perturbation are prominent features in a Drosophila model of Fus-mediated ALS
    • Xia R, Liu Y, Yang L, Gal J, Zhu H, et al. (2012) Motor neuron apoptosis and neuromuscular junction perturbation are prominent features in a Drosophila model of Fus-mediated ALS. Molecular Neurodegeneration 7: 10.
    • (2012) Molecular Neurodegeneration , vol.7 , pp. 10
    • Xia, R.1    Liu, Y.2    Yang, L.3    Gal, J.4    Zhu, H.5
  • 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). Proceedings of the National Academy of Sciences.
    • (2012) Proceedings of the National Academy of Sciences
    • Zhang, Z.C.1    Chook, Y.M.2
  • 38
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM, (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8: 127-134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.