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Volumn 271, Issue 5, 2004, Pages 1035-1045

Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy

Author keywords

Apoptosis; Emerin; Emery Dreifuss muscular dystrophy; Lamin A; MAN1

Indexed keywords

ALANINE; ANTIBODY; EMERIN; FAS ANTIBODY; LAMIN A; MEMBRANE PROTEIN; MUTANT PROTEIN; PROTEIN SUBUNIT; REPRESSOR PROTEIN;

EID: 1542284570     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04007.x     Document Type: Article
Times cited : (122)

References (45)
  • 1
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
    • Bione, S., Maestrini, E., Rivella, S., Mancini, M., Regis, S., Romeo, G. & Toniolo, D. (1994) Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Nat. Genet. 8, 323-327.
    • (1994) Nat. Genet. , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 2
    • 0024419522 scopus 로고
    • Emery-Dreifuss syndrome
    • Emery, A.E.H. (1989) Emery-Dreifuss syndrome. J. Med. Genet. 26, 637-641.
    • (1989) J. Med. Genet. , vol.26 , pp. 637-641
    • Emery, A.E.H.1
  • 3
    • 0034213873 scopus 로고    scopus 로고
    • Emery-Dreifuss muscular dystrophy - A 40 year retrospective
    • Emery, A.E.H. (2000) Emery-Dreifuss muscular dystrophy - a 40 year retrospective. Neuromuscul. Disord. 10, 228-232.
    • (2000) Neuromuscul. Disord. , vol.10 , pp. 228-232
    • Emery, A.E.H.1
  • 5
    • 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
  • 7
    • 0036178210 scopus 로고    scopus 로고
    • Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse
    • Erratum appears in Am. J. Hum. Genet. 70, 1075
    • De Sandre-Giovannoli, A., Chaouch, M., Kozlov, S., Vallat, J.M., Tazir, M., Kassouri, N., Szepetowski, P., Hammadouche, T., Vandenberghe, A., Stewart, C.L. et al. (2002) Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse. Am. J. Hum. Genet. 70, 726-736. [Erratum appears in Am. J. Hum. Genet. 70, 1075.].
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 726-736
    • De Sandre-Giovannoli, A.1    Chaouch, M.2    Kozlov, S.3    Vallat, J.M.4    Tazir, M.5    Kassouri, N.6    Szepetowski, P.7    Hammadouche, T.8    Vandenberghe, A.9    Stewart, C.L.10
  • 9
    • 0035831041 scopus 로고    scopus 로고
    • Nuclear lamins and disease: Insights into nuclear infrastructure
    • Wilson, K.L., Zastrow, M. & Lee, K.K. (2001) Nuclear lamins and disease: insights into nuclear infrastructure. Cell 104, 647-650.
    • (2001) Cell , vol.104 , pp. 647-650
    • Wilson, K.L.1    Zastrow, M.2    Lee, K.K.3
  • 10
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: The nuclear envelope and human disease
    • Burke, B. & Stewart, C.L. (2002) Life at the edge: the nuclear envelope and human disease. Nat. Rev. Mol. Cell Biol. 3, 575-585.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 575-585
    • Burke, B.1    Stewart, C.L.2
  • 15
    • 0034176682 scopus 로고    scopus 로고
    • The nuclear envelope, muscular dystrophy and gene expression
    • Wilson, K.L. (2000) The nuclear envelope, muscular dystrophy and gene expression. Trends Cell Biol. 10, 125-129.
    • (2000) Trends Cell Biol. , vol.10 , pp. 125-129
    • Wilson, K.L.1
  • 16
    • 0033786789 scopus 로고    scopus 로고
    • Nuclear envelope proteins and associated diseases
    • Nagano, A. & Arahata, K. (2000) Nuclear envelope proteins and associated diseases. Curr. Opinion Neurol. 13, 533-539.
    • (2000) Curr. Opinion Neurol. , vol.13 , pp. 533-539
    • Nagano, A.1    Arahata, K.2
  • 17
    • 0035146907 scopus 로고    scopus 로고
    • Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina
    • Cohen, M., Lee, K.K., Wilson, K.L. & Gruenbaum, Y. (2001) Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina. Trends Bioch. Sci. 26, 41-47.
    • (2001) Trends Bioch. Sci. , vol.26 , pp. 41-47
    • Cohen, M.1    Lee, K.K.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 18
    • 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, 801-808.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 801-808
    • Manilal, S.1    Nguyen, T.M.2    Sewry, C.A.3    Morris, G.E.4
  • 20
    • 0031215452 scopus 로고    scopus 로고
    • Emerin, deficiency of which causes Emery-Dreifuss muscular dystrophy, is localized at the inner nuclear membrane
    • Yorifuji, H., Tadano, Y., Tsuchiya, Y., Ogawa, M., Goto, K., Umetani, A., Asaka, Y. & Arahata, K. (1997) Emerin, deficiency of which causes Emery-Dreifuss muscular dystrophy, is localized at the inner nuclear membrane. Neurogenetics 1, 135-140.
    • (1997) Neurogenetics , vol.1 , pp. 135-140
    • Yorifuji, H.1    Tadano, Y.2    Tsuchiya, Y.3    Ogawa, M.4    Goto, K.5    Umetani, A.6    Asaka, Y.7    Arahata, K.8
  • 21
    • 0031969698 scopus 로고    scopus 로고
    • Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype
    • Ellis, J.A., Craxton, M., Yates, J.R. & Kendrick-Jones, J. (1998) Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype. J. Cell Sci. 111, 781-792.
    • (1998) J. Cell Sci. , vol.111 , pp. 781-792
    • Ellis, J.A.1    Craxton, M.2    Yates, J.R.3    Kendrick-Jones, J.4
  • 22
    • 0032852110 scopus 로고    scopus 로고
    • Heart to heart: From nuclear proteins to Emery-Dreifuss muscular dystrophy
    • Morris, G.E. & Manilal, S. (1999) Heart to heart: from nuclear proteins to Emery-Dreifuss muscular dystrophy. Hum. Mol. Genet. 8, 1847-1851.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1847-1851
    • Morris, G.E.1    Manilal, S.2
  • 23
    • 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
  • 26
    • 0035794643 scopus 로고    scopus 로고
    • LAP2 binds to BAF-DNA complexes: Requirement for the LEM-domain and modulation by variable regions
    • Shumaker, D.K., Lee, K.K., Tanhehco, Y.C., Craigie, R. & Wilson, K.L. (2001) LAP2 binds to BAF-DNA complexes: requirement for the LEM-domain and modulation by variable regions. EMBO J. 20, 1754-1764.
    • (2001) EMBO J. , vol.20 , pp. 1754-1764
    • Shumaker, D.K.1    Lee, K.K.2    Tanhehco, Y.C.3    Craigie, R.4    Wilson, K.L.5
  • 27
    • 0036330001 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor: Major roles in chromatin decondensation and nuclear assembly
    • Segura-Totten, M., Kowalski, A.K., Craigie, R. & Wilson, K.L. (2002) Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. J. Cell Biol. 158, 475-485.
    • (2002) J. Cell Biol. , vol.158 , pp. 475-485
    • Segura-Totten, M.1    Kowalski, A.K.2    Craigie, R.3    Wilson, K.L.4
  • 28
    • 0033008195 scopus 로고    scopus 로고
    • Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2 related proteins
    • Kasof, G.M., Goyal, L. & White, E. (1999) Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2 related proteins. Mol. Cell Biol. 19, 4390-4404.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4390-4404
    • Kasof, G.M.1    Goyal, L.2    White, E.3
  • 29
    • 0030605415 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1
    • Nagase, T., Seki, N., Ishikawa, K., Tanaka, A. & Nomura, N. (1996) Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 3, 17-24.
    • (1996) DNA Res. , vol.3 , pp. 17-24
    • Nagase, T.1    Seki, N.2    Ishikawa, K.3    Tanaka, A.4    Nomura, N.5
  • 30
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and BAF compete for binding to emerin
    • Holaska, J.M., Lee, K.K., Kowalski, A.K. & Wilson, K.L. (2003) Transcriptional repressor germ cell-less (GCL) and BAF compete for binding to emerin. 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
  • 32
    • 0026734350 scopus 로고
    • Two different protein kinases act on a different time schedule as glial filament kinases during mitosis
    • Matsuoka, Y., Nishizawa, K., Yano, T., Shibata, M., Ando, S., Takahashi, T. & Inagaki, M. (1992) Two different protein kinases act on a different time schedule as glial filament kinases during mitosis. EMBO J. 11, 2895-2902.
    • (1992) EMBO J. , vol.11 , pp. 2895-2902
    • Matsuoka, Y.1    Nishizawa, K.2    Yano, T.3    Shibata, M.4    Ando, S.5    Takahashi, T.6    Inagaki, M.7
  • 35
    • 0024596722 scopus 로고
    • A cell-killing monoclonal antibody (anti-Fas) to a cell surface antigen co-downregulated with the receptor of tumor necrosis factor
    • Yonehara, S., Ishii, A. & Yonehara, M. (1989) A cell-killing monoclonal antibody (anti-Fas) to a cell surface antigen co-downregulated with the receptor of tumor necrosis factor. J. Exp. Med. 169, 1747-1756.
    • (1989) J. Exp. Med. , vol.169 , pp. 1747-1756
    • Yonehara, S.1    Ishii, A.2    Yonehara, M.3
  • 36
    • 1542382269 scopus 로고    scopus 로고
    • Multiple and surprising new functions for emerin, a nuclear membrane protein
    • in press
    • Bengtsson, L. & Wilson, K.L. (2004) Multiple and surprising new functions for emerin, a nuclear membrane protein. Curr. Opin. Cell Biol. in press.
    • (2004) Curr. Opin. Cell Biol.
    • Bengtsson, L.1    Wilson, K.L.2
  • 38
    • 0037446880 scopus 로고    scopus 로고
    • MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans
    • Liu, J., Lee, K.K., Segura-Totten, M., Neufeld, E., Wilson, K.L. & Gruenbaum, Y. (2003) MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans. Proc. Natl Acad. Sci. USA 100, 4598-4603.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4598-4603
    • Liu, J.1    Lee, K.K.2    Segura-Totten, M.3    Neufeld, E.4    Wilson, K.L.5    Gruenbaum, Y.6
  • 39
    • 18644386771 scopus 로고    scopus 로고
    • Barrier to autointegration factor interacts with the cone-rod homeobox and represses its transactivation function
    • Wang, X., Xu, S., Rivolta, C., Li, L.Y., Peng, G.H., Swain, P.K., Sung, C.H., Swaroop, A., Berson, E.L., Dryja, T.P. et al. (2002) Barrier to autointegration factor interacts with the cone-rod homeobox and represses its transactivation function. J. Biol. Chem. 277, 43288-43300.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43288-43300
    • Wang, X.1    Xu, S.2    Rivolta, C.3    Li, L.Y.4    Peng, G.H.5    Swain, P.K.6    Sung, C.H.7    Swaroop, A.8    Berson, E.L.9    Dryja, T.P.10
  • 40
    • 0033584403 scopus 로고    scopus 로고
    • Molecular cloning and genomic organization of mouse homologue of Drosophila germ cell-less and its expression in germ lineage cells
    • Kimura, T., Yomogida, K., Iwai, N., Kato, Y. & Nakano, T. (1999) Molecular cloning and genomic organization of mouse homologue of Drosophila germ cell-less and its expression in germ lineage cells. Biochem. Biophys. Res. Commun. 262, 223-230.
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 223-230
    • Kimura, T.1    Yomogida, K.2    Iwai, N.3    Kato, Y.4    Nakano, T.5
  • 41
    • 0033571029 scopus 로고    scopus 로고
    • Germ cell-less is required only during the establishment of the germ cell lineage of Drosophila and has activities which are dependent and independent of its localization to the nuclear envelope
    • Robertson, S.E., Dockendorff, T.C., Leatherman, J.L., Faulkner, D.L. & Jongens, T.A. (1999) Germ cell-less is required only during the establishment of the germ cell lineage of Drosophila and has activities which are dependent and independent of its localization to the nuclear envelope. Dev. Biol. 215, 288-297.
    • (1999) Dev. Biol. , vol.215 , pp. 288-297
    • Robertson, S.E.1    Dockendorff, T.C.2    Leatherman, J.L.3    Faulkner, D.L.4    Jongens, T.A.5
  • 42
    • 0033105821 scopus 로고    scopus 로고
    • Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators
    • Ito, M., Yuan, C.-X., Malik, S., Gu, W., Fondell, J.D., Yamamura, S., Fu, Z.-Y., Zhang, X., Qin, J. & Roeder, R.G. (1999) Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators. Mol. Cell 3, 361-370.
    • (1999) Mol. Cell , vol.3 , pp. 361-370
    • Ito, M.1    Yuan, C.-X.2    Malik, S.3    Gu, W.4    Fondell, J.D.5    Yamamura, S.6    Fu, Z.-Y.7    Zhang, X.8    Qin, J.9    Roeder, R.G.10
  • 43
    • 0036155776 scopus 로고    scopus 로고
    • Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C
    • Mislow, J.M., Kim, M.S., Davis, D.B. & McNally, E.M. (2002a) Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C. J. Cell Sci. 115, 61-70.
    • (2002) J. Cell Sci. , vol.115 , pp. 61-70
    • Mislow, J.M.1    Kim, M.S.2    Davis, D.B.3    McNally, E.M.4
  • 45
    • 0030218143 scopus 로고    scopus 로고
    • The SR protein family: Pleiotropic functions in pre-mRNA splicing
    • Valcarcel, J. & Green, M.R. (1996) The SR protein family: pleiotropic functions in pre-mRNA splicing. Trends. Biochem. Sci. 21, 296-301.
    • (1996) Trends. Biochem. Sci. , vol.21 , pp. 296-301
    • Valcarcel, J.1    Green, M.R.2


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