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Volumn 22, Issue 20, 2013, Pages 4136-4147

Decreased number of gemini of coiled bodies and U12 snRNA level in amyotrophic lateral sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

SMALL NUCLEAR RIBONUCLEOPROTEIN; SMALL NUCLEAR RNA; SURVIVAL MOTOR NEURON PROTEIN; TAR DNA BINDING PROTEIN; URIDINE;

EID: 84881518613     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddt262     Document Type: Article
Times cited : (66)

References (53)
  • 4
    • 0037108967 scopus 로고    scopus 로고
    • Higher order arrangement of the eukaryotic nuclear bodies
    • USA
    • Wang, I.F., Reddy, N.M. and Shen, C.K. (2002) Higher order arrangement of the eukaryotic nuclear bodies. Proc. Natl. Acad. Sci.USA, 99, 13583-13588.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 13583-13588
    • Wang, I.F.1    Reddy, N.M.2    Shen, C.K.3
  • 5
    • 34247606414 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation
    • Tan, C.F., Eguchi, H., Tagawa, A., Onodera, O., Iwasaki, T., Tsujino, A., Nishizawa, M., Kakita, A. and Takahashi, H. (2007) TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation. Acta Neuropathol., 113, 535-542.
    • (2007) Acta Neuropathol. , vol.113 , pp. 535-542
    • Tan, C.F.1    Eguchi, H.2    Tagawa, A.3    Onodera, O.4    Iwasaki, T.5    Tsujino, A.6    Nishizawa, M.7    Kakita, A.8    Takahashi, H.9
  • 6
    • 77949878273 scopus 로고    scopus 로고
    • TDP-43 is a developmentally regulated protein essential for early embryonic development
    • Sephton, C.F., Good, S.K., Atkin, S., Dewey, C.M., Mayer, P. 3rd, Herz, J. and Yu, G. (2010) TDP-43 is a developmentally regulated protein essential for early embryonic development. J. Biol. Chem., 285, 6826-6834.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6826-6834
    • Sephton, C.F.1    Good, S.K.2    Atkin, S.3    Dewey, C.M.4    Mayer, P.5    Herz, J.6    Yu, G.7
  • 8
    • 74749107048 scopus 로고    scopus 로고
    • TDP-43, a neuro-pathosignature factor, is essential for early mouse embryogenesis
    • Wu, L.S., Cheng, W.C., Hou, S.C., Yan, Y.T., Jiang, S.T. and Shen, C.K. (2010) TDP-43, a neuro-pathosignature factor, is essential for early mouse embryogenesis. Genesis, 48, 56-62.
    • (2010) Genesis , vol.48 , pp. 56-62
    • Wu, L.S.1    Cheng, W.C.2    Hou, S.C.3    Yan, Y.T.4    Jiang, S.T.5    Shen, C.K.6
  • 9
    • 77958012134 scopus 로고    scopus 로고
    • Deletion of TDP-43down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism
    • Chiang, P.M., Ling, J., Jeong, Y.H., Price, D.L., Aja, S.M. and Wong, P.C. (2010) Deletion of TDP-43down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism. Proc. Natl. Acad. Sci. USA, 107, 16320- 16324.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107
    • Chiang, P.M.1    Ling, J.2    Jeong, Y.H.3    Price, D.L.4    Aja, S.M.5    Wong, P.C.6
  • 10
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne, C., Polymenidou,M.and Cleveland, D.W.(2010)TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet., 19, R46-R64.
    • (2010) Hum. Mol. Genet. , vol.19
    • Lagier-tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 11
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • Kuo, P.H., Doudeva, L.G., Wang, Y.T., Shen, C.K. and Yuan, H.S. (2009) Structural insights into TDP-43 in nucleic-acid binding and domain interactions. Nucleic Acids Res., 37, 1799-1808.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1799-1808
    • Kuo, P.H.1    Doudeva, L.G.2    Wang, Y.T.3    Shen, C.K.4    Yuan, H.S.5
  • 14
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association withRNA splicing and translation machinery
    • Freibaum, B.D., Chitta, R.K., High, A.A. and Taylor, J.P. (2010) Global analysis of TDP-43 interacting proteins reveals strong association withRNA splicing and translation machinery. J. Proteome. Res., 9, 1104-1120.
    • (2010) J. Proteome. Res. , vol.9 , pp. 1104-1120
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 15
    • 57649174592 scopus 로고    scopus 로고
    • TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing
    • Bose, J.K., Wang, I.F., Hung, L., Tarn, W.Y. and Shen, C.K. (2008) TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing. J. Biol. Chem., 283, 28852-28859.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28852-28859
    • Bose, J.K.1    Wang, I.F.2    Hung, L.3    Tarn, W.Y.4    Shen, C.K.5
  • 16
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • Buratti, E., Dork, T., Zuccato, E., Pagani, F., Romano, M. and Baralle, F.E. (2001) Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J., 20, 1774-1784.
    • (2001) EMBO J. , vol.20 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5    Baralle, F.E.6
  • 18
    • 84859361694 scopus 로고    scopus 로고
    • TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR
    • Fiesel, F.C., Weber, S.S., Supper, J., Zell, A. and Kahle, P.J. (2012) TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR. Nucleic Acids Res., 40, 2668-2682.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2668-2682
    • Fiesel, F.C.1    Weber, S.S.2    Supper, J.3    Zell, A.4    Kahle, P.J.5
  • 19
    • 84860863883 scopus 로고    scopus 로고
    • TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells
    • Colombrita, C., Onesto, E., Megiorni, F., Pizzuti, A., Baralle, F.E., Buratti, E., Silani, V. and Ratti, A. (2012) TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells. J. Biol. Chem, 287, 15635-15647.
    • (2012) J. Biol. Chem , vol.287 , pp. 15635-15647
    • Colombrita, C.1    Onesto, E.2    Megiorni, F.3    Pizzuti, A.4    Baralle, F.E.5    Buratti, E.6    Silani, V.7    Ratti, A.8
  • 20
    • 77949477815 scopus 로고    scopus 로고
    • Sporadic ALS has compartment-specific aberrant exon splicing and altered cell-matrix adhesion biology
    • Rabin, S.J., Kim, J.M., Baughn, M., Libby, R.T., Kim, Y.J., Fan, Y., La Spada, A., Stone, B. and Ravits, J. (2010) Sporadic ALS has compartment-specific aberrant exon splicing and altered cell-matrix adhesion biology. Hum. Mol. Genet., 19, 313-328.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 313-328
    • Rabin, S.J.1    Kim, J.M.2    Baughn, M.3    Libby, R.T.4    Kim, Y.J.5    Fan, Y.6    Spada, A.7    Stone, B.8    Ravits, J.9
  • 21
    • 0345169036 scopus 로고    scopus 로고
    • Splicing double: insights from the second spliceosome
    • Patel, A.A. and Steitz, J.A. (2003) Splicing double: insights from the second spliceosome. Nat. Rev. Mol. Cell Biol., 4, 960-970.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 960-970
    • Patel, A.A.1    Steitz, J.A.2
  • 22
    • 0344198459 scopus 로고    scopus 로고
    • The spliceosome: the most complex macromolecular machine in the cell
    • Nilsen, T.W. (2003) The spliceosome: the most complex macromolecular machine in the cell? Bioessays, 25, 1147-1149.
    • (2003) Bioessays , vol.25 , pp. 1147-1149
    • Nilsen, T.W.1
  • 23
    • 26844431946 scopus 로고    scopus 로고
    • Splicing of a rare class of introns by the U12-dependent spliceosome
    • Will, C.L. and Luhrmann, R. (2005) Splicing of a rare class of introns by the U12-dependent spliceosome. Biol. Chem., 386, 713-724.
    • (2005) Biol. Chem. , vol.386 , pp. 713-724
    • Will, C.L.1    Luhrmann, R.2
  • 24
    • 0035476520 scopus 로고    scopus 로고
    • A computational scan for U12-dependent introns in the human genome sequence
    • Levine, A. and Durbin, R. (2001) A computational scan for U12-dependent introns in the human genome sequence. Nucleic Acids Res., 29, 4006-4013.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4006-4013
    • Levine, A.1    Durbin, R.2
  • 25
    • 33846071878 scopus 로고    scopus 로고
    • U12DB: a database of orthologous U12-type spliceosomal introns
    • Alioto, T.S. (2007) U12DB: a database of orthologous U12-type spliceosomal introns. Nucleic Acids Res., 35, D110-D115.
    • (2007) Nucleic Acids Res. , vol.35
    • Alioto, T.S.1
  • 26
    • 0344080588 scopus 로고    scopus 로고
    • Modification of Sm small nuclear RNAs occurs in the nucleoplasmic Cajal body following import from the cytoplasm
    • Jady, B.E., Darzacq, X., Tucker, K.E., Matera, A.G., Bertrand, E. and Kiss, T. (2003) Modification of Sm small nuclear RNAs occurs in the nucleoplasmic Cajal body following import from the cytoplasm. EMBO J., 22, 1878-1888.
    • (2003) EMBO J. , vol.22 , pp. 1878-1888
    • Jady, B.E.1    Darzacq, X.2    Tucker, K.E.3    Matera, A.G.4    Bertrand, E.5    Kiss, T.6
  • 27
    • 79960622503 scopus 로고    scopus 로고
    • Biogenesis and function of nuclear bodies
    • Mao, Y.S., Zhang, B. and Spector, D.L. (2011) Biogenesis and function of nuclear bodies. Trends Genet., 27, 295-306.
    • (2011) Trends Genet. , vol.27 , pp. 295-306
    • Mao, Y.S.1    Zhang, B.2    Spector, D.L.3
  • 28
    • 67651083390 scopus 로고    scopus 로고
    • Spinal muscular atrophy:whydo low levels of survival motor neuron protein make motor neurons sick
    • Burghes, A.H. and Beattie, C.E. (2009) Spinal muscular atrophy:whydo low levels of survival motor neuron protein make motor neurons sick? Nat. Rev. Neurosci., 10, 597-609.
    • (2009) Nat.Rev. Neurosci. , vol.10 , pp. 597-609
    • Burghes, A.H.1    Beattie, C.E.2
  • 29
    • 77958022745 scopus 로고    scopus 로고
    • Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
    • Shan, X., Chiang, P.M., Price, D.L. and Wong, P.C. (2010) Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc. Natl. Acad. Sci. USA, 107, 16325-16330.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16325-16330
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 32
    • 43049168361 scopus 로고    scopus 로고
    • SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing
    • Zhang, Z., Lotti, F., Dittmar, K., Younis, I., Wan, L., Kasim, M. and Dreyfuss, G. (2008) SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing. Cell, 133, 585-600.
    • (2008) Cell , vol.133 , pp. 585-600
    • Zhang, Z.1    Lotti, F.2    Dittmar, K.3    Younis, I.4    Wan, L.5    Kasim, M.6    Dreyfuss, G.7
  • 33
    • 41549119007 scopus 로고    scopus 로고
    • Ribonucleoprotein assembly defects correlate with spinal muscular atrophy severity and preferentially affect a subset of spliceosomal snRNPs
    • e921
    • Gabanella, F., Butchbach, M.E., Saieva, L., Carissimi, C., Burghes, A.H. and Pellizzoni, L. (2007) Ribonucleoprotein assembly defects correlate with spinal muscular atrophy severity and preferentially affect a subset of spliceosomal snRNPs. PLoS One, 2, e921.
    • (2007) PLoS One , vol.2
    • Gabanella, F.1    Butchbach, M.E.2    Saieva, L.3    Carissimi, C.4    Burghes, A.H.5    Pellizzoni, L.6
  • 34
    • 45249106162 scopus 로고    scopus 로고
    • Spinal muscular atrophy
    • Lunn, M.R. and Wang, C.H. (2008) Spinal muscular atrophy. Lancet, 371, 2120-2133.
    • (2008) Lancet , vol.371 , pp. 2120-2133
    • Lunn, M.R.1    Wang, C.H.2
  • 36
    • 34047100275 scopus 로고    scopus 로고
    • A comprehensive interaction map of the human survival of motor neuron (SMN) complex
    • Otter, S., Grimmler, M., Neuenkirchen, N., Chari, A., Sickmann, A. and Fischer, U. (2007) A comprehensive interaction map of the human survival of motor neuron (SMN) complex. J. Biol. Chem., 282, 5825-5833.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5825-5833
    • Otter, S.1    Grimmler, M.2    Neuenkirchen, N.3    Chari, A.4    Sickmann, A.5    Fischer, U.6
  • 38
    • 47949096734 scopus 로고    scopus 로고
    • Sporadic amyotrophic lateral sclerosis: two pathological patternsshownby analysis of distribution of TDP-43-immunoreactive neuronal and glial cytoplasmic inclusions
    • Nishihira, Y., Tan, C.F., Onodera, O., Toyoshima, Y., Yamada, M., Morita, T., Nishizawa, M., Kakita, A. and Takahashi, H. (2008) Sporadic amyotrophic lateral sclerosis: two pathological patternsshownby analysis of distribution of TDP-43-immunoreactive neuronal and glial cytoplasmic inclusions. Acta Neuropathol., 116, 169-182.
    • (2008) Acta Neuropathol. , vol.116 , pp. 169-182
    • Nishihira, Y.1    Tan, C.F.2    Onodera, O.3    Toyoshima, Y.4    Yamada, M.5    Morita, T.6    Nishizawa, M.7    Kakita, A.8    Takahashi, H.9
  • 39
    • 43249101441 scopus 로고    scopus 로고
    • The U11-48 Kprotein contacts the 5 ' splice site of U12-type introns and the U11-59 K protein
    • Turunen, J.J., Will, C.L., Grote, M., Luhrmann,R. and Frilander, M.J. (2008) The U11-48 Kprotein contacts the 5 ' splice site of U12-type introns and the U11-59 K protein. Mol. Cell Biol., 28, 3548-3560.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 3548-3560
    • Turunen, J.J.1    Will, C.L.2    Grote, M.3    Luhrmann, R.4    Frilander, M.J.5
  • 40
    • 70350754211 scopus 로고    scopus 로고
    • Rates of in situ transcription and splicing in large human genes
    • Singh, J. and Padgett, R.A. (2009) Rates of in situ transcription and splicing in large human genes. Nat. Struct. Mol. Biol., 16, 1128-1133.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1128-1133
    • Singh, J.1    Padgett, R.A.2
  • 41
    • 33749261487 scopus 로고    scopus 로고
    • The abundance of the spliceosomal snRNPs is not limiting the splicing of U12-type introns
    • Pessa, H.K., Ruokolainen, A. and Frilander, M.J. (2006) The abundance of the spliceosomal snRNPs is not limiting the splicing of U12-type introns. RNA, 12, 1883-1892.
    • (2006) RNA , vol.12 , pp. 1883-1892
    • Pessa, H.K.1    Ruokolainen, A.2    Frilander, M.J.3
  • 42
    • 34047148903 scopus 로고    scopus 로고
    • Chaperoning ribonucleoprotein biogenesis in health and disease
    • Pellizzoni, L. (2007) Chaperoning ribonucleoprotein biogenesis in health and disease. EMBO Rep., 8, 340-345.
    • (2007) EMBO Rep. , vol.8 , pp. 340-345
    • Pellizzoni, L.1
  • 43
    • 0032952059 scopus 로고    scopus 로고
    • Coiled bodies preferentially associate with U4, U11, and U12 small nuclear RNA genes in interphase HeLa cells but not with U6 and U7 genes
    • Jacobs, E.Y., Frey, M.R., Wu, W., Ingledue, T.C., Gebuhr, T.C., Gao, L., Marzluff, W.F. and Matera, A.G. (1999) Coiled bodies preferentially associate with U4, U11, and U12 small nuclear RNA genes in interphase HeLa cells but not with U6 and U7 genes. Mol. Biol. Cell, 10, 1653-1663.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1653-1663
    • Jacobs, E.Y.1    Frey, M.R.2    Wu, W.3    Ingledue, T.C.4    Gebuhr, T.C.5    Gao, L.6    Marzluff, W.F.7    Matera, A.G.8
  • 45
    • 79953824569 scopus 로고    scopus 로고
    • Mutations in U4atac snRNA, a component of the minor spliceosome, in the developmental disorderMOPD I
    • He, H., Liyanarachchi, S., Akagi, K., Nagy, R., Li, J., Dietrich, R.C., Li, W., Sebastian, N., Wen, B., Xin, B. et al. (2011) Mutations in U4atac snRNA, a component of the minor spliceosome, in the developmental disorderMOPD I. Science, 332, 238-240.
    • (2011) Science , vol.332 , pp. 238-240
    • He, H.1    Liyanarachchi, S.2    Akagi, K.3    Nagy, R.4    Li, J.5    Dietrich, R.C.6    Li, W.7    Sebastian, N.8    Wen, B.9    Xin, B.10
  • 47
    • 58149259990 scopus 로고    scopus 로고
    • De novo formation of a subnuclear body
    • Kaiser, T.E., Intine, R.V. and Dundr, M. (2008) De novo formation of a subnuclear body. Science, 322, 1713-1717.
    • (2008) Science , vol.322 , pp. 1713-1717
    • Kaiser, T.E.1    Intine, R.V.2    Dundr, M.3
  • 49
    • 47949099336 scopus 로고    scopus 로고
    • Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia
    • Mori, F., Tanji, K., Zhang, H.X., Nishihira, Y., Tan, C.F., Takahashi, H. and Wakabayashi, K. (2008) Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia. Acta Neuropathol., 116, 193-203.
    • (2008) Acta Neuropathol , vol.116 , pp. 193-203
    • Mori, F.1    Tanji, K.2    Zhang, H.X.3    Nishihira, Y.4    Tan, C.F.5    Takahashi, H.6    Wakabayashi, K.7
  • 50
    • 35348853257 scopus 로고    scopus 로고
    • TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis
    • Neumann, M., Kwong, L.K., Sampathu, D.M., Trojanowski, J.Q. and Lee, V.M. (2007) TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis. Arch. Neurol., 64, 1388-1394.
    • (2007) Arch. Neurol. , vol.64 , pp. 1388-1394
    • Neumann, M.1    Kwong, L.K.2    Sampathu, D.M.3    Trojanowski, J.Q.4    Lee, V.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.