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Volumn 60, Issue 10, 2003, Pages 2053-2063

Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery

Author keywords

BAF; GCL; Heterochromatin; Lamin associated proteins; Lamins; LEM domain; Transcriptional regulation

Indexed keywords

DNA; EMERIN; INTERMEDIATE FILAMENT PROTEIN; LAMIN A; LAMIN B; LAMIN B RECEPTOR; LAMIN C; LAMINA ASSOCIATED POLYPEPTIDE 1; LAMINA ASSOCIATED POLYPEPTIDE 2; NUCLEAR PROTEIN; RNA POLYMERASE II; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0242383489     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3038-3     Document Type: Review
Times cited : (118)

References (147)
  • 1
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly and interactions
    • Stuurman N., Heins S. and Aebi U. (1998) Nuclear lamins: their structure, assembly and interactions. J. Struct. Biol. 122: 42-66
    • (1998) J. Struct. Biol. , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 3
    • 0033926099 scopus 로고    scopus 로고
    • Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics
    • Dechat T., Vlcek S. and Foisner R. (2000) Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics. J. Struct. Biol. 129: 335-345
    • (2000) J. Struct. Biol. , vol.129 , pp. 335-345
    • Dechat, T.1    Vlcek, S.2    Foisner, R.3
  • 6
    • 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. andGruenbaum Y. (2001a) Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina. Trends Biochem. Sci. 26:41-47
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 41-47
    • Cohen, M.1    Lee, K.K.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 8
    • 0001896725 scopus 로고    scopus 로고
    • Membrane proteins of the nuclear pore complex: Gp210 is conserved in Drosophila, C. elegans and Arabidopsis
    • Cohen M., Wilson K. L. and Gruenbaum Y (2001 ) Membrane proteins of the nuclear pore complex: Gp210 is conserved in Drosophila, C. elegans and Arabidopsis. Gene Then Mol. Biol. 6: 47-55
    • (2001) Gene Then Mol. Biol. , vol.6 , pp. 47-55
    • Cohen, M.1    Wilson, K.L.2    Gruenbaum, Y.3
  • 9
    • 0034687110 scopus 로고    scopus 로고
    • Tunicates have unusual nuclear lamins with a large deletion in the carboxyterminal tail domain
    • Riemer D., Wang J., Zimek A., Swalla B. J. and Weber K. (2000) Tunicates have unusual nuclear lamins with a large deletion in the carboxyterminal tail domain. Gene 255: 317-325
    • (2000) Gene , vol.255 , pp. 317-325
    • Riemer, D.1    Wang, J.2    Zimek, A.3    Swalla, B.J.4    Weber, K.5
  • 10
    • 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., Rolef-Ben Shahar T, Riemer D., Spann, P., Treinin M., Weber K. et al. (2000) Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression and spatial organization of nuclear pore complexes. Mol. Biol. Cell 11: 3937-3947
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3937-3947
    • Liu, J.1    Rolef-Ben Shahar, T.2    Riemer, D.3    Spann, P.4    Treinin, M.5    Weber, K.6
  • 11
    • 0035972145 scopus 로고    scopus 로고
    • Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization
    • Schirmer E. C., Guan T. and Gerace L. (2001) Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization. J. Cell Biol. 153: 479-490
    • (2001) J. Cell Biol. , vol.153 , pp. 479-490
    • Schirmer, E.C.1    Guan, T.2    Gerace, L.3
  • 12
    • 0036968817 scopus 로고    scopus 로고
    • Transmission electron microscope studies of the nuclear envelope in C. elegans embryos
    • Cohen M., Tzur Y B., Neufeld E., Feinstein N., Delannoy M. R., Wilson K. L. et al. (2002) Transmission electron microscope studies of the nuclear envelope in C. elegans embryos. J. Struct. Biol. 140: 232-240
    • (2002) J. Struct. Biol. , vol.140 , pp. 232-240
    • Cohen, M.1    Tzur, Y.B.2    Neufeld, E.3    Feinstein, N.4    Delannoy, M.R.5    Wilson, K.L.6
  • 13
    • 0031005809 scopus 로고    scopus 로고
    • Insertional mutation of the Drosophila nuclear lamin dm(0) gene results in defective nuclear envelopes, clustering of nuclear pore complexes and accumulation of annulate lamellae
    • Lenz-Bohme B., Wismar J., Fuchs S., Reifegerste R., Buchner E., Betz H. et al. (1997) Insertional mutation of the Drosophila nuclear lamin dm(0) gene results in defective nuclear envelopes, clustering of nuclear pore complexes and accumulation of annulate lamellae. J. Cell Biol 137: 1001-1016
    • (1997) J. Cell Biol. , vol.137 , pp. 1001-1016
    • Lenz-Bohme, B.1    Wismar, J.2    Fuchs, S.3    Reifegerste, R.4    Buchner, E.5    Betz, H.6
  • 14
    • 0030863126 scopus 로고    scopus 로고
    • Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis
    • Spann T. P., Moir R. D., Goldman A. E., Stick R. and Goldman R. D. (1997) Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis. J. Cell Biol. 136: 1201-1212
    • (1997) J. Cell Biol. , vol.136 , pp. 1201-1212
    • Spann, T.P.1    Moir, R.D.2    Goldman, A.E.3    Stick, R.4    Goldman, R.D.5
  • 15
    • 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. and 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
  • 17
    • 0030465544 scopus 로고    scopus 로고
    • Lamin proteolysis facilitates nuclear events during apoptosis
    • Rao L., Perez D. and White E. (1996) Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell Biol. 135: 1441-1455
    • (1996) J. Cell Biol. , vol.135 , pp. 1441-1455
    • Rao, L.1    Perez, D.2    White, E.3
  • 18
    • 0037090614 scopus 로고    scopus 로고
    • Caspase-6 gene disruption reveals a requirement for lamin a cleavage in apoptotic chromatin condensation
    • Ruchaud S., Korfali N., Villa P., Kottke T. J., Dingwall C., Kaufmann S. H. et al. (2002) Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. EMBO J. 21: 1967-1977
    • (2002) EMBO J. , vol.21 , pp. 1967-1977
    • Ruchaud, S.1    Korfali, N.2    Villa, P.3    Kottke, T.J.4    Dingwall, C.5    Kaufmann, S.H.6
  • 19
    • 0030731381 scopus 로고    scopus 로고
    • GST-lamin fusion proteins act as dominant negative mutants in Xenopus egg extract and reveal the function of the lamina in DNA replication
    • Ellis D. J., Jenkins H., Whitfield W. G. and Hutchison C. J. (1997) GST-lamin fusion proteins act as dominant negative mutants in Xenopus egg extract and reveal the function of the lamina in DNA replication. J. Cell Sci. 110: 2507-2518
    • (1997) J. Cell Sci. , vol.110 , pp. 2507-2518
    • Ellis, D.J.1    Jenkins, H.2    Whitfield, W.G.3    Hutchison, C.J.4
  • 20
    • 0033636843 scopus 로고    scopus 로고
    • Head and/or CaaX domain deletions of lamin proteins disrupt preformed lamin a and C but not lamin B structure in mammalian cells
    • Izumi M., Vaughan O. A., Hutchison C. J. and Gilbert D. M. (2000) Head and/or CaaX domain deletions of lamin proteins disrupt preformed lamin A and C but not lamin B structure in mammalian cells. Mol. Biol. Cell. 11: 4323-4337
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 4323-4337
    • Izumi, M.1    Vaughan, O.A.2    Hutchison, C.J.3    Gilbert, D.M.4
  • 21
    • 0037128211 scopus 로고    scopus 로고
    • Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription
    • Spann T. P., Goldman A. E., Wang C., Huang S. and Goldman R. D. (2002) Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription. J. Cell Biol. 156: 603-608
    • (2002) J. Cell Biol. , vol.156 , pp. 603-608
    • Spann, T.P.1    Goldman, A.E.2    Wang, C.3    Huang, S.4    Goldman, R.D.5
  • 22
    • 0035694702 scopus 로고    scopus 로고
    • unc-83 encodes a novel component of the nuclear envelope and is essential for proper nuclear migration
    • Starr D. A., Hermann G. J., Malone C. J., Fixsen W., Priess J. R., Horvitz H. R. et al. (2001) unc-83 encodes a novel component of the nuclear envelope and is essential for proper nuclear migration. Development 128: 5039-5050
    • (2001) Development , vol.128 , pp. 5039-5050
    • Starr, D.A.1    Hermann, G.J.2    Malone, C.J.3    Fixsen, W.4    Priess, J.R.5    Horvitz, H.R.6
  • 23
    • 0036193442 scopus 로고    scopus 로고
    • Lamin-dependent localization of UNC-84, a protein required for nuclear migration in C. elegans
    • Lee K. K., Starr D., Liu J., Cohen M., Han M., Wilson K. et al. (2002) Lamin-dependent localization of UNC-84, a protein required for nuclear migration in C. elegans. Mol. Biol. Cell 13: 892-901
    • (2002) Mol. Biol. Cell , vol.13 , pp. 892-901
    • Lee, K.K.1    Starr, D.2    Liu, J.3    Cohen, M.4    Han, M.5    Wilson, K.6
  • 24
    • 2642691663 scopus 로고    scopus 로고
    • Functional dissection of YA, an essential, developmentally regulated nuclear lamina protein in Drosophila melanogaster
    • Liu J. and Wolfner M. F. (1998) Functional dissection of YA, an essential, developmentally regulated nuclear lamina protein in Drosophila melanogaster. Mol. Cell. Biol. 18: 188-197
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 188-197
    • Liu, J.1    Wolfner, M.F.2
  • 25
    • 0027509502 scopus 로고
    • DNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells
    • Furukawa K. and Hotta Y. (1993) cDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells. EMBO J. 12: 97-106
    • (1993) EMBO J. , vol.12 , pp. 97-106
    • Furukawa, K.1    Hotta, Y.2
  • 26
    • 0016401871 scopus 로고
    • Structure, biochemistry, and function of the nuclear envelope
    • Franke W. W. (1974) Structure, biochemistry, and function of the nuclear envelope. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 268: 67-93
    • (1974) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.268 , pp. 67-93
    • Franke, W.W.1
  • 28
    • 0033117126 scopus 로고    scopus 로고
    • Nuclear organization and chromosome segregation
    • Franklin A. E. (1999) Nuclear organization and chromosome segregation. Plant Cell 11: 523-534.
    • (1999) Plant Cell , vol.11 , pp. 523-534
    • Franklin, A.E.1
  • 30
    • 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
    • Hofemeister H., Weber K. and Stick R. (2000) Association of prenylated proteins with the plasma membrane and the inner nuclear membrane is mediated by the same membrane-targeting motifs. Mol. Biol. Cell 11: 3233-3246
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3233-3246
    • Hofemeister, H.1    Weber, K.2    Stick, R.3
  • 31
    • 0025745453 scopus 로고
    • In vitro reconstitution of recombinant lamin a and a lamin a mutant lacking the carboxy-terminal tail
    • Gieffers C. and Krohne G. (1991) In vitro reconstitution of recombinant lamin A and a lamin A mutant lacking the carboxy-terminal tail. Eur. J. Cell Biol. 55: 191-1999
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 191-1999
    • Gieffers, C.1    Krohne, G.2
  • 32
    • 0026568833 scopus 로고
    • The role of the head and tail domain in lamin structure and assembly: Analysis of bacterially expressed chicken lamin a and truncated B2 lamins
    • Heitlinger E., Peter M., Lustig A., Villiger W., Nigg E. A. and Aebi U. (1992) The role of the head and tail domain in lamin structure and assembly: analysis of bacterially expressed chicken lamin A and truncated B2 lamins. J. Struct. Biol. 108: 74-89
    • (1992) J. Struct. Biol. , vol.108 , pp. 74-89
    • Heitlinger, E.1    Peter, M.2    Lustig, A.3    Villiger, W.4    Nigg, E.A.5    Aebi, U.6
  • 33
    • 0000052626 scopus 로고    scopus 로고
    • Structural organization and biological roles of the nuclear lamina
    • Harel A., Goldberg M., Ulitzur N. and Gruenbaum Y. (1998) Structural organization and biological roles of the nuclear lamina. Gene Ther. Mol. Biol. 1: 529-542
    • (1998) Gene Ther. Mol. Biol. , vol.1 , pp. 529-542
    • Harel, A.1    Goldberg, M.2    Ulitzur, N.3    Gruenbaum, Y.4
  • 34
    • 0027729310 scopus 로고
    • A nuclear lamin of the nematode Caenorhabditis elegans with unusual structural features; cDNA cloning and gene organization
    • Riemer D., Dodemont H. and Weber K. (1993) A nuclear lamin of the nematode Caenorhabditis elegans with unusual structural features; cDNA cloning and gene organization. Eur. J. Cell Biol. 62: 214-223
    • (1993) Eur. J. Cell Biol. , vol.62 , pp. 214-223
    • Riemer, D.1    Dodemont, H.2    Weber, K.3
  • 35
    • 0023840620 scopus 로고
    • Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene
    • Gruenbaum Y., Landesman Y., Drees B., Bare J. W., Saumweber H., Paddy M. R. et al. (1988) Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene. J. Cell Biol. 106: 585-596
    • (1988) J. Cell Biol. , vol.106 , pp. 585-596
    • Gruenbaum, Y.1    Landesman, Y.2    Drees, B.3    Bare, J.W.4    Saumweber, H.5    Paddy, M.R.6
  • 36
    • 0027285880 scopus 로고
    • A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate filament protein
    • Bossie C. A. and Sanders M. M. (1993) A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate filament protein. J. Cell Sci. 104: 1263-1272
    • (1993) J. Cell Sci. , vol.104 , pp. 1263-1272
    • Bossie, C.A.1    Sanders, M.M.2
  • 37
    • 0022648101 scopus 로고
    • Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins
    • McKeon F. D., Kirschner M. W. and Caput D. (1986) Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319: 463-468
    • (1986) Nature , vol.319 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 38
    • 0023032014 scopus 로고
    • cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins
    • Fisher D. Z., Chaudhary N. and Blobel G. (1986) cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl. Acad. Sci. USA 83: 6450-6454
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 39
    • 0024241247 scopus 로고
    • Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones
    • Hoger T. H., Krohne G. and Franke W. W. (1988) Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones. Eur. J. Cell Biol. 47: 283-290
    • (1988) Eur. J. Cell Biol. , vol.47 , pp. 283-290
    • Hoger, T.H.1    Krohne, G.2    Franke, W.W.3
  • 40
    • 0028342511 scopus 로고
    • Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice
    • Furukawa K., Inagaki H. and Hotta Y. (1994) Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice. Exp. Cell Res. 212: 426-430
    • (1994) Exp. Cell Res. , vol.212 , pp. 426-430
    • Furukawa, K.1    Inagaki, H.2    Hotta, Y.3
  • 41
    • 0033939554 scopus 로고    scopus 로고
    • The dynamics of the nuclear lamins during the cell cycle-relationship between structure and function
    • Moir R. D., Spann T. P., Lopez-Soler R. I., Yoon M., Goldman A. E., Khuon S. et al. (2000) The dynamics of the nuclear lamins during the cell cycle-relationship between structure and function. J. Struct. Biol. 129: 324-334
    • (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    Khuon, S.6
  • 42
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozak P., Sasseville A. M., Raymond Y. and Cook P. R. (1995) Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J. Cell Sci. 108: 635-644
    • (1995) J. Cell Sci. , vol.108 , pp. 635-644
    • Hozak, P.1    Sasseville, A.M.2    Raymond, Y.3    Cook, P.R.4
  • 43
    • 0037049554 scopus 로고    scopus 로고
    • Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription
    • Kumaran R. I., Muralikrishna B, and Parnaik V. K. (2002) Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription. J. Cell Biol. 159: 783-793
    • (2002) J. Cell Biol. , vol.159 , pp. 783-793
    • Kumaran, R.I.1    Muralikrishna, B.2    Parnaik, V.K.3
  • 44
    • 0027752440 scopus 로고
    • Lamin B distribution and association with peripheral chromatin revealed by optical sectioning and electron microscopy tomography
    • Belmont A. S., Zhai Y. and Thilenius A. (1993) Lamin B distribution and association with peripheral chromatin revealed by optical sectioning and electron microscopy tomography. J. Cell Biol. 123: 1671-1685
    • (1993) J. Cell Biol. , vol.123 , pp. 1671-1685
    • Belmont, A.S.1    Zhai, Y.2    Thilenius, A.3
  • 45
    • 0031965429 scopus 로고    scopus 로고
    • In vivo association of lamins with nucleic acids in Drosophila melanogaster
    • Rzepecki R., Bogachev S. S., Kokoza E., Stuurman N. and Fisher P. A. (1998) In vivo association of lamins with nucleic acids in Drosophila melanogaster. J. Cell Sci. 111: 121-129
    • (1998) J. Cell Sci. , vol.111 , pp. 121-129
    • Rzepecki, R.1    Bogachev, S.S.2    Kokoza, E.3    Stuurman, N.4    Fisher, P.A.5
  • 47
    • 0029967125 scopus 로고    scopus 로고
    • DNA from Drosophila melanogaster beta-heterochromatin binds specifically to nuclear lamins in vitro and the nuclear envelope in situ
    • Baricheva E. A., Berrios M., Bogachev S. S., Borisevich I. V., Lapik E. R., Sharakhov I. V. et al. (1996) DNA from Drosophila melanogaster beta-heterochromatin binds specifically to nuclear lamins in vitro and the nuclear envelope in situ. Gene 171: 171-176
    • (1996) Gene , vol.171 , pp. 171-176
    • Baricheva, E.A.1    Berrios, M.2    Bogachev, S.S.3    Borisevich, I.V.4    Lapik, E.R.5    Sharakhov, I.V.6
  • 48
    • 0025302814 scopus 로고
    • The in vitro DNA-binding properties of purified nuclear lamin proteins and vimentin
    • Shoeman R. L. and Traub P. ( 1990) The in vitro DNA-binding properties of purified nuclear lamin proteins and vimentin. J. Biol. Chem. 265: 9055-9061
    • (1990) J. Biol. Chem. , vol.265 , pp. 9055-9061
    • Shoeman, R.L.1    Traub, P.2
  • 49
    • 0032191345 scopus 로고    scopus 로고
    • Facilitation of chromatin dynamics by SARs
    • Hart C. M. and Laemmli U. K. (1998) Facilitation of chromatin dynamics by SARs. Curr. Opin. Genet. Dev. 8: 519-525
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 519-525
    • Hart, C.M.1    Laemmli, U.K.2
  • 50
    • 0024894099 scopus 로고
    • Protein:DNA interactions at chromosomal loop attachment sites
    • Blasquez V. C., Sperry A. O., Cockerill P. N. and Garrard W. T. (1989) Protein:DNA interactions at chromosomal loop attachment sites. Genome 31: 503-539
    • (1989) Genome , vol.31 , pp. 503-539
    • Blasquez, V.C.1    Sperry, A.O.2    Cockerill, P.N.3    Garrard, W.T.4
  • 51
    • 0028168825 scopus 로고
    • Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove
    • Luderus M. E., den Blaauwen J., de Smit O., Compton D. A. and van Driel R. (1994) Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove. Mol. Cell. Biol. 14: 6297-6305
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6297-6305
    • Luderus, M.E.1    Den Blaauwen, J.2    De Smit, O.3    Compton, D.A.4    Van Driel, R.5
  • 52
    • 0030025220 scopus 로고    scopus 로고
    • Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state
    • Zhao K., Harel A., Stuurman N., Guedalia D. and Gruenbaum Y. (1996) Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state. FEBS Lett. 380: 161-164
    • (1996) FEBS Lett. , vol.380 , pp. 161-164
    • Zhao, K.1    Harel, A.2    Stuurman, N.3    Guedalia, D.4    Gruenbaum, Y.5
  • 53
    • 0026343513 scopus 로고
    • Interaction of Xenopus lamins a and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain
    • Hoger T. H., Krohne G. and Kleinschmidt J. A. (1991) Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain. Exp. Cell Res. 197: 280-289
    • (1991) Exp. Cell Res. , vol.197 , pp. 280-289
    • Hoger, T.H.1    Krohne, G.2    Kleinschmidt, J.A.3
  • 55
    • 0025005766 scopus 로고
    • Lamins a and C bind and assemble at the surface of mitotic chromosomes
    • Glass J. R. and Gerace L. (1990) Lamins A and C bind and assemble at the surface of mitotic chromosomes. J. Cell Biol. 111: 1047-1057
    • (1990) J. Cell Biol. , vol.111 , pp. 1047-1057
    • Glass, J.R.1    Gerace, L.2
  • 57
    • 0026657886 scopus 로고
    • Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract
    • Ulitzur N., Harel A., Feinstein N. and Gruenbaum Y. (1992) Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract. J. Cell Biol. 119: 17-25.
    • (1992) J. Cell Biol. , vol.119 , pp. 17-25
    • Ulitzur, N.1    Harel, A.2    Feinstein, N.3    Gruenbaum, Y.4
  • 58
    • 0025056506 scopus 로고
    • On the cell-free association of lamins a and C with metaphase chromosomes
    • Burke, B. (1990) On the cell-free association of lamins A and C with metaphase chromosomes. Exp. Cell Res. 186: 169-176
    • (1990) Exp. Cell Res. , vol.186 , pp. 169-176
    • Burke, B.1
  • 59
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura H., Glass C. and Gerace L. (1995) A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones. J. Cell Biol. 131: 33-44
    • (1995) J. Cell Biol. , vol.131 , pp. 33-44
    • Taniura, H.1    Glass, C.2    Gerace, L.3
  • 62
    • 0037015302 scopus 로고    scopus 로고
    • The photomorphogenesis regulator DET1 binds the amino-terminal tail of histone H2B in a nucleosome context
    • Benvenuto G., Formiggini F., Laflamme P., Malakhov M. and Bowler C. (2002) The photomorphogenesis regulator DET1 binds the amino-terminal tail of histone H2B in a nucleosome context. Curr. Biol. 12: 1529-1534
    • (2002) Curr. Biol. , vol.12 , pp. 1529-1534
    • Benvenuto, G.1    Formiggini, F.2    Laflamme, P.3    Malakhov, M.4    Bowler, C.5
  • 63
    • 0026671560 scopus 로고
    • The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins
    • Simos G. and Georgatos S. D. (1992) The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins. EMBO J. 11: 4027-4036
    • (1992) EMBO J. , vol.11 , pp. 4027-4036
    • Simos, G.1    Georgatos, S.D.2
  • 64
    • 0028363978 scopus 로고
    • Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane
    • Ye Q. and Worman H. J. ( 1994) Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane. J. Biol. Chem. 269: 11306-11311
    • (1994) J. Biol. Chem. , vol.269 , pp. 11306-11311
    • Ye, Q.1    Worman, H.J.2
  • 65
    • 0032535470 scopus 로고    scopus 로고
    • The human lamin B receptor/sterol reductase multigene family
    • Holmer L., Pezhman A. and Worman H. J. (1998) The human lamin B receptor/sterol reductase multigene family. Genomics 54: 469-476
    • (1998) Genomics , vol.54 , pp. 469-476
    • Holmer, L.1    Pezhman, A.2    Worman, H.J.3
  • 66
    • 0025149541 scopus 로고
    • The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains
    • Worman H. J., Evans C. D. and Blobel G. (1990) The lamin B receptor of the nuclear envelope inner membrane: a polytopic protein with eight potential transmembrane domains. J. Cell Biol. 111: 1535-1542
    • (1990) J. Cell Biol. , vol.111 , pp. 1535-1542
    • Worman, H.J.1    Evans, C.D.2    Blobel, G.3
  • 67
    • 0031001130 scopus 로고    scopus 로고
    • cDNA cloning of nuclear localization signal binding protein NBP60, a rat homologue of lamin B receptor, and identification of binding sites of human lamin B receptor for nuclear localization signals and chromatin
    • Kawahire S., Takeuchi M., Gohshi T., Sasagawa S., Shimada M., Takahashi M. et al. (1997) cDNA cloning of nuclear localization signal binding protein NBP60, a rat homologue of lamin B receptor, and identification of binding sites of human lamin B receptor for nuclear localization signals and chromatin. J. Biochem. 121: 881-889
    • (1997) J. Biochem. , vol.121 , pp. 881-889
    • Kawahire, S.1    Takeuchi, M.2    Gohshi, T.3    Sasagawa, S.4    Shimada, M.5    Takahashi, M.6
  • 68
    • 0034732949 scopus 로고    scopus 로고
    • Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker
    • Duband-Goulet I. and Courvalin J. C. (2000). Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker. Biochemistry 39: 6483-6488
    • (2000) Biochemistry , vol.39 , pp. 6483-6488
    • Duband-Goulet, I.1    Courvalin, J.C.2
  • 69
    • 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 J. C. and Worman H. J. (1997) Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. J. Biol. Chem. 272: 14983-14989
    • (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
  • 70
    • 0034756597 scopus 로고    scopus 로고
    • Histones H3 /H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1
    • Polioudaki H., Kourmouli N., Drosou V, Bakou A., Theodoropoulos P. A., Singh P. B. et al. (2001) Histones H3 /H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1. EMBO Rep. 2: 920-935
    • (2001) EMBO Rep. , vol.2 , pp. 920-935
    • Polioudaki, H.1    Kourmouli, N.2    Drosou, V.3    Bakou, A.4    Theodoropoulos, P.A.5    Singh, P.B.6
  • 71
    • 0033677568 scopus 로고    scopus 로고
    • HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics
    • Martins S. B., Eide T., Steen R. L., Jahnsen T., Skalhegg B. S. and Collas P (2000) HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics. J. Cell Sci. 113: 3703-3711
    • (2000) J. Cell Sci. , vol.113 , pp. 3703-3711
    • Martins, S.B.1    Eide, T.2    Steen, R.L.3    Jahnsen, T.4    Skalhegg, B.S.5    Collas, P.6
  • 72
    • 0034026194 scopus 로고    scopus 로고
    • The HP1 protein family: Getting a grip on chromatin
    • Eissenberg J. C. and Elgin S. C. (2000) The HP1 protein family: getting a grip on chromatin. Curr. Opin. Genet. Dev. 10: 204-210
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 204-210
    • Eissenberg, J.C.1    Elgin, S.C.2
  • 73
    • 0036574913 scopus 로고    scopus 로고
    • Unravelling heterochromatin: Competition between positive and negative factors regulates accessibility
    • Dillon N. and Festenstein R. (2002) Unravelling heterochromatin: competition between positive and negative factors regulates accessibility. Trends Genet. 18: 252-258
    • (2002) Trends Genet. , vol.18 , pp. 252-258
    • Dillon, N.1    Festenstein, R.2
  • 74
    • 0036699522 scopus 로고    scopus 로고
    • Mutations in the gene encoding, the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly)
    • Hoffmann K., Dreger C. K., Olins A. L., Olins D. E., Shultz L. D., Lucke B. et al. (2002) Mutations in the gene encoding, the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly). Nat. Gen. 31: 410-414
    • (2002) Nat. Gen. , vol.31 , pp. 410-414
    • Hoffmann, K.1    Dreger, C.K.2    Olins, A.L.3    Olins, D.E.4    Shultz, L.D.5    Lucke, B.6
  • 75
    • 0345535128 scopus 로고    scopus 로고
    • Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene
    • Waterham H. R., Koster J., Mooyer P., Noort G.v. G., Kelley R. I., Wilcox W. R. et al. (2003) Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene. Am. J. Hum. Genet. 72: 1013-1017
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 1013-1017
    • Waterham, H.R.1    Koster, J.2    Mooyer, P.3    Noort, G.V.G.4    Kelley, R.I.5    Wilcox, W.R.6
  • 76
    • 0035793608 scopus 로고    scopus 로고
    • Cloning and characterization of an atypical Type IV P-type ATPase that binds to the RING motif of RUSH transcription factors
    • Mansharamani M., Hewetson A. and Chilton B. S. (2001) Cloning and characterization of an atypical Type IV P-type ATPase that binds to the RING motif of RUSH transcription factors. J. Biol. Chem. 276: 3641-3649
    • (2001) J. Biol. Chem. , vol.276 , pp. 3641-3649
    • Mansharamani, M.1    Hewetson, A.2    Chilton, B.S.3
  • 77
    • 0034681345 scopus 로고    scopus 로고
    • MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin
    • Lin F., Blake D. L., Callebaut I., Skerjanc I. S., Holmer L., McBurney M. W. et al. (2000) MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin. J. Biol. Chem. 275: 4840-4847
    • (2000) J. Biol. Chem. , vol.275 , pp. 4840-4847
    • Lin, F.1    Blake, D.L.2    Callebaut, I.3    Skerjanc, I.S.4    Holmer, L.5    McBurney, M.W.6
  • 78
    • 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
  • 79
    • 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. and 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
  • 80
    • 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. and 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
  • 81
    • 0032539631 scopus 로고    scopus 로고
    • A previously unidentified host protein protects retroviral DNA from autointegration
    • Lee M. S. and Craigie R. (1998) A previously unidentified host protein protects retroviral DNA from autointegration. Proc. Natl. Acad. Sci. USA 95: 1528-1533
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1528-1533
    • Lee, M.S.1    Craigie, R.2
  • 82
    • 0031720496 scopus 로고    scopus 로고
    • Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration
    • Cai M., Huang Y., Zheng R., Wei S. Q., Ghirlando R., Lee M. S. et al. (1998) Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration. Nat. Struct. Biol. 5: 903-909
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 903-909
    • Cai, M.1    Huang, Y.2    Zheng, R.3    Wei, S.Q.4    Ghirlando, R.5    Lee, M.S.6
  • 83
    • 0034255236 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) bridges DNa in a discrete, higher-order nucleoprotein complex
    • Zheng R., Ghirlando R., Lee M. S., Mizuuchi K., Krause M. and Craigie R. (2000) Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. Proc. Natl. Acad. Sci. USA 97: 8997-9002
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8997-9002
    • Zheng, R.1    Ghirlando, R.2    Lee, M.S.3    Mizuuchi, K.4    Krause, M.5    Craigie, R.6
  • 84
    • 19144372651 scopus 로고    scopus 로고
    • The characterization and localization of the mouse thymopoietin/lamina- associated polypeptide 2 gene and its alternatively spliced products
    • Berger R., Theodor L., Shoham J., Gokkel E., Brok-Simom F., Avraham K. B. et al. (1996) The characterization and localization of the mouse thymopoietin/lamina-associated polypeptide 2 gene and its alternatively spliced products. Genome Res. 6: 361-370
    • (1996) Genome Res. , vol.6 , pp. 361-370
    • Berger, R.1    Theodor, L.2    Shoham, J.3    Gokkel, E.4    Brok-Simom, F.5    Avraham, K.B.6
  • 85
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R., and Gerace L. (1993) Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73: 1267-1279
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 86
    • 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 K. L., Craigie R. and Clore G. M. (2001) 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. 20: 4399-4407
    • (2001) EMBO J. , vol.20 , pp. 4399-4407
    • Cai, M.1    Huang, Y.2    Ghirlando, R.3    Wilson, K.L.4    Craigie, R.5    Clore, G.M.6
  • 87
    • 0035193241 scopus 로고    scopus 로고
    • Nuclear envelope and nuclear matrix: Interactions and dynamics
    • Vlcek S., Dechat T. and Foisner R. (2001) Nuclear envelope and nuclear matrix: interactions and dynamics. Cell. Mol. Life Sci. 58: 1758-1765
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1758-1765
    • Vlcek, S.1    Dechat, T.2    Foisner, R.3
  • 88
    • 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. and Collas P (2003) HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication. J. Cell Biol. 160: 177-188
    • (2003) J. Cell Biol. , vol.160 , pp. 177-188
    • Martins, S.1    Eikvar, S.2    Furukawa, K.3    Collas, P.4
  • 89
    • 0032541346 scopus 로고    scopus 로고
    • Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics
    • Dechat T., Gotzmann J., Stockinger A., Harris C. A., Talle M. A., Siekierka J. J. et al. (1998) Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics. EMBO J. 17: 4887-4902
    • (1998) EMBO J. , vol.17 , pp. 4887-4902
    • Dechat, T.1    Gotzmann, J.2    Stockinger, A.3    Harris, C.A.4    Talle, M.A.5    Siekierka, J.J.6
  • 91
    • 0033570904 scopus 로고    scopus 로고
    • Functional diversity of LAP2alpha and LAP2beta in postmitotic chromosome association is caused by an alpha-specific nuclear targeting domain
    • Vlcek S., Just H., Dechat T and Foisner R. (1999) Functional diversity of LAP2alpha and LAP2beta in postmitotic chromosome association is caused by an alpha-specific nuclear targeting domain. EMBO J. 18: 6370-6384
    • (1999) EMBO J. , vol.18 , pp. 6370-6384
    • Vlcek, S.1    Just, H.2    Dechat, T.3    Foisner, R.4
  • 92
    • 0035831041 scopus 로고    scopus 로고
    • Lamins and disease: Insights into nuclear infrastructure
    • Wilson K. L., Zastrow M. S. and Lee K. K. (2001 ) Lamins and disease: insights into nuclear infrastructure. Cell 104: 647-650
    • (2001) Cell , vol.104 , pp. 647-650
    • Wilson, K.L.1    Zastrow, M.S.2    Lee, K.K.3
  • 93
    • 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
  • 94
    • 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. et al. (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
  • 95
    • 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. and 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
  • 96
    • 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., Kendrick-Jones J. and 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.1    Kendrick-Jones, J.2    Ellis, J.A.3
  • 98
    • 0036899615 scopus 로고    scopus 로고
    • The nuclear lamina and inherited disease
    • Worman H. J. and Courvalin J. C. (2002) The nuclear lamina and inherited disease. Trends Cell Biol. 12: 591-598
    • (2002) Trends Cell Biol. , vol.12 , pp. 591-598
    • Worman, H.J.1    Courvalin, J.C.2
  • 99
    • 0036500323 scopus 로고    scopus 로고
    • The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans
    • Gruenbaum Y., Lee K. K., Liu J., Cohen M. and Wilson K. L. (2002) The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans. J. Cell Sci. 115: 923-929
    • (2002) J. Cell Sci. , vol.115 , pp. 923-929
    • Gruenbaum, Y.1    Lee, K.K.2    Liu, J.3    Cohen, M.4    Wilson, K.L.5
  • 100
    • 0026011247 scopus 로고
    • The Drosophila maternal-effect gene fs(1)Ya encodes a cell cycle-dependent nuclear envelope component required for embryonic mitosis
    • Lin H. F. and Wolfner M. F. (1991) The Drosophila maternal-effect gene fs(1)Ya encodes a cell cycle-dependent nuclear envelope component required for embryonic mitosis. Cell 64: 49-62
    • (1991) Cell , vol.64 , pp. 49-62
    • Lin, H.F.1    Wolfner, M.F.2
  • 101
    • 0031862732 scopus 로고    scopus 로고
    • Interactions among Drosophila nuclear envelope proteins lamin, otefin and YA
    • Goldberg M., Lu H., Stuurman N., Ashery Padan R., Weiss A. M., Yu J. et al. (1998) Interactions among Drosophila nuclear envelope proteins lamin, otefin and YA. Mol. Cell. Biol. 18: 4315-4323
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4315-4323
    • Goldberg, M.1    Lu, H.2    Stuurman, N.3    Ashery Padan, R.4    Weiss, A.M.5    Yu, J.6
  • 102
    • 0030907906 scopus 로고    scopus 로고
    • The developmentally regulated Drosophila embryonic nuclear lamina protein 'Young Arrest' (fs(1)ya) is capable of associating with chromatin
    • Lopez J. M. and Wolfner M. F. (1997) The developmentally regulated Drosophila embryonic nuclear lamina protein 'Young Arrest' (fs(1)ya) is capable of associating with chromatin. J. Cell Sci. 110: 643-651
    • (1997) J. Cell Sci. , vol.110 , pp. 643-651
    • Lopez, J.M.1    Wolfner, M.F.2
  • 103
    • 0036177772 scopus 로고    scopus 로고
    • The Drosophila nuclear lamina protein YA binds to DNA and histone H2B with four domains
    • Yu J. and Wolfner M. F. (2002) The Drosophila nuclear lamina protein YA binds to DNA and histone H2B with four domains. Mol. Biol. Cell 13: 558-569
    • (2002) Mol. Biol. Cell , vol.13 , pp. 558-569
    • Yu, J.1    Wolfner, M.F.2
  • 104
    • 0025924582 scopus 로고
    • A complex containing p34cdc2 and cyclin B phosphorylates the nuclear lamin and disassembles nuclei of clam oocytes in vitro
    • Dessev G., Iovcheva D. C., Bischoff J. R., Beach D. and Goldman R. (1991) A complex containing p34cdc2 and cyclin B phosphorylates the nuclear lamin and disassembles nuclei of clam oocytes in vitro. J. Cell Biol. 112: 523-533
    • (1991) J. Cell Biol. , vol.112 , pp. 523-533
    • Dessev, G.1    Iovcheva, D.C.2    Bischoff, J.R.3    Beach, D.4    Goldman, R.5
  • 105
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin a that prevent nuclear lamina disassembly in mitosis
    • Heald R. and McKeon F. (1990) Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 61: 579-589
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 106
    • 0029116778 scopus 로고
    • Interphase phosphorylation of the Drosophila nuclear lamin: Site-mapping using a monoclonal antibody
    • Stuurman N., Maus N. and Fisher P. A. (1995) Interphase phosphorylation of the Drosophila nuclear lamin: site-mapping using a monoclonal antibody. J. Cell Sci. 108: 3137-3144
    • (1995) J. Cell Sci. , vol.108 , pp. 3137-3144
    • Stuurman, N.1    Maus, N.2    Fisher, P.A.3
  • 107
    • 0036424455 scopus 로고    scopus 로고
    • In vivo phosphorylation of Drosophila melanogaster nuclear lamins during both interphase and mitosis
    • Rzepecki R. and Fisher P. A. (2002) In vivo phosphorylation of Drosophila melanogaster nuclear lamins during both interphase and mitosis. Cell. Mol. Biol. Lett. 7: 859-876
    • (2002) Cell. Mol. Biol. Lett. , vol.7 , pp. 859-876
    • Rzepecki, R.1    Fisher, P.A.2
  • 108
    • 0036185987 scopus 로고    scopus 로고
    • The binding of lamin B receptor to chromatin is regulated by phosphorylation in the RS region
    • Takano M., Takeuchi M., Ito H., Furukawa K., Sugimoto K., Omata S. et al. (2002) The binding of lamin B receptor to chromatin is regulated by phosphorylation in the RS region. Eur. J. Biochem. 269: 943-953
    • (2002) Eur. J. Biochem. , vol.269 , pp. 943-953
    • Takano, M.1    Takeuchi, M.2    Ito, H.3    Furukawa, K.4    Sugimoto, K.5    Omata, S.6
  • 109
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R. and Gerace L. (1993) Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73: 1267-1279
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 110
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M., O'Carroll D., Rea S., Mechtler K. and Jenuwein T. (2001) Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410: 116-120
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 111
    • 0035253606 scopus 로고    scopus 로고
    • The spatial organization of human chromosomes within the nuclei of normal and emerin-mutant cells
    • Boyle S., Gilchrist S., Bridger J., Mahy N., Ellis J. and Bickmore W. (2001) The spatial organization of human chromosomes within the nuclei of normal and emerin-mutant cells. Hum. Mol. Genet. 10: 211-219
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 211-219
    • Boyle, S.1    Gilchrist, S.2    Bridger, J.3    Mahy, N.4    Ellis, J.5    Bickmore, W.6
  • 112
    • 0022544604 scopus 로고
    • The relative intranuclear positions of Barr bodies in XXX non-transformed human fibroblasts
    • Belmont A. S., Bignone F. and Ts'o P. O. (1986) The relative intranuclear positions of Barr bodies in XXX non-transformed human fibroblasts. Exp. Cell Res. 165: 165-179
    • (1986) Exp. Cell Res. , vol.165 , pp. 165-179
    • Belmont, A.S.1    Bignone, F.2    Ts'o, P.O.3
  • 113
    • 0032929777 scopus 로고    scopus 로고
    • Heterochromatin
    • Hennig W. (1999) Heterochromatin. Chromosoma 108: 1-9
    • (1999) Chromosoma , vol.108 , pp. 1-9
    • Hennig, W.1
  • 114
    • 0029943141 scopus 로고    scopus 로고
    • Perturbation of nuclear architecture by long-distance chromosome interactions
    • Dernburg A. F., Broman K. W., Fung J. C., Marshall W. F., Philips J., Agard D. A. et al. (1996) Perturbation of nuclear architecture by long-distance chromosome interactions. Cell 85: 745-759
    • (1996) Cell , vol.85 , pp. 745-759
    • Dernburg, A.F.1    Broman, K.W.2    Fung, J.C.3    Marshall, W.F.4    Philips, J.5    Agard, D.A.6
  • 115
    • 0033615636 scopus 로고    scopus 로고
    • A functional enhancer suppresses silencing of a transgene and prevents its localization close to centrometric heterochromatin
    • Francastel C., Walters M. C., Groudine M. and Martin D. I. (1999) A functional enhancer suppresses silencing of a transgene and prevents its localization close to centrometric heterochromatin. Cell 99: 259-269
    • (1999) Cell , vol.99 , pp. 259-269
    • Francastel, C.1    Walters, M.C.2    Groudine, M.3    Martin, D.I.4
  • 116
    • 0035150980 scopus 로고    scopus 로고
    • Interphase movements of a DNA chromosome region modulated by VP16 transcriptional activator
    • Tumbar T. and Belmont A. S. (2001) Interphase movements of a DNA chromosome region modulated by VP16 transcriptional activator. Nat. Cell Biol. 3: 134-139
    • (2001) Nat. Cell Biol. , vol.3 , pp. 134-139
    • Tumbar, T.1    Belmont, A.S.2
  • 117
    • 0032490917 scopus 로고    scopus 로고
    • Perinuclear localization of chromatin facilitates transcriptional silencing
    • Andrulis E. D., Neiman A. M., Zappulla D. C. and Sternglanz R. (1998) Perinuclear localization of chromatin facilitates transcriptional silencing. Nature 394: 592-595
    • (1998) Nature , vol.394 , pp. 592-595
    • Andrulis, E.D.1    Neiman, A.M.2    Zappulla, D.C.3    Sternglanz, R.4
  • 118
  • 119
    • 0036123996 scopus 로고    scopus 로고
    • Nuclear organization and silencing: Putting things in their place
    • Hediger F. and Gasser S. M. (2002) Nuclear organization and silencing: putting things in their place. Nat. Cell Biol. 4: E53-E55
    • (2002) Nat. Cell Biol. , vol.4
    • Hediger, F.1    Gasser, S.M.2
  • 121
    • 0035696932 scopus 로고    scopus 로고
    • Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy
    • Raharjo W. H., Enarson P., Sullivan T., Stewart C. L. and Burke B. (2001) Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy. J. Cell Sci. 114: 4447-4457
    • (2001) J. Cell Sci. , vol.114 , pp. 4447-4457
    • Raharjo, W.H.1    Enarson, P.2    Sullivan, T.3    Stewart, C.L.4    Burke, B.5
  • 122
    • 0037225049 scopus 로고    scopus 로고
    • Expression of lamin a mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy
    • Favreau C., Dubosclard E., Ostlund C., Vigouroux C., Capeau J., Wehnert M. et al. (2003) Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy. Exp. Cell Res. 282: 14-23
    • (2003) Exp. Cell Res. , vol.282 , pp. 14-23
    • Favreau, C.1    Dubosclard, E.2    Ostlund, C.3    Vigouroux, C.4    Capeau, J.5    Wehnert, M.6
  • 123
    • 0034842046 scopus 로고    scopus 로고
    • A nuclear lamin is required for cytoplasmic organization and egg polarity in Drosophila
    • Guillemin K., Williams T. and Krasnow M. A. (2001) A nuclear lamin is required for cytoplasmic organization and egg polarity in Drosophila. Nat. Cell Biol. 3: 848-851
    • (2001) Nat. Cell Biol. , vol.3 , pp. 848-851
    • Guillemin, K.1    Williams, T.2    Krasnow, M.A.3
  • 124
    • 0026775180 scopus 로고
    • The germ cell-less gene product: A posteriorly localized component necessary for germ cell development in Drosophila
    • Jongens T. A., Hay B., Jan L. Y. and Jan Y. N. (1992) The germ cell-less gene product: a posteriorly localized component necessary for germ cell development in Drosophila. Cell 70: 569-584
    • (1992) Cell , vol.70 , pp. 569-584
    • Jongens, T.A.1    Hay, B.2    Jan, L.Y.3    Jan, Y.N.4
  • 125
    • 0034177686 scopus 로고    scopus 로고
    • Identification of a mouse germ cell-less homologue with conserved activity in Drosophila
    • Leatherman J. L., Kaestner K. H. and Jongens T. A. (2000) Identification of a mouse germ cell-less homologue with conserved activity in Drosophila. Mech. Dev. 92: 145-153
    • (2000) Mech. Dev. , vol.92 , pp. 145-153
    • Leatherman, J.L.1    Kaestner, K.H.2    Jongens, T.A.3
  • 126
    • 0028071622 scopus 로고
    • Germ cell-less encodes a cell type-specific nuclear pore-associated protein and functions early in the germ-cell specification pathway of Drosophila
    • Jongens T. A., Ackerman L. D., Swedlow J. R., Jan L. Y. and Jan Y. N. (1994) Germ cell-less encodes a cell type-specific nuclear pore-associated protein and functions early in the germ-cell specification pathway of Drosophila. Genes Dev. 8: 2123-2136
    • (1994) Genes Dev. , vol.8 , pp. 2123-2136
    • Jongens, T.A.1    Ackerman, L.D.2    Swedlow, J.R.3    Jan, L.Y.4    Jan, Y.N.5
  • 127
    • 0034777991 scopus 로고    scopus 로고
    • Nuclear membrane protein, LAP2β, mediates transcriptional repression alone and together with its binding partner GCL (germ cell-less)
    • Nili E., Cojocarul G. S., Kalma Y., Ginsberg D., Copeland N. G., Gilbert D. J. et al. (2001) Nuclear membrane protein, LAP2β, mediates transcriptional repression alone and together with its binding partner GCL (germ cell-less). J. Cell Sci. 114: 3297-3307
    • (2001) J. Cell Sci. , vol.114 , pp. 3297-3307
    • Nili, E.1    Cojocarul, G.S.2    Kalma, Y.3    Ginsberg, D.4    Copeland, N.G.5    Gilbert, D.J.6
  • 128
    • 0033521615 scopus 로고    scopus 로고
    • Integration of a growth-suppressing BTB/POZ domain protein with the DP component of the E2F transcription factor
    • de la Luna S., Allen K. E., Mason S. L. and La Thangue N. B. (1999) Integration of a growth-suppressing BTB/POZ domain protein with the DP component of the E2F transcription factor. EMBO J. 18: 212-228
    • (1999) EMBO J. , vol.18 , pp. 212-228
    • De La Luna, S.1    Allen, K.E.2    Mason, S.L.3    La Thangue, N.B.4
  • 129
    • 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. and 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
  • 130
    • 0344671608 scopus 로고    scopus 로고
    • Functions of the retinoblastoma protein
    • Kaelin W. G. Jr (1999) Functions of the retinoblastoma protein. Bioessays 21: 950-958
    • (1999) Bioessays , vol.21 , pp. 950-958
    • Kaelin W.G., Jr.1
  • 131
    • 0027976913 scopus 로고
    • The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein
    • Mancini M. A., Shan B., Nickerson J. A., Penman S. and Lee W. H. (1994) The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein. Proc. Natl. Acad. Sci. USA 91: 418-422
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 418-422
    • Mancini, M.A.1    Shan, B.2    Nickerson, J.A.3    Penman, S.4    Lee, W.H.5
  • 132
    • 0028064990 scopus 로고
    • Complex formation between lamin a and the retinoblastoma gene product: Identification of the domain on lamin a required for its interaction
    • Ozaki T., Saijo M., Murakami K., Enomoto H., Taya Y. and Sakiyama S. (1994) Complex formation between lamin A and the retinoblastoma gene product: identification of the domain on lamin A required for its interaction. Oncogene 9: 2649-2653
    • (1994) Oncogene , vol.9 , pp. 2649-2653
    • Ozaki, T.1    Saijo, M.2    Murakami, K.3    Enomoto, H.4    Taya, Y.5    Sakiyama, S.6
  • 133
    • 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. and 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
  • 134
    • 0036848357 scopus 로고    scopus 로고
    • In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin P/C
    • Dreuillet C., Tillit J., Kress M. and Ernoult-Lange M. (2002) In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin P/C. Nucleic Acids Res. 30: 4634-4642
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4634-4642
    • Dreuillet, C.1    Tillit, J.2    Kress, M.3    Ernoult-Lange, M.4
  • 135
    • 0025159482 scopus 로고
    • A gene that encodes a protein consisting solely of zinc finger domains is preferentially expressed in transformed mouse cells
    • Ernoult-Lange M., Kress M. and Hamer D. (1990) A gene that encodes a protein consisting solely of zinc finger domains is preferentially expressed in transformed mouse cells. Mol. Cell. Biol. 10: 418-421
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 418-421
    • Ernoult-Lange, M.1    Kress, M.2    Hamer, D.3
  • 136
    • 0030948576 scopus 로고    scopus 로고
    • Human and mouse MOK2 proteins are associated with nuclear ribonucleoprotein components and bind specifically to RNA and DNA through their zinc finger domains
    • Arranz V., Harper F., Florentin Y., Puvion E., Kress M. and Ernoult-Lange M. (1997) Human and mouse MOK2 proteins are associated with nuclear ribonucleoprotein components and bind specifically to RNA and DNA through their zinc finger domains. Mol. Cell. Biol. 17: 2116-2126
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2116-2126
    • Arranz, V.1    Harper, F.2    Florentin, Y.3    Puvion, E.4    Kress, M.5    Ernoult-Lange, M.6
  • 137
    • 0034059075 scopus 로고    scopus 로고
    • Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy
    • Cao H. and Hegele R. A. (2000) Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy. Hum. Mol. Genet. 9: 109-112
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 109-112
    • Cao, H.1    Hegele, R.A.2
  • 139
    • 0036251153 scopus 로고    scopus 로고
    • SREBPs: Activators of the complete program of cholesterol and fatty acid synthesis in the liver
    • Horton J. D., Goldstein J. L. and Brown M. S. (2002) SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver. J. Clin. Invest. 109: 1125-1131
    • (2002) J. Clin. Invest. , vol.109 , pp. 1125-1131
    • Horton, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 140
    • 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. and 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
  • 141
    • 0037446880 scopus 로고    scopus 로고
    • MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in C. elegans
    • Liu J., Lee K. K., Segura-Totten M., Neufeld E., Wilson K. L., and Gruenbaum Y. (2003) MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in C. elegans. Proc. Natl. Acad. Sci. USA 15: 4598-4603
    • (2003) Proc. Natl. Acad. Sci. USA , vol.15 , pp. 4598-4603
    • Liu, J.1    Lee, K.K.2    Segura-Totten, M.3    Neufeld, E.4    Wilson, K.L.5    Gruenbaum, Y.6
  • 142
    • 0037959860 scopus 로고    scopus 로고
    • XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos
    • Osada S., Ohmori S. Y., and Taira M. (2003) XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos. Development 130: 1783-1794
    • (2003) Development , vol.130 , pp. 1783-1794
    • Osada, S.1    Ohmori, S.Y.2    Taira, M.3
  • 143
    • 0030681031 scopus 로고    scopus 로고
    • Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression
    • Imai S. I., Nishibayashi S., Takao K., Tomifuji M., Fujino T., Hasegawa M. et al. (1997) Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression. Mol. Biol. Cell 8: 2407-2419
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2407-2419
    • Imai, S.I.1    Nishibayashi, S.2    Takao, K.3    Tomifuji, M.4    Fujino, T.5    Hasegawa, M.6
  • 144
    • 0032483368 scopus 로고    scopus 로고
    • Glucose-dependent translocation of insulin promoter factor-1 (IPF-1) between the nuclear periphery and the nucleoplasm of single MIN6 beta-cells
    • Rafiq I., Kennedy H. J. and Rutter G. A. (1998) Glucose-dependent translocation of insulin promoter factor-1 (IPF-1) between the nuclear periphery and the nucleoplasm of single MIN6 beta-cells. J. Biol. Chem. 273: 23241-23247
    • (1998) J. Biol. Chem. , vol.273 , pp. 23241-23247
    • Rafiq, I.1    Kennedy, H.J.2    Rutter, G.A.3
  • 145
    • 0036809115 scopus 로고    scopus 로고
    • SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization
    • Ross S, Best J. L., Zon L. I. and Gill G. (2002) SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization. Mol. Cell. 10: 831-842
    • (2002) Mol. Cell. , vol.10 , pp. 831-842
    • Ross, S.1    Best, J.L.2    Zon, L.I.3    Gill, G.4
  • 146
    • 0032512832 scopus 로고    scopus 로고
    • The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding regionbut is distinct from its chromatin interaction domain
    • Furukawa K., Fritze C. E. and Gerace L. (1998) The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding regionbut is distinct from its chromatin interaction domain. J. Biol. Chem. 273: 4213-4219
    • (1998) J. Biol. Chem. , vol.273 , pp. 4213-4219
    • Furukawa, K.1    Fritze, C.E.2    Gerace, L.3
  • 147
    • 0031559831 scopus 로고    scopus 로고
    • Characterization of the chromatin binding activity of lamina-associated polypeptide (LAP) 2
    • Furukawa K., Glass C. and Kondo T. (1997) Characterization of the chromatin binding activity of lamina-associated polypeptide (LAP) 2. Biochem. Biophys. Res. Commun. 238: 240-246
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 240-246
    • Furukawa, K.1    Glass, C.2    Kondo, T.3


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