메뉴 건너뛰기




Volumn 15, Issue 4, 2005, Pages 277-293

Linkage of lamins to fidelity of gene transcription

Author keywords

Chromatin remodeling; Emery Dreifuss muscular dystrophy; Gene transcription; Lamin A C; Laminopathies; Pre lamin A

Indexed keywords

DNA BINDING PROTEIN; ENVELOPE PROTEIN; LAMIN; LAMIN A; LAMIN C; PROTEIN PRECURSOR; TRANSCRIPTION FACTOR;

EID: 33645451179     PISSN: 10454403     EISSN: None     Source Type: Journal    
DOI: 10.1615/critreveukargeneexpr.v15.i4.10     Document Type: Review
Times cited : (10)

References (148)
  • 2
    • 0035316574 scopus 로고    scopus 로고
    • Chromosome territories, nuclear architecture and gene regulation in mammalian cells
    • Cremer T, Cremer C. Chromosome territories, nuclear architecture and gene regulation in mammalian cells. Nat Rev Genet. 2001;2:292-301.
    • (2001) Nat Rev Genet , vol.2 , pp. 292-301
    • Cremer, T.1    Cremer, C.2
  • 3
    • 9444241024 scopus 로고    scopus 로고
    • Positioning the genome within the nucleus
    • Verschure PJ. Positioning the genome within the nucleus. Biol Cell. 2004;96:569-77.
    • (2004) Biol Cell , vol.96 , pp. 569-577
    • Verschure, P.J.1
  • 9
    • 0037464584 scopus 로고    scopus 로고
    • DNA triplet repeats mediate heterochromatin-protein-1-sensitive variegated gene silencing
    • Saveliev A, Everett C, Sharpe T, Webster Z, Festenstein R. DNA triplet repeats mediate heterochromatin-protein-1-sensitive variegated gene silencing. Nature. 2003;422:909-13.
    • (2003) Nature , vol.422 , pp. 909-913
    • Saveliev, A.1    Everett, C.2    Sharpe, T.3    Webster, Z.4    Festenstein, R.5
  • 10
    • 0034902187 scopus 로고    scopus 로고
    • Nucleosome mobilization and positioning by IDWI-containing chromatin-remodeling factors
    • Langst G, Becker PB. Nucleosome mobilization and positioning by IDWI-containing chromatin-remodeling factors. J Cell Sci. 2001;114:2561-8.
    • (2001) J Cell Sci , vol.114 , pp. 2561-2568
    • Langst, G.1    Becker, P.B.2
  • 13
    • 2342517250 scopus 로고    scopus 로고
    • Regulation of heterochromatin by histone methylation and small RNAs
    • Grewal SIS, Rice JC. Regulation of heterochromatin by histone methylation and small RNAs. Curr Opin Cell Biol. 2004;16:230-8.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 230-238
    • Grewal, S.I.S.1    Rice, J.C.2
  • 14
    • 5444263735 scopus 로고    scopus 로고
    • Epigenetic aspects of differentiation
    • Arney KL, Fisher AG. Epigenetic aspects of differentiation. J Cell Sci. 2004;117:4355-63.
    • (2004) J Cell Sci , vol.117 , pp. 4355-4363
    • Arney, K.L.1    Fisher, A.G.2
  • 15
    • 0142058200 scopus 로고    scopus 로고
    • The spatial organization of centromeric heterochromatin during normal human lymphopoiesis: Evidence for ontogenically determined spatial patterns
    • Alcobia I, Quina AS, Neves H, Clode N, Parreira L. The spatial organization of centromeric heterochromatin during normal human lymphopoiesis: evidence for ontogenically determined spatial patterns. Exp Cell Res. 2003;290:358-69.
    • (2003) Exp Cell Res , vol.290 , pp. 358-369
    • Alcobia, I.1    Quina, A.S.2    Neves, H.3    Clode, N.4    Parreira, L.5
  • 17
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: The nuclear envelope and human disease
    • Burke B, Stewart CL. Life at the edge: the nuclear envelope and human disease. Nat Rev Mol Cell Biol. 2002;3:575-85.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 575-585
    • Burke, B.1    Stewart, C.L.2
  • 18
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R, Gerace L. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell. 1993;73:1267-79.
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 19
  • 21
    • 0035881480 scopus 로고    scopus 로고
    • Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: One binds BAF and the other binds DNA
    • Cai M, Huang Y, Ghirlando R, Wilson KL, Craige R, Clore GM. Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. EMBO J. 2001;20:4399-407.
    • (2001) EMBO J , vol.20 , pp. 4399-4407
    • Cai, M.1    Huang, Y.2    Ghirlando, R.3    Wilson, K.L.4    Craige, R.5    Clore, G.M.6
  • 22
    • 0035794643 scopus 로고    scopus 로고
    • LAP2 binds to BAF-DNA complexes: Requirement for the LEM domain and modulation by variable regions
    • Shumaker DK, Lee KK, Tanhehco YC, Craigie R, Wilson KL. LAP2 binds to BAF-DNA complexes: requirement for the LEM domain and modulation by variable regions. EMBO J. 2001;20:1754-64.
    • (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
  • 23
    • 0037455537 scopus 로고    scopus 로고
    • HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication
    • Martins S, Eikvar S, Furukawa K, Collas P. HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication. J Cell Biol. 2003;160 :177-88.
    • (2003) J Cell Biol , vol.160 , pp. 177-188
    • Martins, S.1    Eikvar, S.2    Furukawa, K.3    Collas, P.4
  • 24
    • 0030987777 scopus 로고    scopus 로고
    • Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR
    • Ye Q, Callebaut I, Pezhman A, Courvalin JC, Worman HJ. Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. J Biol Chem. 1997;272:14983-9.
    • (1997) J Biol Chem , vol.272 , pp. 14983-14989
    • Ye, Q.1    Callebaut, I.2    Pezhman, A.3    Courvalin, J.C.4    Worman, H.J.5
  • 28
    • 0029869424 scopus 로고    scopus 로고
    • The nuclear pore complex and lamina: Three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy
    • Goldberg MW, Allen TD. The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy. J Mol Biol. 1996;257:848-65.
    • (1996) J Mol Biol , vol.257 , pp. 848-865
    • Goldberg, M.W.1    Allen, T.D.2
  • 29
    • 0034638842 scopus 로고    scopus 로고
    • Nuclear lamins A and B1. Different pathways of assembly during nuclear envelope formation in living cells
    • Moir RD, Yoon M, Khuon S, Goldman RD. Nuclear lamins A and B1. Different pathways of assembly during nuclear envelope formation in living cells. J Cell Biol. 2000;151:1155-68.
    • (2000) J Cell Biol , vol.151 , pp. 1155-1168
    • Moir, R.D.1    Yoon, M.2    Khuon, S.3    Goldman, R.D.4
  • 30
    • 0024561417 scopus 로고
    • Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: A developmental study
    • Rober RA, Weber K, Osborn M. Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: a developmental study. Development. 1989;105:365-78.
    • (1989) Development , vol.105 , pp. 365-378
    • Rober, R.A.1    Weber, K.2    Osborn, M.3
  • 31
    • 0034490814 scopus 로고    scopus 로고
    • Association of prenylated proteins with the plasma membrane and the inner nuclear membrane is mediated by the same membrane-targeting motifs
    • Hofmeister H, Weber K, Stick R. Association of prenylated proteins with the plasma membrane and the inner nuclear membrane is mediated by the same membrane-targeting motifs. Mol Biol Cell. 2000;11:3233-46.
    • (2000) Mol Biol Cell , vol.11 , pp. 3233-3246
    • Hofmeister, H.1    Weber, K.2    Stick, R.3
  • 32
    • 0024828257 scopus 로고
    • Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina
    • Weber K, Plessmann U, Traub P. Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina. FEBS Lett. 1989;257:411-4.
    • (1989) FEBS Lett , vol.257 , pp. 411-414
    • Weber, K.1    Plessmann, U.2    Traub, P.3
  • 34
    • 16344392142 scopus 로고    scopus 로고
    • Laminopathies: Involvement of structural nuclear proteins in the pathogenesis of an increasing number of human diseases
    • Maraldi NM, Squarzoni S, Sabatelli P, Capanni C, Mattioli E, Ognibene A, Lattanzi G. Laminopathies: involvement of structural nuclear proteins in the pathogenesis of an increasing number of human diseases. J Cell Physiol. 2005;203:319-27.
    • (2005) J Cell Physiol , vol.203 , pp. 319-327
    • Maraldi, N.M.1    Squarzoni, S.2    Sabatelli, P.3    Capanni, C.4    Mattioli, E.5    Ognibene, A.6    Lattanzi, G.7
  • 37
    • 0033749567 scopus 로고    scopus 로고
    • Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes
    • Liu J, Ben-Shahar TR, Riemer D, Treinin M, Spann P, Weber K, Fire A, Gruenbaum Y. Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes. Mol Biol Cell. 2000;11:3937-47.
    • (2000) Mol Biol Cell , vol.11 , pp. 3937-3947
    • Liu, J.1    Ben-Shahar, T.R.2    Riemer, D.3    Treinin, M.4    Spann, P.5    Weber, K.6    Fire, A.7    Gruenbaum, Y.8
  • 38
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozak P, Sasseville AM, Raymond Y, Cook PR. Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J Cell Sci. 1995;108:635-44.
    • (1995) J Cell Sci , vol.108 , pp. 635-644
    • Hozak, P.1    Sasseville, A.M.2    Raymond, Y.3    Cook, P.R.4
  • 39
    • 0037049554 scopus 로고    scopus 로고
    • Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription
    • Kumaran RI, Muralikrishna B, Parnaik VK. Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription. J Cell Biol. 2002;159:783-93.
    • (2002) J Cell Biol , vol.159 , pp. 783-793
    • Kumaran, R.I.1    Muralikrishna, B.2    Parnaik, V.K.3
  • 40
    • 16344380741 scopus 로고    scopus 로고
    • Sequestration of pRb by ciclin D3 causes intranuclear reorganization of lamin A/C during muscle cell differentiation
    • Mariappan I, Parnaik VK. Sequestration of pRb by ciclin D3 causes intranuclear reorganization of lamin A/C during muscle cell differentiation. Mol Biol Cell. 2005;16:1948-60.
    • (2005) Mol Biol Cell , vol.16 , pp. 1948-1960
    • Mariappan, I.1    Parnaik, V.K.2
  • 41
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: Integrating isolated clues
    • Zastrow MS, Vlcek S, Wilson KL. Proteins that bind A-type lamins: integrating isolated clues. J Cell Sci. 2004;117:979-87.
    • (2004) J Cell Sci , vol.117 , pp. 979-987
    • Zastrow, M.S.1    Vlcek, S.2    Wilson, K.L.3
  • 42
    • 0037439661 scopus 로고    scopus 로고
    • ANChors away: An actin based mechanism of nuclear positioning
    • Starr DA, Han M. ANChors away: an actin based mechanism of nuclear positioning. J Cell Sci. 2003;116:211-6.
    • (2003) J Cell Sci , vol.116 , pp. 211-216
    • Starr, D.A.1    Han, M.2
  • 43
    • 0035972145 scopus 로고    scopus 로고
    • Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization
    • Schimer EC, Guan T, Gerace L. Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization. J Cell Biol. 2001;153:479-90.
    • (2001) J Cell Biol , vol.153 , pp. 479-490
    • Schimer, E.C.1    Guan, T.2    Gerace, L.3
  • 44
    • 0037446880 scopus 로고    scopus 로고
    • MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorabditis elegans
    • U S A
    • Liu J, Lee KK, Segura-Totten M, Neufeld E, Wilson KL, Gruenbaum Y. MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorabditis elegans. Proc Natl Acad Sci U S A. 2003;100:4598-603.
    • (2003) Proc Natl Acad Sci , 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
  • 46
    • 0035694237 scopus 로고    scopus 로고
    • Identification of essential genes in cultured mammalian cells using small interfering RNAs
    • Harborth J, Elbashir SM, Bechert K, Tuschl T, Weber K. Identification of essential genes in cultured mammalian cells using small interfering RNAs. J Cell Sci. 2001;114:4557-65.
    • (2001) J Cell Sci , vol.114 , pp. 4557-4565
    • Harborth, J.1    Elbashir, S.M.2    Bechert, K.3    Tuschl, T.4    Weber, K.5
  • 47
    • 0030681031 scopus 로고    scopus 로고
    • Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression
    • Imai S, Nishibayashi S, Takao K, Tomifuji M, Fujino T, Hasegawa M, Takano T. Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression. Mol Biol Cell. 1997;8:2407-19.
    • (1997) Mol Biol Cell , vol.8 , pp. 2407-2419
    • Imai, S.1    Nishibayashi, S.2    Takao, K.3    Tomifuji, M.4    Fujino, T.5    Hasegawa, M.6    Takano, T.7
  • 48
    • 0033939554 scopus 로고    scopus 로고
    • Review: The dynamics of the nuclear lamins during the cell cycle. Relationship between structure and function
    • Moir RD, Spann TP, Lopez-Soler RI, Yoon M, Goldman AE, Khuo S, Goldberg RD. Review: the dynamics of the nuclear lamins during the cell cycle. Relationship between structure and function. J Struct Biol. 2000;129:324-34.
    • (2000) J Struct Biol , vol.129 , pp. 324-334
    • Moir, R.D.1    Spann, T.P.2    Lopez-Soler, R.I.3    Yoon, M.4    Goldman, A.E.5    Khuo, S.6    Goldberg, R.D.7
  • 49
    • 0035972254 scopus 로고    scopus 로고
    • Mistargeting of B-type lamins at the end of mitosis: Implications on cell survival and regulation of lamins A/C expression
    • Steen RL, Collas P. Mistargeting of B-type lamins at the end of mitosis: implications on cell survival and regulation of lamins A/C expression. J Cell Biol. 2001;153:621-6.
    • (2001) J Cell Biol , vol.153 , pp. 621-626
    • Steen, R.L.1    Collas, P.2
  • 50
    • 0036848357 scopus 로고    scopus 로고
    • In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C
    • Dreuillet C, Tillit J, Kress M, Ernoult-Lange M. In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C. Nucleic Acids Res. 2002;30:4634-42.
    • (2002) Nucleic Acids Res , vol.30 , pp. 4634-4642
    • Dreuillet, C.1    Tillit, J.2    Kress, M.3    Ernoult-Lange, M.4
  • 51
    • 0035146907 scopus 로고    scopus 로고
    • Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina
    • Cohen M, Lee KK, Wilson KL, Gruenbaum Y. Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina. Trends Biochem Sci. 2001;26:41-7.
    • (2001) Trends Biochem Sci , vol.26 , pp. 41-47
    • Cohen, M.1    Lee, K.K.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 52
    • 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 RA, Hutchison CJ. Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein. Mol Biol Cell. 2002;13:4401-13.
    • (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
  • 53
    • 14044265165 scopus 로고    scopus 로고
    • Remodelling of the nuclear lamina and nucleoskeleton is required for skeletal muscle differentiation in vitro
    • Markiewicz E, Ledran M, Hutchison CJ. Remodelling of the nuclear lamina and nucleoskeleton is required for skeletal muscle differentiation in vitro. J Cell Sci. 2005;118:409-20.
    • (2005) J Cell Sci , vol.118 , pp. 409-420
    • Markiewicz, E.1    Ledran, M.2    Hutchison, C.J.3
  • 54
    • 3042829496 scopus 로고    scopus 로고
    • A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteosomal degradation
    • U S A
    • Johnson BR, Nitta RT, Froch RL, Mounkes L, Barbie DA, Stewart CL, Harlow E, Kennedy BK. A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteosomal degradation. Proc Natl Acad Sci U S A. 2004;101:9677-82.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 9677-9682
    • Johnson, B.R.1    Nitta, R.T.2    Froch, R.L.3    Mounkes, L.4    Barbie, D.A.5    Stewart, C.L.6    Harlow, E.7    Kennedy, B.K.8
  • 55
    • 0842347426 scopus 로고    scopus 로고
    • Expression of a mutant lamin A that causes Emery-Dreyfuss muscular dystrophy inhibits in vitro differentiation of C2C12 myoblasts
    • Favreau C, Higuet D, Courvalin JC, Buendia B. Expression of a mutant lamin A that causes Emery-Dreyfuss muscular dystrophy inhibits in vitro differentiation of C2C12 myoblasts. Mol Cell Biol. 2004;24:1481-92.
    • (2004) Mol Cell Biol , vol.24 , pp. 1481-1492
    • Favreau, C.1    Higuet, D.2    Courvalin, J.C.3    Buendia, B.4
  • 57
    • 2342463022 scopus 로고    scopus 로고
    • BAF: Roles in chromatin, nuclear structure and retrovirus integration
    • Segura-Totten M, Wilson KL. BAF: roles in chromatin, nuclear structure and retrovirus integration. Trends Cell Biol. 2004;14:261-6.
    • (2004) Trends Cell Biol , vol.14 , pp. 261-266
    • Segura-Totten, M.1    Wilson, K.L.2
  • 59
    • 0035694820 scopus 로고    scopus 로고
    • Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF
    • Lee KK, Haraguchi T, Lee RS, Koujin T, Hiraoka Y, Wilson KL. Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J Cell Sci. 2001;114:4567-73.
    • (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
  • 61
    • 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 JM, Lee KK, Kowalski AK, Wilson KL. Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J Biol Chem. 2003;278:6969-75.
    • (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
  • 62
    • 1542284570 scopus 로고    scopus 로고
    • Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by missense mutation that causes Emery-Dreifuss muscular dystrophy
    • Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y. Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by missense mutation that causes Emery-Dreifuss muscular dystrophy. Eur J Biochem. 2004;271:1035-45.
    • (2004) Eur J Biochem , vol.271 , pp. 1035-1045
    • Haraguchi, T.1    Holaska, J.M.2    Yamane, M.3    Koujin, T.4    Hashiguchi, N.5    Mori, C.6    Wilson, K.L.7    Hiraoka, Y.8
  • 65
    • 0036864411 scopus 로고    scopus 로고
    • Sterol regulatory element-binding proteins: Transcriptional activators of lipid synthesis
    • Horton JD. Sterol regulatory element-binding proteins: transcriptional activators of lipid synthesis. Biochem Soc Trans. 2002;30:1091-5.
    • (2002) Biochem Soc Trans , vol.30 , pp. 1091-1095
    • Horton, J.D.1
  • 66
    • 0036537888 scopus 로고    scopus 로고
    • A novel interaction between lamin A and SREBP1: Implications for partial lipodystrophy and other laminopathies
    • Lloyd DJ, Trembath RC, Shackleton S. A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies. Hum Mol Genet. 2002;11:769-77.
    • (2002) Hum Mol Genet , vol.11 , pp. 769-777
    • Lloyd, D.J.1    Trembath, R.C.2    Shackleton, S.3
  • 68
    • 0034987343 scopus 로고    scopus 로고
    • The HIV protease inhibitor indinavir impairs sterol regulatory element-binding protein-1 intranuclear localization, inhibits preadipocyte differentiation, and induces insulin resistance
    • Caron M, Auclair M, Vigouroux C, Glorian M, Forest C, Capeau J. The HIV protease inhibitor indinavir impairs sterol regulatory element-binding protein-1 intranuclear localization, inhibits preadipocyte differentiation, and induces insulin resistance. Diabetes. 2001;50:1378-88.
    • (2001) Diabetes , vol.50 , pp. 1378-1388
    • Caron, M.1    Auclair, M.2    Vigouroux, C.3    Glorian, M.4    Forest, C.5    Capeau, J.6
  • 69
    • 0035090666 scopus 로고    scopus 로고
    • Molecular basis of partial lipodystrophy and prospects for therapy
    • Hegele RA. Molecular basis of partial lipodystrophy and prospects for therapy. Trends Mol Med. 2001;7:121-6.
    • (2001) Trends Mol Med , vol.7 , pp. 121-126
    • Hegele, R.A.1
  • 73
    • 2142808834 scopus 로고    scopus 로고
    • Fat's loss is bone's gain
    • Pel L, Tontonoz P. Fat's loss is bone's gain. J Clin Invest. 2004;113:805-6.
    • (2004) J Clin Invest , vol.113 , pp. 805-806
    • Pel, L.1    Tontonoz, P.2
  • 74
    • 0028871780 scopus 로고
    • Transdifferentiation of myoblasts by the adipogenic transcription factors PPAR gamma and C/EBP alpha
    • U S A
    • Hu E, Tontonoz P, Spiegelman BM. Transdifferentiation of myoblasts by the adipogenic transcription factors PPAR gamma and C/EBP alpha. Proc Natl Acad Sci U S A. 1995;92:9856-60.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 9856-9860
    • Hu, E.1    Tontonoz, P.2    Spiegelman, B.M.3
  • 75
    • 0037078328 scopus 로고    scopus 로고
    • Bone morphogenetic protein and retinoic acid signaling cooperate to induce osteoblast differentiation of preadipocytes
    • Skillington J, Choy L, Derynck R. Bone morphogenetic protein and retinoic acid signaling cooperate to induce osteoblast differentiation of preadipocytes. J Cell Biol. 2002;159:135-46.
    • (2002) J Cell Biol , vol.159 , pp. 135-146
    • Skillington, J.1    Choy, L.2    Derynck, R.3
  • 76
    • 0038607705 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-activated receptor-gamma inhibits the Runx2-mediated transcription of osteocalcin in osteoblasts
    • Jeon MJ, Kim JA, Kwon SH, Kim SW, Park KS, Park SW, Kim SY, Shin CS. Activation of peroxisome proliferator-activated receptor-gamma inhibits the Runx2-mediated transcription of osteocalcin in osteoblasts. J Biol Chem. 2003;278:23270-7.
    • (2003) J Biol Chem , vol.278 , pp. 23270-23277
    • Jeon, M.J.1    Kim, J.A.2    Kwon, S.H.3    Kim, S.W.4    Park, K.S.5    Park, S.W.6    Kim, S.Y.7    Shin, C.S.8
  • 77
    • 33645457559 scopus 로고    scopus 로고
    • Emery-Dreifuss muscular dystrophy
    • Engel AG, Franzini-Armstrong C, editors. New York: McGraw-Hill
    • Maraldi NM, Merlini L. Emery-Dreifuss muscular dystrophy. In: Engel AG, Franzini-Armstrong C, editors. Myology. New York: McGraw-Hill; 2004.
    • (2004) Myology
    • Maraldi, N.M.1    Merlini, L.2
  • 78
    • 9544245803 scopus 로고    scopus 로고
    • Heterochromatin structure and function
    • Dillon N. Heterochromatin structure and function. Biol Cell. 2004;96:631-7.
    • (2004) Biol Cell , vol.96 , pp. 631-637
    • Dillon, N.1
  • 81
    • 0242365630 scopus 로고    scopus 로고
    • Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: Altered intermolecular interaction with emerin and implications for gene transcription
    • Capanni C, Cenni V, Mattioli E, Sabatelli P, Ognibene A, Columbaro M, Parnaik VK, Wehnert M, Maraldi NM, Squarzoni S, Lattanzi G. Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription. Exp Cell Res. 2003;291:122-34.
    • (2003) Exp Cell Res , vol.291 , pp. 122-134
    • Capanni, C.1    Cenni, V.2    Mattioli, E.3    Sabatelli, P.4    Ognibene, A.5    Columbaro, M.6    Parnaik, V.K.7    Wehnert, M.8    Maraldi, N.M.9    Squarzoni, S.10    Lattanzi, G.11
  • 87
    • 1842457722 scopus 로고    scopus 로고
    • Chromatin inheritance upon Zeste-mediated Brahma recruitment at a minimal cellular memory module
    • Dejardin J, Cavalli G. Chromatin inheritance upon Zeste-mediated Brahma recruitment at a minimal cellular memory module. EMBO J. 2004;23:857-68.
    • (2004) EMBO J , vol.23 , pp. 857-868
    • Dejardin, J.1    Cavalli, G.2
  • 88
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang Y, Reinberger D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev. 2001;15:2343-60.
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberger, D.2
  • 89
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science. 2001;293:1074-80.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 90
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner BM. Cellular memory and the histone code. Cell. 2002;111:285-91.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 91
    • 0347955358 scopus 로고    scopus 로고
    • Histone methyl-transferases direct different degrees of methylation to define distinct chromatin domains
    • Rice J, Briggs S, Ueberheide B, Barber C, Shabanowitz J, Hunt D, Shinkai Y, Allis C. Histone methyl-transferases direct different degrees of methylation to define distinct chromatin domains. Mol Cell. 2003;12:1591-8.
    • (2003) Mol Cell , vol.12 , pp. 1591-1598
    • Rice, J.1    Briggs, S.2    Ueberheide, B.3    Barber, C.4    Shabanowitz, J.5    Hunt, D.6    Shinkai, Y.7    Allis, C.8
  • 92
    • 19644381697 scopus 로고    scopus 로고
    • Differential subnuclear localization and replication timing of histone H3 lysine 9 methylation states
    • Mar 23; [Epub ahead of print]
    • Wu R, Terry AV, Singh PB, Gilbert DM. Differential subnuclear localization and replication timing of histone H3 lysine 9 methylation states. Mol Biol Cell. 2005 Mar 23; [Epub ahead of print]
    • (2005) Mol Biol Cell
    • Wu, R.1    Terry, A.V.2    Singh, P.B.3    Gilbert, D.M.4
  • 95
    • 0036966358 scopus 로고    scopus 로고
    • HP1: Facts, open questions, and speculation
    • Singh PB, Georgatos SD. HP1: facts, open questions, and speculation. J Struct Biol. 2003;140:10-6.
    • (2003) J Struct Biol , vol.140 , pp. 10-16
    • Singh, P.B.1    Georgatos, S.D.2
  • 96
    • 0037154983 scopus 로고    scopus 로고
    • The contribution of nuclear compartmentalization to gene regulation
    • Carmo-Fonseca M. The contribution of nuclear compartmentalization to gene regulation. Cell. 2002;108:513-21.
    • (2002) Cell , vol.108 , pp. 513-521
    • Carmo-Fonseca, M.1
  • 97
    • 0038054340 scopus 로고    scopus 로고
    • Spatial proximity of translocation-prone gene loci in human lymphomas
    • Roix JJ, McQueen P, Munson PJ, Prada LA, Misteli T. Spatial proximity of translocation-prone gene loci in human lymphomas. Nat Genet. 2003;34:287-91.
    • (2003) Nat Genet , vol.34 , pp. 287-291
    • Roix, J.J.1    McQueen, P.2    Munson, P.J.3    Prada, L.A.4    Misteli, T.5
  • 98
    • 0035834009 scopus 로고    scopus 로고
    • Nuclear relocation of a transactivator subunit precedes target gene activation
    • U S A
    • Francastel C, Magis W, Groudine M. Nuclear relocation of a transactivator subunit precedes target gene activation. Proc Natl Acad Sci U S A. 2001;98:12120-5.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 12120-12125
    • Francastel, C.1    Magis, W.2    Groudine, M.3
  • 99
    • 0038022718 scopus 로고    scopus 로고
    • Targeting genes and transcription factors to segregated nuclear compartments
    • Isogai Y, Tjian R. Targeting genes and transcription factors to segregated nuclear compartments. Curr Opin Cell Biol. 2003;15:296-303.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 296-303
    • Isogai, Y.1    Tjian, R.2
  • 100
    • 0025272702 scopus 로고
    • Cells of the cell immune and hemopoietic system of the mouse lack lamins A/C: Distinction versus other somatic cells
    • Rober RA, Sauter H, Weber K, Osborn M. Cells of the cell immune and hemopoietic system of the mouse lack lamins A/C: distinction versus other somatic cells. J Cell Sci. 1990;95:587-98.
    • (1990) J Cell Sci , vol.95 , pp. 587-598
    • Rober, R.A.1    Sauter, H.2    Weber, K.3    Osborn, M.4
  • 101
    • 0033083793 scopus 로고    scopus 로고
    • Dynamic repositioning of genes in the nucleus of lymphocytes preparing for cell division
    • Brown KE, Baxter J, Graf D, Merkenschlager M, Fisher AG. Dynamic repositioning of genes in the nucleus of lymphocytes preparing for cell division. Mol Cell. 1999;3:207-17.
    • (1999) Mol Cell , vol.3 , pp. 207-217
    • Brown, K.E.1    Baxter, J.2    Graf, D.3    Merkenschlager, M.4    Fisher, A.G.5
  • 102
    • 10444225317 scopus 로고    scopus 로고
    • Cytoskeletal influences on nuclear shape in granulocytic HL-60 cells
    • Olins AL, Olins DE. Cytoskeletal influences on nuclear shape in granulocytic HL-60 cells. BMC Cell Biol. 2004;5:30.
    • (2004) BMC Cell Biol , vol.5 , pp. 30
    • Olins, A.L.1    Olins, D.E.2
  • 103
    • 0035355509 scopus 로고    scopus 로고
    • Binding of Ikaros to the lambda5 promoter silences transcription through a mechanism that does not require heterochromatin formation
    • Sabbattini P. Lundgren M, Georgiou A, Chow C, Varnes G, Dillon N. Binding of Ikaros to the lambda5 promoter silences transcription through a mechanism that does not require heterochromatin formation. EMBO J. 2001;20:2812-22.
    • (2001) EMBO J , vol.20 , pp. 2812-2822
    • Sabbattini, P.1    Lundgren, M.2    Georgiou, A.3    Chow, C.4    Varnes, G.5    Dillon, N.6
  • 104
    • 0033200389 scopus 로고    scopus 로고
    • Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation
    • Tang QQ, Lane MD. Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation. Genes Dev. 1999;13:2231-41.
    • (1999) Genes Dev , vol.13 , pp. 2231-2241
    • Tang, Q.Q.1    Lane, M.D.2
  • 105
    • 0035833262 scopus 로고    scopus 로고
    • Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter
    • Muller WG, Walker D, Hager GL, McNally JG. Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter. J Cell Biol. 2001;154:33-48.
    • (2001) J Cell Biol , vol.154 , pp. 33-48
    • Muller, W.G.1    Walker, D.2    Hager, G.L.3    McNally, J.G.4
  • 106
    • 0036591875 scopus 로고    scopus 로고
    • Mechanisms of chromatin assembly and transcription
    • Kadam S, Emerson BM. Mechanisms of chromatin assembly and transcription. Curr Opin Cell Biol. 2002;14:262-8.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 262-268
    • Kadam, S.1    Emerson, B.M.2
  • 109
    • 0032478672 scopus 로고    scopus 로고
    • In vitro interaction of the carboxy-terminal domain of lamin A with actin
    • Sasseville AM, Langeher Y. In vitro interaction of the carboxy-terminal domain of lamin A with actin. FEBS Lett. 1998;425:485-9.
    • (1998) FEBS Lett , vol.425 , pp. 485-489
    • Sasseville, A.M.1    Langeher, Y.2
  • 110
    • 19344378383 scopus 로고    scopus 로고
    • Emerin caps the pointed end of actin filaments: Evidence for an actin cortical network at the nuclear inner membrane
    • Holaska JM, Kowalski AK, Wilson KL. Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. PloS Biol. 2004;2:E231.
    • (2004) PloS Biol , vol.2
    • Holaska, J.M.1    Kowalski, A.K.2    Wilson, K.L.3
  • 111
    • 0023871214 scopus 로고
    • Insulin stimulates incorporation of 32Pi into nuclear lamins A and C in quiescent BHK-21 cells
    • Friedman DL, Ken R. Insulin stimulates incorporation of 32Pi into nuclear lamins A and C in quiescent BHK-21 cells. J Biol Chem. 1988;263:1103-6.
    • (1988) J Biol Chem , vol.263 , pp. 1103-1106
    • Friedman, D.L.1    Ken, R.2
  • 113
    • 1842529177 scopus 로고    scopus 로고
    • Regulation of binding of lamin B receptor to chromatin by SR protein kinase and cdc2 kinase in Xenopus egg extracts
    • Takano M, Koyama Y, Ito H, Hoshino S, Onogi H, Hagiwara M, Furukawa K, Horigome T. Regulation of binding of lamin B receptor to chromatin by SR protein kinase and cdc2 kinase in Xenopus egg extracts. J Biol Chem. 2004;279:13265-71.
    • (2004) J Biol Chem , vol.279 , pp. 13265-13271
    • Takano, M.1    Koyama, Y.2    Ito, H.3    Hoshino, S.4    Onogi, H.5    Hagiwara, M.6    Furukawa, K.7    Horigome, T.8
  • 114
    • 4143103828 scopus 로고    scopus 로고
    • A phosphorylation cluster in the chromatin-binding region regulates chromosome association of LAP2alpha
    • Gajewski A, Csaszar E, Foisner R. A phosphorylation cluster in the chromatin-binding region regulates chromosome association of LAP2alpha. J Biol Chem. 2004;279:35813-21.118.
    • (2004) J Biol Chem , vol.279
    • Gajewski, A.1    Csaszar, E.2    Foisner, R.3
  • 115
  • 120
    • 0242383489 scopus 로고    scopus 로고
    • Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery
    • Mattout-Drubezki A, Gruenbaum Y. Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery. Cell Mol Life Sci. 2003;60:2053-63.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2053-2063
    • Mattout-Drubezki, A.1    Gruenbaum, Y.2
  • 122
    • 0027442899 scopus 로고
    • The alpha-helical rod domain of human lamins A and C contains a chromatin binding site
    • Glass CA, Glass JR, Taniura H, Hasel KW, Blevitt JM, Gerace L. The alpha-helical rod domain of human lamins A and C contains a chromatin binding site. EMBO J. 1993;12:4413-24.
    • (1993) EMBO J , vol.12 , pp. 4413-4424
    • Glass, C.A.1    Glass, J.R.2    Taniura, H.3    Hasel, K.W.4    Blevitt, J.M.5    Gerace, L.6
  • 123
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura H, Glass C, Gerace L. A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones. J Cell Biol. 1995;131:33-44.
    • (1995) J Cell Biol , vol.131 , pp. 33-44
    • Taniura, H.1    Glass, C.2    Gerace, L.3
  • 130
    • 0041919374 scopus 로고    scopus 로고
    • Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia
    • Agarwal AK, Fryns JP, Auchus RJ, Garg A. Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia. Hum Mol Genet. 2003;12:1995-2001.
    • (2003) Hum Mol Genet , vol.12 , pp. 1995-2001
    • Agarwal, A.K.1    Fryns, J.P.2    Auchus, R.J.3    Garg, A.4
  • 132
    • 0028274845 scopus 로고
    • The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties
    • Hennekes H, Nigg EA. The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J Cell Sci. 1994;107:1019-29.
    • (1994) J Cell Sci , vol.107 , pp. 1019-1029
    • Hennekes, H.1    Nigg, E.A.2
  • 133
    • 0141530040 scopus 로고    scopus 로고
    • A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation
    • Maske CP, Hollinshead MS, Higbee NC, Bergo MO, Young SG, Vaux DJ. A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation. J Cell Biol. 2003;162:1223-32.
    • (2003) J Cell Biol , vol.162 , pp. 1223-1232
    • Maske, C.P.1    Hollinshead, M.S.2    Higbee, N.C.3    Bergo, M.O.4    Young, S.G.5    Vaux, D.J.6
  • 135
    • 0033569878 scopus 로고    scopus 로고
    • Prenylated prelamin A interacts with Narf, a novel nuclear protein
    • Barton RM, Worman HJ. Prenylated prelamin A interacts with Narf, a novel nuclear protein. J Biol Chem. 1999;274:30008-18.
    • (1999) J Biol Chem , vol.274 , pp. 30008-30018
    • Barton, R.M.1    Worman, H.J.2
  • 136
    • 0028831126 scopus 로고
    • Lamin A precursor is localized to intranuclear foci
    • Sasseville AM, Raymond Y. Lamin A precursor is localized to intranuclear foci. J Cell Sci. 1995;108:273-85.
    • (1995) J Cell Sci , vol.108 , pp. 273-285
    • Sasseville, A.M.1    Raymond, Y.2
  • 137
    • 0034672686 scopus 로고    scopus 로고
    • Functional aspects of polyisoprenoid protein substituents: Roles in protein-protein interaction and trafficking
    • Sinensky M. Functional aspects of polyisoprenoid protein substituents: roles in protein-protein interaction and trafficking. Biochim Biophys Acta. 2000;1529:203-9.
    • (2000) Biochim Biophys Acta , vol.1529 , pp. 203-209
    • Sinensky, M.1
  • 138
    • 0034613286 scopus 로고    scopus 로고
    • RhoA prenylation is required for promotion of cell growth and transformation and cytoskeleton organization but not for induction of serum response element transcription
    • Allal C, Favre G, Couderc B, Salicio S, Sixou S, Hamilton AD, Sebti SM. RhoA prenylation is required for promotion of cell growth and transformation and cytoskeleton organization but not for induction of serum response element transcription. J Biol Chem. 2000;275:31001-8.
    • (2000) J Biol Chem , vol.275 , pp. 31001-31008
    • Allal, C.1    Favre, G.2    Couderc, B.3    Salicio, S.4    Sixou, S.5    Hamilton, A.D.6    Sebti, S.M.7
  • 139
    • 1542382269 scopus 로고    scopus 로고
    • Multiple and surprising new functions for emerin, a nuclear membrane protein
    • Bengtsson L, Wilson KL. Multiple and surprising new functions for emerin, a nuclear membrane protein. Curr Opin Cell Biol. 2004;16:73-9.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 73-79
    • Bengtsson, L.1    Wilson, K.L.2
  • 140
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP, FLIP and FRET analyses in living HeLa cells
    • Shimi T, Koujin T, Segura-Totten M, Wilson KL, Haraguchi T, Hiraoka Y. Dynamic interaction between BAF and emerin revealed by FRAP, FLIP and FRET analyses in living HeLa cells. J Struct Biol. 2004;147:31-41.
    • (2004) J Struct Biol , vol.147 , pp. 31-41
    • Shimi, T.1    Koujin, T.2    Segura-Totten, M.3    Wilson, K.L.4    Haraguchi, T.5    Hiraoka, Y.6
  • 144
    • 17644373758 scopus 로고    scopus 로고
    • Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome
    • Scaffidi P, Misteli T. Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome. Nat Med. 2005;11:440-5.
    • (2005) Nat Med , vol.11 , pp. 440-445
    • Scaffidi, P.1    Misteli, T.2
  • 146
    • 14944383792 scopus 로고    scopus 로고
    • RNAi of FACE1 protease results in growth inhibition of human cells expressing lamin A: Implications for Hutchinson-Gilford progeria syndrome
    • Gruber J, Lampe T, Osbom M, Weber K. RNAi of FACE1 protease results in growth inhibition of human cells expressing lamin A: implications for Hutchinson-Gilford progeria syndrome. J Cell Sci. 2005;118:689-96.
    • (2005) J Cell Sci , vol.118 , pp. 689-696
    • Gruber, J.1    Lampe, T.2    Osbom, M.3    Weber, K.4
  • 147
    • 0028016261 scopus 로고
    • Expression of prelamin A but not mature lamin A confers sensitivity of DNA biosynthesis to lovostatin on F9 teratocarcinoma cells
    • Sinensky M, McLain T, Fantle K. Expression of prelamin A but not mature lamin A confers sensitivity of DNA biosynthesis to lovostatin on F9 teratocarcinoma cells. J Cell Sci. 1994;107:2215-8.
    • (1994) J Cell Sci , vol.107 , pp. 2215-2218
    • Sinensky, M.1    McLain, T.2    Fantle, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.