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Volumn 5, Issue 5, 2004, Pages 410-415

Actin up in the nucleus

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; DEOXYRIBONUCLEASE;

EID: 2342510389     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1370     Document Type: Review
Times cited : (222)

References (61)
  • 1
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D. G. & Nelson, W. J. Origins of cell polarity. Cell 84, 335-344 (1996).
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 2
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin remodeling
    • Olave, I. A., Reck-Peterson, S. L. & Crabtree, G. R. Nuclear actin and actin-related proteins in chromatin remodeling. Annu. Rev. Biochem. 71, 755-781 (2002).
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 4
    • 0018601589 scopus 로고
    • An actin filament matrix in hand-isolated nuclei of X. laevis oocytes
    • Clark, T. G. & Rosenbaum, J. L. An actin filament matrix in hand-isolated nuclei of X. laevis oocytes. Cell 18, 1101-1108 (1979).
    • (1979) Cell , vol.18 , pp. 1101-1108
    • Clark, T.G.1    Rosenbaum, J.L.2
  • 5
    • 0017716157 scopus 로고
    • Diffusible and bound actin nuclei of Xenopus laevis oocytes
    • Clark, T. G. & Merriam, R. W. Diffusible and bound actin nuclei of Xenopus laevis oocytes. Cell 12, 883-891, (1977).
    • (1977) Cell , vol.12 , pp. 883-891
    • Clark, T.G.1    Merriam, R.W.2
  • 6
    • 0020702214 scopus 로고
    • Association of actin with the nuclear matrix from bovine lymphocytes
    • Nakayasu, H. & Ueda, K. Association of actin with the nuclear matrix from bovine lymphocytes. Exp. Cell Res. 143, 55-62 (1983).
    • (1983) Exp. Cell Res. , vol.143 , pp. 55-62
    • Nakayasu, H.1    Ueda, K.2
  • 7
    • 0037039159 scopus 로고    scopus 로고
    • Directed proteomic analysis of the human nucleolus
    • Andersen, J. S. et al. Directed proteomic analysis of the human nucleolus. Curr. Biol. 12, 1-11 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1-11
    • Andersen, J.S.1
  • 8
    • 0022416568 scopus 로고
    • Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells
    • Nakayasu, H. & Ueda, K. Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells. Cell Struct. Funct. 10, 305-309 (1985).
    • (1985) Cell Struct. Funct. , vol.10 , pp. 305-309
    • Nakayasu, H.1    Ueda, K.2
  • 9
    • 0026062542 scopus 로고
    • Complexing of actin and other nuclear proteins to DNA by cis-diamminedichloroplatinum(II) and chromium compounds
    • Miller, C. A. III, Cohen, M. D. & Costa, M. Complexing of actin and other nuclear proteins to DNA by cis-diamminedichloroplatinum(II) and chromium compounds. Carcinogenesis 12, 269-276 (1991).
    • (1991) Carcinogenesis , vol.12 , pp. 269-276
    • Miller III, C.A.1    Cohen, M.D.2    Costa, M.3
  • 10
    • 0032957520 scopus 로고    scopus 로고
    • Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody
    • Gonsior, S. M. et al. Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody. J. Cell Sci. 112, 797-809 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 797-809
    • Gonsior, S.M.1
  • 11
    • 0018428638 scopus 로고
    • Nuclear actin bundles in Amoeba, Dictyostelium and human HeLa cells induced by dimethyl sulfoxide
    • Fukui, Y. & Katsumaru, H. Nuclear actin bundles in Amoeba, Dictyostelium and human HeLa cells induced by dimethyl sulfoxide. Exp. Cell Res. 120, 451-455 (1979).
    • (1979) Exp. Cell Res. , vol.120 , pp. 451-455
    • Fukui, Y.1    Katsumaru, H.2
  • 12
    • 0037515668 scopus 로고    scopus 로고
    • Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells
    • Pendleton, A., Pope, B., Weeds, A. & Koffer, A. Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells. J. Biol. Chem. 278, 14394-14400 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14394-14400
    • Pendleton, A.1    Pope, B.2    Weeds, A.3    Koffer, A.4
  • 13
    • 0024429070 scopus 로고
    • Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin
    • Ohta, Y., Nishida, E., Sakai, H. & Miyamoto, E. Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin. J. Biol. Chem. 264, 16143-16146 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 16143-16146
    • Ohta, Y.1    Nishida, E.2    Sakai, H.3    Miyamoto, E.4
  • 14
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein
    • Wada, A., Fukuda, M., Mishima, M. & Nishida, E. Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J. 17, 1635-1641 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 15
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6: A novel nuclear export receptor that is specific for profilin-actin complexes
    • Stuven, T., Hartmann, E. & Gorlich, D. Exportin 6: a novel nuclear export receptor that is specific for profilin-actin complexes. EMBO J. 22, 5928-5940 (2003).
    • (2003) EMBO J. , vol.22 , pp. 5928-5940
    • Stuven, T.1    Hartmann, E.2    Gorlich, D.3
  • 16
    • 0242501529 scopus 로고    scopus 로고
    • Profilin I colocalizes with speckles and Cajal bodies: A possible role in pre-mRNA splicing
    • Skare, P., Kreivi, J. P., Bergstrom, A. & Karlsson, R. Profilin I colocalizes with speckles and Cajal bodies: a possible role in pre-mRNA splicing. Exp. Cell Res. 286, 12-21 (2003).
    • (2003) Exp. Cell Res. , vol.286 , pp. 12-21
    • Skare, P.1    Kreivi, J.P.2    Bergstrom, A.3    Karlsson, R.4
  • 17
    • 0036679163 scopus 로고    scopus 로고
    • The MEK kinase Ssk2p promotes actin cytoskeleton recovery after osmotic stress
    • Yuzyuk, T., Foehr, M. & Amberg, D. C. & The MEK kinase Ssk2p promotes actin cytoskeleton recovery after osmotic stress. Mol. Biol. Cell 13, 2869-2880 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2869-2880
    • Yuzyuk, T.1    Foehr, M.2    Amberg, D.C.3
  • 18
    • 0037769208 scopus 로고    scopus 로고
    • Actin recovery and bud emergence in osmotically stressed cells requires the conserved actin interacting mitogen-activated protein kinase kinase kinase Ssk2p/MTK1 and the scaffold protein Spa2p
    • Yuzyuk, T. & Amberg, D. C. Actin recovery and bud emergence in osmotically stressed cells requires the conserved actin interacting mitogen-activated protein kinase kinase kinase Ssk2p/MTK1 and the scaffold protein Spa2p. Mol. Biol. Cell 14, 3013-3026 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3013-3026
    • Yuzyuk, T.1    Amberg, D.C.2
  • 19
    • 0018148629 scopus 로고
    • Immunocytochemical study of lampbrush chromosomes: Presence of tubulin and actin
    • Karsenti, E., Gounon, P. & Bornens, M. Immunocytochemical study of lampbrush chromosomes: presence of tubulin and actin. Biol. Cell. 31, 219-224 (1978).
    • (1978) Biol. Cell. , vol.31 , pp. 219-224
    • Karsenti, E.1    Gounon, P.2    Bornens, M.3
  • 20
    • 0021677114 scopus 로고
    • Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes
    • Scheer, U., Hinssen, H., Franke, W. W. & Jockusch, B. M. Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes. Cell 39, 111-22 (1984).
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.M.4
  • 21
    • 0030836598 scopus 로고    scopus 로고
    • Evidence for the presence of myosin in the nucleus
    • Nowak, G. et al. Evidence for the presence of myosin in the nucleus. J. Biol. Chem. 272, 17176-17181 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 17176-17181
    • Nowak, G.1
  • 22
    • 0034644632 scopus 로고    scopus 로고
    • A myosin I isoform in the nucleus
    • Pestic-Dragovich, L. et al. A myosin I isoform in the nucleus. Science 290, 337-341 (2000).
    • (2000) Science , vol.290 , pp. 337-341
    • Pestic-Dragovich, L.1
  • 23
    • 0035809913 scopus 로고    scopus 로고
    • Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs. An unexpected role for actin
    • Hofmann, W. et al. Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs. An unexpected role for actin. J. Cell Biol. 152, 895-910 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 895-910
    • Hofmann, W.1
  • 24
    • 0037016753 scopus 로고    scopus 로고
    • Nuclear DNA Helicase II/RNA helicase A binds to filamentous actin
    • Zhang, S. et al. Nuclear DNA Helicase II/RNA helicase A binds to filamentous actin. J. Biol. Chem. 277, 843-853 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 843-853
    • Zhang, S.1
  • 25
    • 0035795419 scopus 로고    scopus 로고
    • Actin bound to the heterogeneous nuclear ribonucleoprotein hrp36 is associated with Balbiani ring mRNA from the gene to polysomes
    • Percipalle, P. et al. Actin bound to the heterogeneous nuclear ribonucleoprotein hrp36 is associated with Balbiani ring mRNA from the gene to polysomes. J. Cell Biol. 153, 229-236 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 229-236
    • Percipalle, P.1
  • 26
    • 0037089149 scopus 로고    scopus 로고
    • Nuclear actin is associated with a specific subset of hnRNP A/B-type proteins
    • Percipalle, P. et al. Nuclear actin is associated with a specific subset of hnRNP A/B-type proteins. Nucleic Acids Res. 30, 1725-1734 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1725-1734
    • Percipalle, P.1
  • 27
    • 0037637576 scopus 로고    scopus 로고
    • An actin-ribonucleoprotein interaction is involved in transcription by RNA polymerase II
    • Percipalle, P. et al. An actin-ribonucleoprotein interaction is involved in transcription by RNA polymerase II. Proc. Natl Acad. Sci. USA 100, 6475-6480 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6475-6480
    • Percipalle, P.1
  • 28
    • 0032567080 scopus 로고    scopus 로고
    • Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling
    • Zhao, K. et al. Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell 95, 625-636 (1998).
    • (1998) Cell , vol.95 , pp. 625-636
    • Zhao, K.1
  • 29
    • 0031736990 scopus 로고    scopus 로고
    • The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of distinct protein complexes
    • Papoulas, O. et al. The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of distinct protein complexes. Development 125, 3955-3966 (1998).
    • (1998) Development , vol.125 , pp. 3955-3966
    • Papoulas, O.1
  • 30
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • Shen, X., Mizuguchi, G., Hamiche, A. & Wu, C. A chromatin remodelling complex involved in transcription and DNA processing. Nature 406, 541-544 (2000).
    • (2000) Nature , vol.406 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 31
    • 0033634693 scopus 로고    scopus 로고
    • Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription
    • Galarneau, L. et al. Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription. Mol. Cell 5, 927-937 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 927-937
    • Galarneau, L.1
  • 32
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • Ikura, T. et al. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102, 463-473 (2000).
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1
  • 33
    • 0034700134 scopus 로고    scopus 로고
    • The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes
    • Xue, Y. et al. The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes. Proc. Natl Acad. Sci. USA 97, 13015-13020 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13015-13020
    • Xue, Y.1
  • 34
    • 0035839104 scopus 로고    scopus 로고
    • The p400 complex is an essential E1A transformation target
    • Fuchs, M. et al. The p400 complex is an essential E1A transformation target. Cell 106, 297-307 (2001).
    • (2001) Cell , vol.106 , pp. 297-307
    • Fuchs, M.1
  • 35
    • 0037022632 scopus 로고    scopus 로고
    • Phosphatidylinositol-dependent actin filament binding by the SWI/ SNF-like BAF chromatin remodeling complex
    • Rando, O. J., Zhao, K., Janmey, P. & Crabtree, G. R. Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex. Proc. Natl Acad. Sci. USA 99, 2824-2829 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2824-2829
    • Rando, O.J.1    Zhao, K.2    Janmey, P.3    Crabtree, G.R.4
  • 36
    • 0033625535 scopus 로고    scopus 로고
    • The EAST protein of Drosophila controls an expandable nuclear endoskeleton
    • Wasser, M. & Chia, W. The EAST protein of Drosophila controls an expandable nuclear endoskeleton. Nature Cell Biol. 2, 268-275 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 268-275
    • Wasser, M.1    Chia, W.2
  • 37
    • 0027512335 scopus 로고
    • Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells
    • Conboy, J. G. Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells. Semin. Hematol. 30, 58-73 (1993).
    • (1993) Semin. Hematol. , vol.30 , pp. 58-73
    • Conboy, J.G.1
  • 38
    • 0030992443 scopus 로고    scopus 로고
    • Structural protein 4.1 in the nucleus of human cells: Dynamic rearrangements during cell division
    • Krauss, S. W. et al. Structural protein 4.1 in the nucleus of human cells: dynamic rearrangements during cell division. J. Cell Biol. 137, 275-289 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 275-289
    • Krauss, S.W.1
  • 39
    • 0346106162 scopus 로고    scopus 로고
    • Two distinct domains of protein 4.1 critical for assembly of functional nuclei in vitro
    • Krauss, S. W. et al. Two distinct domains of protein 4.1 critical for assembly of functional nuclei in vitro. J. Biol. Chem. 277, 44339-44346 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44339-44346
    • Krauss, S.W.1
  • 40
    • 0141703273 scopus 로고    scopus 로고
    • Nuclear actin and protein 4.1: Essential interactions during nuclear assembly in vitro
    • Krauss, S. W., Chen, C., Penman, S. & Heald, R. Nuclear actin and protein 4.1: essential interactions during nuclear assembly in vitro. Proc. Natl Acad. Sci. USA 100, 10752-10757 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10752-10757
    • Krauss, S.W.1    Chen, C.2    Penman, S.3    Heald, R.4
  • 41
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the erythrocyte membrane skeleton
    • Byers, T. J. & Branton, D. Visualization of the protein associations in the erythrocyte membrane skeleton. Proc. Natl Acad. Sci. USA 62, 6153-6157 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.62 , pp. 6153-6157
    • Byers, T.J.1    Branton, D.2
  • 42
    • 0022486512 scopus 로고
    • Ultrastructure of the intact skeleton of the human erythrocyte membrane
    • Shen, B. W., Josephs, R. & Steck. T. L. Ultrastructure of the intact skeleton of the human erythrocyte membrane. J. Cell Biol. 102, 997-1006 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 997-1006
    • Shen, B.W.1    Josephs, R.2    Steck, T.L.3
  • 43
    • 0032478672 scopus 로고    scopus 로고
    • In vitro interaction of the carboxy-terminal domain of lamin A with actin
    • Sasseville, A. M. & Langelier, Y. In vitro interaction of the carboxy-terminal domain of lamin A with actin. FEBS Lett. 425, 485-489 (1998).
    • (1998) FEBS Lett. , vol.425 , pp. 485-489
    • Sasseville, A.M.1    Langelier, Y.2
  • 44
    • 0344211826 scopus 로고    scopus 로고
    • Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts
    • Lattanzi, G. et al. Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts. Biochem. Biophys. Res. Commun. 303, 764-770 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 764-770
    • Lattanzi, G.1
  • 46
    • 0016361516 scopus 로고
    • Actin is the naturally occurring inhibitor of deoxyribonuclease I
    • Lazarides, E. & Lindberg, U. Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc. Natl Acad. Sci. USA 71, 4742-4746 (1974).
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4742-4746
    • Lazarides, E.1    Lindberg, U.2
  • 47
    • 0021513584 scopus 로고
    • Is actin a transcription initiation factor for RNA polymerase B?
    • Egly, J. M., Miyamoto, N. G., Moncollin, V. & Chambon, P. Is actin a transcription initiation factor for RNA polymerase B? EMBO J. 3, 2363-2371 (1984).
    • (1984) EMBO J. , vol.3 , pp. 2363-2371
    • Egly, J.M.1    Miyamoto, N.G.2    Moncollin, V.3    Chambon, P.4
  • 48
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • Pederson, T. & Aebi, U. Actin in the nucleus: what form and what for? J. Struct. Biol. 140, 3-9 (2002).
    • (2002) J. Struct. Biol. , vol.140 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 49
    • 0027133190 scopus 로고
    • Cytochemical localization of actin and myosin aggregates in interphase nuclei in situ
    • Milankov, K. & De Boni, U. Cytochemical localization of actin and myosin aggregates in interphase nuclei in situ. Exp. Cell Res. 209, 189-199 (1993).
    • (1993) Exp. Cell Res. , vol.209 , pp. 189-199
    • Milankov, K.1    De Boni, U.2
  • 50
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein, L. R., Graceffa, P. & Dominguez, R. The crystal structure of uncomplexed actin in the ADP state. Science 293, 708-711 (2001).
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 51
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • Wertman, K. F., Drubin, D. G. & Botstein, D. Systematic mutational analysis of the yeast ACT1 gene. Genetics 132, 337-350 (1992).
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 52
    • 0020123666 scopus 로고
    • Actin polymerization and its regulation by proteins from nonmuscle cells
    • Korn, E. D. Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol. Rev. 62, 672-737 (1982).
    • (1982) Physiol. Rev. , vol.62 , pp. 672-737
    • Korn, E.D.1
  • 53
    • 0027365677 scopus 로고
    • gCap39 is a nuclear and cytoplasmic protein
    • Onoda, K., Yu, F. X. & Yin, H. L. gCap39 is a nuclear and cytoplasmic protein. Cell Motil. Cytoskeleton 26, 227-238 (1993).
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 227-238
    • Onoda, K.1    Yu, F.X.2    Yin, H.L.3
  • 54
    • 0035921434 scopus 로고    scopus 로고
    • Comparisons of CapG and gelsolin-null macrophages: Demonstration of a unique role for CapG in receptor-mediated ruffling, phagocytosis, and vesicle rocketing
    • Witke, W., Li, W., Kwiatkowski, D. J. & Southwick, F. S. Comparisons of CapG and gelsolin-null macrophages: demonstration of a unique role for CapG in receptor-mediated ruffling, phagocytosis, and vesicle rocketing. J. Cell Biol. 154, 775-784 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 775-784
    • Witke, W.1    Li, W.2    Kwiatkowski, D.J.3    Southwick, F.S.4
  • 55
    • 0030967789 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: A potential mechanism for communication between sites of cell adhesion and the nucleus
    • Nix, D. A. & Beckerle, M. C. Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. J. Cell Biol. 138, 1139-1147 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 1139-1147
    • Nix, D.A.1    Beckerle, M.C.2
  • 56
    • 0034906978 scopus 로고    scopus 로고
    • ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity
    • Fradelizi, J. et al. ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity. Nature Cell Biol. 3, 699-707 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 699-707
    • Fradelizi, J.1
  • 57
    • 0035851920 scopus 로고    scopus 로고
    • Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein
    • Weins, A. et al. Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. J. Cell Biol. 155, 393-404 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 393-404
    • Weins, A.1
  • 58
    • 0036840585 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase regulates nuclear translocation of NF-E2-related factor 2 through actin rearrangement in response to oxidative stress
    • Kang, K. W., Lee, S. J., Park, J. W. & Kim, S. G. Phosphatidylinositol 3-kinase regulates nuclear translocation of NF-E2-related factor 2 through actin rearrangement in response to oxidative stress. Mol. Pharmacol. 62, 1001-1010 (2002).
    • (2002) Mol. Pharmacol. , vol.62 , pp. 1001-1010
    • Kang, K.W.1    Lee, S.J.2    Park, J.W.3    Kim, S.G.4
  • 59
    • 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. & Ellis, J. A. 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).
    • (1999) J. Cell Sci. , vol.112 , pp. 2571-2582
    • Fairley, E.A.1    Kendrick-Jones, J.2    Ellis, J.A.3
  • 60
    • 0037684765 scopus 로고    scopus 로고
    • The nucleoskeleton: Lamins and actin are major players in essential nuclear functions
    • Shumaker, D. K., Kuczmarski, E. R. & Goldman, R. D. The nucleoskeleton: lamins and actin are major players in essential nuclear functions. Curr. Opin. Cell Biol. 15, 358-366 (2003).
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 358-366
    • Shumaker, D.K.1    Kuczmarski, E.R.2    Goldman, R.D.3
  • 61
    • 0034160165 scopus 로고    scopus 로고
    • Searching for a function for nuclear actin
    • Rando, O. J., Zhao, K. & Crabtree, G. R. Searching for a function for nuclear actin. Trends Cell Biol. 10, 92-97 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 92-97
    • Rando, O.J.1    Zhao, K.2    Crabtree, G.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.