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Volumn 342, Issue 4, 2006, Pages 1040-1048

Emp is a component of the nuclear matrix of mammalian cells and undergoes dynamic rearrangements during cell division

Author keywords

Actin; Cytokinesis; Emp; Erythroblast; Macrophage; Mitosis; Nuclear actin; Nuclear matrix

Indexed keywords

ACTIN; NUCLEAR PROTEIN; PROTEIN EMP; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 33644884682     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.060     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0027971588 scopus 로고
    • The association of erythroblasts with macrophages promotes erythroid proliferation and maturation: A 30-kD heparin-binding protein is involved in this contact
    • M. Hanspal, and J.S. Hanspal The association of erythroblasts with macrophages promotes erythroid proliferation and maturation: a 30-kD heparin-binding protein is involved in this contact Blood 84 1994 3494 3504
    • (1994) Blood , vol.84 , pp. 3494-3504
    • Hanspal, M.1    Hanspal, J.S.2
  • 2
    • 0032532042 scopus 로고    scopus 로고
    • Molecular identification and functional characterization of a novel protein that mediates the attachment of erythroblasts to macrophages
    • M. Hanspal, Y. Smockova, and Q. Uong Molecular identification and functional characterization of a novel protein that mediates the attachment of erythroblasts to macrophages Blood 92 1998 2940 2950
    • (1998) Blood , vol.92 , pp. 2940-2950
    • Hanspal, M.1    Smockova, Y.2    Uong, Q.3
  • 3
    • 1442307960 scopus 로고    scopus 로고
    • Mechanism of protein sorting during erythroblast enucleation: Role of cytoskeletal connectivity
    • J.C.-M. Lee, J.A. Gimm, A.J. Lo, M.J. Koury, S.W. Krauss, N. Mohandas, and J.A. Chasis Mechanism of protein sorting during erythroblast enucleation: role of cytoskeletal connectivity Blood 103 2004 1912 1919
    • (2004) Blood , vol.103 , pp. 1912-1919
    • Lee, J.C.-M.1    Gimm, J.A.2    Lo, A.J.3    Koury, M.J.4    Krauss, S.W.5    Mohandas, N.6    Chasis, J.A.7
  • 4
    • 0024411243 scopus 로고
    • Sequence requirements for synthetic peptide-mediated translocation to the nucleus
    • D. Chelsky, R. Ralph, and G. Jonak Sequence requirements for synthetic peptide-mediated translocation to the nucleus Mol. Cell. Biol. 9 1989 2487 2492
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2487-2492
    • Chelsky, D.1    Ralph, R.2    Jonak, G.3
  • 5
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • D. He, J.A. Nickerson, and S. Penman Core filaments of the nuclear matrix J. Cell Biol. 110 1990 569 580
    • (1990) J. Cell Biol. , vol.110 , pp. 569-580
    • He, D.1    Nickerson, J.A.2    Penman, S.3
  • 6
    • 0024221204 scopus 로고
    • Visualization of a filamentous nucleoskeleton with a 23 nm axial repeat
    • D.A. Jackson, and P.R. Cook Visualization of a filamentous nucleoskeleton with a 23 nm axial repeat EMBO J. 7 1988 3667 3678
    • (1988) EMBO J. , vol.7 , pp. 3667-3678
    • Jackson, D.A.1    Cook, P.R.2
  • 7
    • 0021046130 scopus 로고
    • Actively transcribed genes are associated with the nuclear matrix
    • E.M. Ciejek, M.J. Tsai, and B.W. O'Malley Actively transcribed genes are associated with the nuclear matrix Nature (London) 306 1983 607 609
    • (1983) Nature (London) , vol.306 , pp. 607-609
    • Ciejek, E.M.1    Tsai, M.J.2    O'Malley, B.W.3
  • 8
    • 0026065461 scopus 로고
    • Preservation of specific RNA distribution within the chromatin-depleted nuclear substructure demonstrated by in situ hybridization coupled with biochemical fractionation
    • Y. Xing, and J.B. Lawrence Preservation of specific RNA distribution within the chromatin-depleted nuclear substructure demonstrated by in situ hybridization coupled with biochemical fractionation J. Cell Biol. 112 1991 1055 1063
    • (1991) J. Cell Biol. , vol.112 , pp. 1055-1063
    • Xing, Y.1    Lawrence, J.B.2
  • 10
    • 0016861690 scopus 로고
    • Nuclear protein matrix: Association with newly synthesized DNA
    • R. Berezney, and D.S. Coffey Nuclear protein matrix: association with newly synthesized DNA Science 189 1975 291
    • (1975) Science , vol.189 , pp. 291
    • Berezney, R.1    Coffey, D.S.2
  • 11
    • 0018858066 scopus 로고
    • A fixed site of DNA replication in eucaryotic cells
    • D.M. Pardoll, B. Vogelstein, and D.S. Coffey A fixed site of DNA replication in eucaryotic cells Cell 19 1980 527 536
    • (1980) Cell , vol.19 , pp. 527-536
    • Pardoll, D.M.1    Vogelstein, B.2    Coffey, D.S.3
  • 12
    • 0021360588 scopus 로고
    • Nuclear matrix DNA from chicken erythrocytes contains beta-globin gene sequences
    • P.C. Hentzen, J.H. Rho, and I. Bekhor Nuclear matrix DNA from chicken erythrocytes contains beta-globin gene sequences Proc. Natl. Acad. Sci. USA 81 1984 304 307
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 304-307
    • Hentzen, P.C.1    Rho, J.H.2    Bekhor, I.3
  • 13
    • 0020077227 scopus 로고
    • The ovalbumin gene is associated with the nuclear matrix of chicken oviduct cells
    • S.I. Robinson, B.D. Nelkin, and B. Vogelstein The ovalbumin gene is associated with the nuclear matrix of chicken oviduct cells Cell 28 1982 99 106
    • (1982) Cell , vol.28 , pp. 99-106
    • Robinson, S.I.1    Nelkin, B.D.2    Vogelstein, B.3
  • 14
    • 0022423297 scopus 로고
    • The association of transcribed genes with the nuclear matrix of Drosophila cells during heat shock
    • D. Small, B. Nelkin, and B. Vogelstein B The association of transcribed genes with the nuclear matrix of Drosophila cells during heat shock Nucleic Acids Res. 13 1985 2413 2431
    • (1985) Nucleic Acids Res. , vol.13 , pp. 2413-2431
    • Small, D.1    Nelkin, B.2    Vogelstein, B.B.3
  • 15
    • 0021702708 scopus 로고
    • Organization and modulation of nuclear lamina structure
    • L. Gerace, C. Comeau, and M. Benson Organization and modulation of nuclear lamina structure J. Cell Sci. Suppl. 1 1984 137 160
    • (1984) J. Cell Sci. , Issue.SUPPL. 1 , pp. 137-160
    • Gerace, L.1    Comeau, C.2    Benson, M.3
  • 16
    • 0023505969 scopus 로고
    • Nuclear lamin LI of Xenopus laevis: CDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily
    • G. Krohne, S.L. Wollin, F.D. McKeon, W.W. Franke, and M.W. Kirschner Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily EMBO J. 6 1987 3801 3808
    • (1987) EMBO J. , vol.6 , pp. 3801-3808
    • Krohne, G.1    Wollin, S.L.2    McKeon, F.D.3    Franke, W.W.4    Kirschner, M.W.5
  • 17
    • 0023032014 scopus 로고
    • CDNA sequencing of nuclear lamins a and C reveals primary and secondary structural homology to intermediate filament proteins
    • D.Z. Fisher, N. Chaudhary, and G. Blobel cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins Proc. Natl. Acad. Sci. USA 83 1986 6450 6454
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 18
    • 0040860278 scopus 로고
    • In situ localization of DNA topoisomerase II, a major polypeptide component of the Drosophila nuclear matrix fraction
    • M. Berrios, N. Osheroff, and P.A. Fisher In situ localization of DNA topoisomerase II, a major polypeptide component of the Drosophila nuclear matrix fraction Proc. Natl. Acad. Sci. USA 82 1985 4142 4146
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4142-4146
    • Berrios, M.1    Osheroff, N.2    Fisher, P.A.3
  • 19
    • 0021174889 scopus 로고
    • 2+/calmodulin-dependent protein kinases from the neuronal nuclear matrix and post-synaptic density are structurally related
    • 2+/calmodulin- dependent protein kinases from the neuronal nuclear matrix and post-synaptic density are structurally related Proc. Natl. Acad. Sci. USA 81 1984 4311 4315
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4311-4315
    • Sahyoun, N.1    Levine, H.2    Cuatrecasas, P.3
  • 20
    • 0019132556 scopus 로고
    • Human-specific nuclear protein that associates with the polar region of the mitotic apparatus: Distribution in a human/hamster hybrid cell
    • B. Lyderson, and D. Petijohn Human-specific nuclear protein that associates with the polar region of the mitotic apparatus: distribution in a human/hamster hybrid cell Cell 22 1980 489 499
    • (1980) Cell , vol.22 , pp. 489-499
    • Lyderson, B.1    Petijohn, D.2
  • 21
    • 0027978833 scopus 로고
    • Localization of NuMA protein isoforms in the nuclear matrix of mammalian cells
    • C. Zeng, D. He, and B.R. Brinkley Localization of NuMA protein isoforms in the nuclear matrix of mammalian cells Cell Motil. Cytoskeleton. 29 1994 167 176
    • (1994) Cell Motil. Cytoskeleton. , vol.29 , pp. 167-176
    • Zeng, C.1    He, D.2    Brinkley, B.R.3
  • 22
    • 0141703273 scopus 로고    scopus 로고
    • Nuclear actin and protein 4.1: Essential interactions during nuclear assembly in vitro
    • S.W. Krauss, C. Chen, S. Penman, and R. Heald Nuclear actin and protein 4.1: essential interactions during nuclear assembly in vitro Proc. Natl. Acad. Sci. USA 100 2003 10752 10757
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10752-10757
    • Krauss, S.W.1    Chen, C.2    Penman, S.3    Heald, R.4
  • 23
    • 0017716157 scopus 로고
    • Diffusible and bound actin nuclei of Xenopus laevis oocytes
    • T.G. Clark, and R.W. Merriam Diffusible and bound actin nuclei of Xenopus laevis oocytes Cell 12 1977 883 891
    • (1977) Cell , vol.12 , pp. 883-891
    • Clark, T.G.1    Merriam, R.W.2
  • 24
    • 0020162216 scopus 로고
    • The nuclear matrix: Three-dimensional architecture and protein composition
    • D.G. Capco, K.M. Wan, and S. Penman The nuclear matrix: three-dimensional architecture and protein composition Cell 29 1982 847 858
    • (1982) Cell , vol.29 , pp. 847-858
    • Capco, D.G.1    Wan, K.M.2    Penman, S.3
  • 25
    • 0022416568 scopus 로고
    • Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells
    • H. Nakasayu, and K. Ueda Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells Cell Struct. Funct. 10 1985 305 309
    • (1985) Cell Struct. Funct. , vol.10 , pp. 305-309
    • Nakasayu, H.1    Ueda, K.2
  • 26
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin remodeling
    • I.A. Olave, S.L. Reck-Peterson, and G.R. Crabtree Nuclear actin and actin-related proteins in chromatin remodeling Annu. Rev. Biochem. 71 2002 755 781
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 29
    • 0035968304 scopus 로고    scopus 로고
    • A new spectrin, beta IV, has a major truncated isoform that associates with promyelocytic leukemia protein nuclear bodies and the nuclear matrix
    • W.T. Tse, J. Tang, O. Jin, C. Korsgren, K.M. John, A.L. Kung, B. Gwynn, L.L. Peters, and S.E. Lux A new spectrin, beta IV, has a major truncated isoform that associates with promyelocytic leukemia protein nuclear bodies and the nuclear matrix J. Biol. Chem. 276 2001 23974 23985
    • (2001) J. Biol. Chem. , vol.276 , pp. 23974-23985
    • Tse, W.T.1    Tang, J.2    Jin, O.3    Korsgren, C.4    John, K.M.5    Kung, A.L.6    Gwynn, B.7    Peters, L.L.8    Lux, S.E.9
  • 30
    • 0037515668 scopus 로고    scopus 로고
    • Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells
    • A. Pendelton, B. Pope, A. Weeds, and A. Koffer Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells J. Biol. Chem. 278 2003 14394 14400
    • (2003) J. Biol. Chem. , vol.278 , pp. 14394-14400
    • Pendelton, A.1    Pope, B.2    Weeds, A.3    Koffer, A.4
  • 32
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • J.V. Frangioni, and B.G. Neel Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins Anal. Biochem. 210 1993 179 187
    • (1993) Anal. Biochem. , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature (London) 227 1970 680 685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehlin, and J. Gordon Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications Proc. Natl. Acad. Sci. USA 76 1979 4350 4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 35
    • 0033381420 scopus 로고    scopus 로고
    • Lamins and lamin-binding proteins in functional chromatin organization
    • J. Gotzmann, and R. Foisner Lamins and lamin-binding proteins in functional chromatin organization Crit. Rev. Eukaryot. Gene Expr. 9 1999 257 265
    • (1999) Crit. Rev. Eukaryot. Gene Expr. , vol.9 , pp. 257-265
    • Gotzmann, J.1    Foisner, R.2
  • 36
    • 0024565325 scopus 로고
    • TPA-induced differentiation and adhesion of U937 cells: Changes in ultrastructure, cytoskeletal organization and expression of cell surface antigens
    • R. Hass, H. Bartels, N. Topley, M. Hadam, L. Kohler, M. Goppelt-Strube, and K. Resch TPA-induced differentiation and adhesion of U937 cells: changes in ultrastructure, cytoskeletal organization and expression of cell surface antigens Eur. J. Cell Biol. 48 1989 282 293
    • (1989) Eur. J. Cell Biol. , vol.48 , pp. 282-293
    • Hass, R.1    Bartels, H.2    Topley, N.3    Hadam, M.4    Kohler, L.5    Goppelt-Strube, M.6    Resch, K.7
  • 37
    • 0025115231 scopus 로고
    • Factor required for mammalian spliceosome assembly is localized to discrete regions in the nucleus
    • X.D. Fu, and T. Maniatis Factor required for mammalian spliceosome assembly is localized to discrete regions in the nucleus Nature (London) 343 1990 437 441
    • (1990) Nature (London) , vol.343 , pp. 437-441
    • Fu, X.D.1    Maniatis, T.2
  • 38
    • 0035795419 scopus 로고    scopus 로고
    • Actin bound to the heterogeneous nuclear ribonucleoprotein hrp36 is associated with Balbiani ring mRNA from the gene to polysomes
    • P. Percipalle, J. Zhao, B. Pope, A. Weeds, U. Lindbergh, and B. Daneholt Actin bound to the heterogeneous nuclear ribonucleoprotein hrp36 is associated with Balbiani ring mRNA from the gene to polysomes J. Cell Biol. 153 2001 229 236
    • (2001) J. Cell Biol. , vol.153 , pp. 229-236
    • Percipalle, P.1    Zhao, J.2    Pope, B.3    Weeds, A.4    Lindbergh, U.5    Daneholt, B.6
  • 39
    • 0022200026 scopus 로고
    • Association of rapidly-labelled RNAs with actin in nuclear matrix from mouse L5178Y cells
    • H. Nakayasu, and K. Ueda Association of rapidly-labelled RNAs with actin in nuclear matrix from mouse L5178Y cells Exp. Cell Res. 160 1985 319 330
    • (1985) Exp. Cell Res. , vol.160 , pp. 319-330
    • Nakayasu, H.1    Ueda, K.2
  • 40
    • 0023411029 scopus 로고
    • Cytochalasin B selectively releases ovalbumin mRNA precursors but not the mature ovalbumin mRNA from hen oviduct nuclear matrix
    • H.C. Schroder, D. Troltsch, R. Wenger, M. Bachman, B. Diehl-Seifert, and W.E.G. Muller Cytochalasin B selectively releases ovalbumin mRNA precursors but not the mature ovalbumin mRNA from hen oviduct nuclear matrix Eur. J. Biochem. 167 1987 239 245
    • (1987) Eur. J. Biochem. , vol.167 , pp. 239-245
    • Schroder, H.C.1    Troltsch, D.2    Wenger, R.3    Bachman, M.4    Diehl-Seifert, B.5    Muller, W.E.G.6
  • 41
    • 0027319999 scopus 로고
    • Distribution of snRNPs, splicing factor SC-35 and actin in interphase nuclei: Immunocytochemical evidence for differential distribution during changes in functional states
    • D.J. Sahlas, K. Milankov, P.C. Park, and U. De Boni Distribution of snRNPs, splicing factor SC-35 and actin in interphase nuclei: immunocytochemical evidence for differential distribution during changes in functional states J. Cell Sci. 105 1993 347 357
    • (1993) J. Cell Sci. , vol.105 , pp. 347-357
    • Sahlas, D.J.1    Milankov, K.2    Park, P.C.3    De Boni, U.4
  • 42
    • 0034110276 scopus 로고    scopus 로고
    • Rev-dependent association of the intron-containing HIV-1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin-B
    • T. Kimura, I. Hashimoto, A. Yamamoto, M. Nishikawa, and J.I. Fijisawa Rev-dependent association of the intron-containing HIV-1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin-B Genes Cells 5 2000 289 307
    • (2000) Genes Cells , vol.5 , pp. 289-307
    • Kimura, T.1    Hashimoto, I.2    Yamamoto, A.3    Nishikawa, M.4    Fijisawa, J.I.5
  • 44
    • 0014260928 scopus 로고
    • Nuclear elimination from the normoblast of fetal guinea pig liver as studied with electron microscopy and serial sectioning techniques
    • F.R. Campbell Nuclear elimination from the normoblast of fetal guinea pig liver as studied with electron microscopy and serial sectioning techniques Anal. Rec. 160 1968 539 553
    • (1968) Anal. Rec. , vol.160 , pp. 539-553
    • Campbell, F.R.1
  • 45
    • 0019348113 scopus 로고
    • A reevaluation of the process of enucleation in mammalian erythroid cells
    • E.A. Repasky, and B.S. Eckert A reevaluation of the process of enucleation in mammalian erythroid cells Prog. Clin. Biol. Res. 55 1981 679 692
    • (1981) Prog. Clin. Biol. Res. , vol.55 , pp. 679-692
    • Repasky, E.A.1    Eckert, B.S.2
  • 46
    • 0014140648 scopus 로고
    • The mechanism of denucleation in circulating erythroblasts
    • C.F. Simpson, and J.M. Kling The mechanism of denucleation in circulating erythroblasts J. Cell Biol. 35 1967 237 245
    • (1967) J. Cell Biol. , vol.35 , pp. 237-245
    • Simpson, C.F.1    Kling, J.M.2
  • 47
    • 0014098369 scopus 로고
    • An electron microscopic study of nuclear elimination from the late erythroblast
    • E. Skutelsky, and D. Danon An electron microscopic study of nuclear elimination from the late erythroblast J. Cell Biol. 33 1967 625 635
    • (1967) J. Cell Biol. , vol.33 , pp. 625-635
    • Skutelsky, E.1    Danon, D.2
  • 48
    • 0014807460 scopus 로고
    • Comparative study of nuclear expulsion from the late erythroblast and cytokinesis
    • E. Skutelsky, and D. Danon Comparative study of nuclear expulsion from the late erythroblast and cytokinesis Exp. Cell Res. 60 1970 427 436
    • (1970) Exp. Cell Res. , vol.60 , pp. 427-436
    • Skutelsky, E.1    Danon, D.2
  • 49
    • 0015028065 scopus 로고
    • Actin-like filaments in the cleavage furrow of newt egg
    • M.M. Perry, H.A. John, and N.S. Thomas Actin-like filaments in the cleavage furrow of newt egg Exp. Cell Res. 65 1971 249 253
    • (1971) Exp. Cell Res. , vol.65 , pp. 249-253
    • Perry, M.M.1    John, H.A.2    Thomas, N.S.3
  • 50
    • 0011014320 scopus 로고
    • Actin in dividing cells: Contractile ring filaments bind heavy meromyosin
    • T.E. Schroeder Actin in dividing cells: contractile ring filaments bind heavy meromyosin Proc. Natl. Acad. Sci. USA 70 1973 1688 1692
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 1688-1692
    • Schroeder, T.E.1


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