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Volumn 270, Issue 11, 2003, Pages 2459-2466

Emerin interacts in vitro with the splicing-associated factor, YT521-B

Author keywords

Emery Dreifuss muscular dystrophy; Gene regulation; Lamin; RNA splicing; Yeast two hybrid

Indexed keywords

ALANINE; COMPLEMENTARY DNA; EMERIN; LAMIN A; LAMIN C; NUCLEAR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR YT521B; UNCLASSIFIED DRUG;

EID: 0038392580     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03617.x     Document Type: Article
Times cited : (89)

References (45)
  • 4
    • 0035194146 scopus 로고    scopus 로고
    • The role of the nuclear envelope in Emery-Dreifuss muscular dystrophy
    • Morris, G.E. (2001) The role of the nuclear envelope in Emery-Dreifuss muscular dystrophy. Trends Mol. Med. 7, 572-577.
    • (2001) Trends Mol. Med. , vol.7 , pp. 572-577
    • Morris, G.E.1
  • 5
    • 0010397284 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
    • Manilal, S., Nguyen, T.M., Sewry, C.A. & Morris, G.E. (1996) The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. Hum. Mol. Genet. 5, 801-806.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 801-806
    • Manilal, S.1    Nguyen, T.M.2    Sewry, C.A.3    Morris, G.E.4
  • 6
    • 0033786789 scopus 로고    scopus 로고
    • Nuclear envelope proteins and associated diseases
    • Nagano, A. & Arahata, K. (1996) Nuclear envelope proteins and associated diseases. Curr. Opin. Neurol. 13, 533-539.
    • (1996) Curr. Opin. Neurol. , vol.13 , pp. 533-539
    • Nagano, A.1    Arahata, K.2
  • 7
    • 0032771080 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane
    • Fairley, E.A.L., Kendrick-Jones, J. & Ellis, J.A. (1999) The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane. J. Cell Sci. 112, 2571-2582.
    • (1999) J. Cell Sci. , vol.112 , pp. 2571-2582
    • Fairley, E.A.L.1    Kendrick-Jones, J.2    Ellis, J.A.3
  • 9
    • 0035694820 scopus 로고    scopus 로고
    • Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF
    • Lee, K.K., Haraguchi, T., Lee, R.S., Koujin, T., Hiraoka, Y. & Wilson, K.L. (2001) Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J. Cell Sci. 114, 4567-4573.
    • (2001) J. Cell Sci. , vol.114 , pp. 4567-4573
    • Lee, K.K.1    Haraguchi, T.2    Lee, R.S.3    Koujin, T.4    Hiraoka, Y.5    Wilson, K.L.6
  • 10
    • 0032778974 scopus 로고    scopus 로고
    • LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction
    • Furukawa, K. (1999) LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction. J. Cell Sci. 112, 2485-2492.
    • (1999) J. Cell Sci. , vol.112 , pp. 2485-2492
    • Furukawa, K.1
  • 15
    • 0033125723 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy database
    • Yates, J.R.W. & Wehnert, M. (1999) The Emery-Dreifuss muscular dystrophy database. Neuromusc. Disord. 9, 199.
    • (1999) Neuromusc. Disord. , vol.9 , pp. 199
    • Yates, J.R.W.1    Wehnert, M.2
  • 16
    • 0031005848 scopus 로고    scopus 로고
    • Emerin deletion reveals a common X-chromosome inversion mediated by inverted repeats
    • Small, K., Iber, J. & Warren, S.T. (1997) Emerin deletion reveals a common X-chromosome inversion mediated by inverted repeats. Nature Genet. 16, 96-99.
    • (1997) Nature Genet. , vol.16 , pp. 96-99
    • Small, K.1    Iber, J.2    Warren, S.T.3
  • 17
    • 0032939360 scopus 로고    scopus 로고
    • Changes at P183 of emerin weaken its protein-protein interactions resulting in Emery-Dreifuss muscular dystrophy
    • Ellis, J.A., Yates, J.R.W., Kendrick-Jones, J. & Brown, C.A. (1999) Changes at P183 of emerin weaken its protein-protein interactions resulting in Emery-Dreifuss muscular dystrophy. Hum. Genet. 104, 262-268.
    • (1999) Hum. Genet. , vol.104 , pp. 262-268
    • Ellis, J.A.1    Yates, J.R.W.2    Kendrick-Jones, J.3    Brown, C.A.4
  • 18
    • 0033083786 scopus 로고    scopus 로고
    • Distinct regions specify the nuclear membrane targeting of emerin, the responsible protein for Emery-Dreifuss muscular dystrophy
    • Tsuchiya, Y., Hase, A., Ogawa, M., Yorifuji, H. & Arahata, K. (1999) Distinct regions specify the nuclear membrane targeting of emerin, the responsible protein for Emery-Dreifuss muscular dystrophy. Eur. J. Biochem. 259, 859-865.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 859-865
    • Tsuchiya, Y.1    Hase, A.2    Ogawa, M.3    Yorifuji, H.4    Arahata, K.5
  • 19
  • 20
    • 0035850713 scopus 로고    scopus 로고
    • How does a g993t mutation in the emerin gene cause Emery-Dreifuss muscular dystrophy?
    • Holt, I., Clements, L., Manilal, S. & Morris, G.E. (2001) How does a g993t mutation in the emerin gene cause Emery-Dreifuss muscular dystrophy? Biochem. Biophys. Res. Commun. 287, 1129-1133.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 1129-1133
    • Holt, I.1    Clements, L.2    Manilal, S.3    Morris, G.E.4
  • 24
    • 0031882856 scopus 로고    scopus 로고
    • Cloning a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation
    • Imai, Y., Matsuo, N., Ogawa, S., Tohyama, M. & Takagi, T. (1998) Cloning a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation. Mol. Brain Res. 53, 33-40.
    • (1998) Mol. Brain Res. , vol.53 , pp. 33-40
    • Imai, Y.1    Matsuo, N.2    Ogawa, S.3    Tohyama, M.4    Takagi, T.5
  • 26
    • 0035084090 scopus 로고    scopus 로고
    • The R482Q lamin A/C mutation that causes lipodystrophy does not prevent nuclear targeting of lamin A in adipocytes or its interaction with emerin
    • Holt, I., Clements, L., Manilal, S., Brown, S.C. & Morris, G.E. (2001) The R482Q lamin A/C mutation that causes lipodystrophy does not prevent nuclear targeting of lamin A in adipocytes or its interaction with emerin. Eur. J. Hum. Genet. 9, 204-208.
    • (2001) Eur. J. Hum. Genet. , vol.9 , pp. 204-208
    • Holt, I.1    Clements, L.2    Manilal, S.3    Brown, S.C.4    Morris, G.E.5
  • 27
    • 0342505309 scopus 로고    scopus 로고
    • DNA binding domains in diverse nuclear receptors function as nuclear export signals
    • Black, B.E., Levesque, L., Holaska, J.M., Wood, T.C. & Paschal, B.M. (1999) DNA binding domains in diverse nuclear receptors function as nuclear export signals. Mol. Cell Biol. 19, 8616-8624.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8616-8624
    • Black, B.E.1    Levesque, L.2    Holaska, J.M.3    Wood, T.C.4    Paschal, B.M.5
  • 28
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • Holaska, J.M., Lee, K.K., Kowalski, A.K. & Wilson, K.L. (2003) Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J. Biol. Chem. 278, 6969-6975.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6969-6975
    • Holaska, J.M.1    Lee, K.K.2    Kowalski, A.K.3    Wilson, K.L.4
  • 31
    • 0035292694 scopus 로고    scopus 로고
    • Lipoprotein lipase: Physiology, biochemistry, and molecular biology
    • Goldberg, I.J. & Merkel, M. (2001) Lipoprotein lipase: physiology, biochemistry, and molecular biology. Frontiers Biosci. 6, 388-405.
    • (2001) Frontiers Biosci. , vol.6 , pp. 388-405
    • Goldberg, I.J.1    Merkel, M.2
  • 33
    • 0038931747 scopus 로고    scopus 로고
    • Coupling of signal transduction to alternative pre-mRNA splicing by a composite splice regulator
    • König, H., Ponta, H. & Herrlich, P. (1998) Coupling of signal transduction to alternative pre-mRNA splicing by a composite splice regulator. EMBO J. 17, 2904-2913.
    • (1998) EMBO J. , vol.17 , pp. 2904-2913
    • König, H.1    Ponta, H.2    Herrlich, P.3
  • 35
    • 0036729874 scopus 로고    scopus 로고
    • Myotonic dystrophy: Clinical and molecular parallels between myotonic dystrophy type 1 and type 2
    • Ranum, L.P. & Day, J.W. (2002) Myotonic dystrophy: clinical and molecular parallels between myotonic dystrophy type 1 and type 2. Curr. Neurol. Neurosci. Report 2, 465-470.
    • (2002) Curr. Neurol. Neurosci. Report , vol.2 , pp. 465-470
    • Ranum, L.P.1    Day, J.W.2
  • 36
    • 0036347927 scopus 로고    scopus 로고
    • Loss of the muscle-specific chloride channel in type 1 myotonic dystrophy due to misregulated alternative splicing
    • Charlet, B.N., Savkur, R.S., Singh, G., Philips, A.V., Grice, E.A. & Cooper, T.A. (2002) Loss of the muscle-specific chloride channel in type 1 myotonic dystrophy due to misregulated alternative splicing. Mol Cell. 10, 45-53.
    • (2002) Mol. Cell. , vol.10 , pp. 45-53
    • Charlet, B.N.1    Savkur, R.S.2    Singh, G.3    Philips, A.V.4    Grice, E.A.5    Cooper, T.A.6
  • 37
    • 0036347525 scopus 로고    scopus 로고
    • Expanded CUG repeats trigger aberrant splicing of C1C-1 chloride channel pre-mRNA and hyperexcitability of skeletal muscle in myotonic dystrophy
    • Mankodi, A., Takahashi, M.P., Jiang, H., Beck, C.L., Bowers, W.J., Moxley, R.T., Cannon, S.C. & Thornton, C.A. (2002) Expanded CUG repeats trigger aberrant splicing of C1C-1 chloride channel pre-mRNA and hyperexcitability of skeletal muscle in myotonic dystrophy. Mol. Cell. 10, 35-44.
    • (2002) Mol. Cell. , vol.10 , pp. 35-44
    • Mankodi, A.1    Takahashi, M.P.2    Jiang, H.3    Beck, C.L.4    Bowers, W.J.5    Moxley, R.T.6    Cannon, S.C.7    Thornton, C.A.8
  • 38
    • 0034873099 scopus 로고    scopus 로고
    • Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy
    • Savkur, R.S., Philips, A.V. & Cooper, T.A. (2001) Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy. Nature Genet. 29, 40-47.
    • (2001) Nature Genet. , vol.29 , pp. 40-47
    • Savkur, R.S.1    Philips, A.V.2    Cooper, T.A.3
  • 39
    • 0032076126 scopus 로고    scopus 로고
    • Disruption of splicing regulated by a CUG-binding protein in myotonic dystrophy
    • Philips, A.V., Timchenko, L.T. & Cooper, T.A. (1998) Disruption of splicing regulated by a CUG-binding protein in myotonic dystrophy. Science 280, 737-741.
    • (1998) Science , vol.280 , pp. 737-741
    • Philips, A.V.1    Timchenko, L.T.2    Cooper, T.A.3
  • 40
    • 0036927671 scopus 로고    scopus 로고
    • Defects in pre-mRNA processing as causes of and predisposition to diseases
    • Stoilov, P., Meshorer, E., Gencheva, M., Glick, D., Soreq, H. & Stamm, S. (2002) Defects in pre-mRNA processing as causes of and predisposition to diseases. DNA Cell Biol. 21, 803-818.
    • (2002) DNA Cell Biol. , vol.21 , pp. 803-818
    • Stoilov, P.1    Meshorer, E.2    Gencheva, M.3    Glick, D.4    Soreq, H.5    Stamm, S.6
  • 41
    • 0036537888 scopus 로고    scopus 로고
    • A novel interaction between lamin A and SREBP1: Implications for partial lipodystrophy and other laminopathies
    • Lloyd, D.J., Trembath, R.C. & Shackleton, S. (2002) A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies. Hum. Mol. Genet. 11, 769-777.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 769-777
    • Lloyd, D.J.1    Trembath, R.C.2    Shackleton, S.3
  • 42
    • 1842854443 scopus 로고    scopus 로고
    • Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein
    • Markiewicz, E., Dechat, T., Foisner, R., Quinlan, R.A. & Hutchison, C.J. (2002) Lamin A/C Binding Protein LAP2alpha Is Required for Nuclear Anchorage of Retinoblastoma Protein. Mol. Biol. Cell. 13, 4401-4413.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 4401-4413
    • Markiewicz, E.1    Dechat, T.2    Foisner, R.3    Quinlan, R.A.4    Hutchison, C.J.5
  • 43
    • 0002653508 scopus 로고    scopus 로고
    • The reverse two-hybrid system
    • Bartel, P. & Fields, S., eds. Oxford University Press, New York
    • Vidal, M. (1997) The reverse two-hybrid system. In The Two-Hybrid System. (Bartel, P. & Fields, S., eds), p. 109. Oxford University Press, New York.
    • (1997) The Two-Hybrid System , pp. 109
    • Vidal, M.1
  • 44
    • 0029894254 scopus 로고    scopus 로고
    • RBF, a novel RE-related gene that regulates E2F activity and interacts with cyclin E in Drosophila
    • Du, W., Vidal, M., Xie, J.E. & Dyson, N. (1996) RBF, a novel RE-related gene that regulates E2F activity and interacts with cyclin E in Drosophila. Genes Dev. 10, 1206-1218.
    • (1996) Genes Dev. , vol.10 , pp. 1206-1218
    • Du, W.1    Vidal, M.2    Xie, J.E.3    Dyson, N.4
  • 45
    • 0026639625 scopus 로고
    • Protein interaction cloning in yeast-identification of mammalian proteins that react with the leucine zipper of jun
    • Chevray, P.M. & Nathans, D. (1992) Protein interaction cloning in yeast-identification of mammalian proteins that react with the leucine zipper of jun. Proc. Natl. Acad. Sci. USA 89, 5789-5793.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5789-5793
    • Chevray, P.M.1    Nathans, D.2


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