메뉴 건너뛰기




Volumn 582, Issue 14, 2008, Pages 2033-2040

Nuclear actin dynamics - From form to function

Author keywords

Actin; Actin dynamics; Actin binding protein; Nuclear transport; Nucleus

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; CARRIER PROTEINS AND BINDING PROTEINS; EXPORTIN 6;

EID: 44449142302     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.04.010     Document Type: Short Survey
Times cited : (75)

References (62)
  • 1
    • 0014443113 scopus 로고
    • Intranuclear fibrillar bodies in actinomycin D-treated oocytes
    • Lane N.J. Intranuclear fibrillar bodies in actinomycin D-treated oocytes. J. Cell Biol. 40 (1969) 286-291
    • (1969) J. Cell Biol. , vol.40 , pp. 286-291
    • Lane, N.J.1
  • 2
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes
    • Stuven T., Hartmann E., and Gorlich D. Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes. EMBO J. 22 (2003) 5928-5940
    • (2003) EMBO J. , vol.22 , pp. 5928-5940
    • Stuven, T.1    Hartmann, E.2    Gorlich, D.3
  • 3
    • 32644451623 scopus 로고    scopus 로고
    • Nucleoplasmic beta-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations
    • McDonald D., Carrero G., Andrin C., de Vries G., and Hendzel M.J. Nucleoplasmic beta-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J. Cell Biol. 172 (2006) 541-552
    • (2006) J. Cell Biol. , vol.172 , pp. 541-552
    • McDonald, D.1    Carrero, G.2    Andrin, C.3    de Vries, G.4    Hendzel, M.J.5
  • 4
    • 33646495978 scopus 로고    scopus 로고
    • Actin in transcription and transcription regulation
    • Miralles F., and Visa N. Actin in transcription and transcription regulation. Curr. Opin. Cell Biol. 18 (2006) 261-266
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 261-266
    • Miralles, F.1    Visa, N.2
  • 5
    • 34250849566 scopus 로고    scopus 로고
    • Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL
    • Vartiainen M.K., Guettler S., Larijani B., and Treisman R. Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL. Science 316 (2007) 1749-1752
    • (2007) Science , vol.316 , pp. 1749-1752
    • Vartiainen, M.K.1    Guettler, S.2    Larijani, B.3    Treisman, R.4
  • 6
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport
    • Terry L.J., Shows E.B., and Wente S.R. Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport. Science 318 (2007) 1412-1416
    • (2007) Science , vol.318 , pp. 1412-1416
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 7
    • 33644747345 scopus 로고    scopus 로고
    • A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    • Bohnsack M.T., Stuven T., Kuhn C., Cordes V.C., and Gorlich D. A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes. Nat. Cell Biol. 8 (2006) 257-263
    • (2006) Nat. Cell Biol. , vol.8 , pp. 257-263
    • Bohnsack, M.T.1    Stuven, T.2    Kuhn, C.3    Cordes, V.C.4    Gorlich, D.5
  • 8
    • 0026550804 scopus 로고
    • The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin
    • Iida K., Matsumoto S., and Yahara I. The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Struct. Funct. 17 (1992) 39-46
    • (1992) Cell Struct. Funct. , vol.17 , pp. 39-46
    • Iida, K.1    Matsumoto, S.2    Yahara, I.3
  • 10
    • 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., and Koffer A. 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
    • Pendleton, A.1    Pope, B.2    Weeds, A.3    Koffer, A.4
  • 11
    • 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., and Nishida E. Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J. 17 (1998) 1635-1641
    • (1998) EMBO J. , vol.17 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 12
    • 0022379715 scopus 로고
    • Morphological study of the mammalian stress response: characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli, and appearance of intranuclear actin filaments in rat fibroblasts after heat-shock treatment
    • Welch W.J., and Suhan J.P. Morphological study of the mammalian stress response: characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli, and appearance of intranuclear actin filaments in rat fibroblasts after heat-shock treatment. J. Cell Biol. 101 (1985) 1198-1211
    • (1985) J. Cell Biol. , vol.101 , pp. 1198-1211
    • Welch, W.J.1    Suhan, J.P.2
  • 13
    • 0018428638 scopus 로고
    • Nuclear actin bundles in Amoeba, Dictyostelium and human HeLa cells induced by dimethyl sulfoxide
    • Fukui Y., and Katsumaru H. Nuclear actin bundles in Amoeba, Dictyostelium and human HeLa cells induced by dimethyl sulfoxide. Exp. Cell Res. 120 (1979) 451-455
    • (1979) Exp. Cell Res. , vol.120 , pp. 451-455
    • Fukui, Y.1    Katsumaru, H.2
  • 14
    • 1642556795 scopus 로고    scopus 로고
    • Nuclear accumulation of globular actin as a cellular senescence marker
    • Kwak I.H., Kim H.S., Choi O.R., Ryu M.S., and Lim I.K. Nuclear accumulation of globular actin as a cellular senescence marker. Cancer Res. 64 (2004) 572-580
    • (2004) Cancer Res. , vol.64 , pp. 572-580
    • Kwak, I.H.1    Kim, H.S.2    Choi, O.R.3    Ryu, M.S.4    Lim, I.K.5
  • 15
    • 36749037144 scopus 로고    scopus 로고
    • Mechanisms underlying intranuclear rod formation
    • Domazetovska A., et al. Mechanisms underlying intranuclear rod formation. Brain 130 (2007) 3275-3284
    • (2007) Brain , vol.130 , pp. 3275-3284
    • Domazetovska, A.1
  • 16
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles F., Posern G., Zaromytidou A.I., and Treisman R. Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell 113 (2003) 329-342
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 18
    • 11144353441 scopus 로고    scopus 로고
    • A simple model for the cooperative stabilisation of actin filaments by phalloidin and jasplakinolide
    • Visegrady B., Lorinczy D., Hild G., Somogyi B., and Nyitrai M. A simple model for the cooperative stabilisation of actin filaments by phalloidin and jasplakinolide. FEBS Lett. 579 (2005) 6-10
    • (2005) FEBS Lett. , vol.579 , pp. 6-10
    • Visegrady, B.1    Lorinczy, D.2    Hild, G.3    Somogyi, B.4    Nyitrai, M.5
  • 19
    • 0032957520 scopus 로고    scopus 로고
    • Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody
    • Gonsior S.M., Platz S., Buchmeier S., Scheer U., Jockusch B.M., and Hinssen H. Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody. J. Cell Sci. 112 (1999) 797-809
    • (1999) J. Cell Sci. , vol.112 , pp. 797-809
    • Gonsior, S.M.1    Platz, S.2    Buchmeier, S.3    Scheer, U.4    Jockusch, B.M.5    Hinssen, H.6
  • 22
    • 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 (2001) 895-910
    • (2001) J. Cell Biol. , vol.152 , pp. 895-910
    • Hofmann, W.1
  • 23
    • 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., and Heald R. 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
  • 24
    • 40749162732 scopus 로고    scopus 로고
    • Nuclear receptor-enhanced transcription requires motor- and LSD1-dependent gene networking in interchromatin granules
    • Nunez E., et al. Nuclear receptor-enhanced transcription requires motor- and LSD1-dependent gene networking in interchromatin granules. Cell 132 (2008) 996-1010
    • (2008) Cell , vol.132 , pp. 996-1010
    • Nunez, E.1
  • 25
    • 0036900955 scopus 로고    scopus 로고
    • ADF/cofilin and actin dynamics in disease
    • Bamburg J.R., and Wiggan O.P. ADF/cofilin and actin dynamics in disease. Trends Cell Biol. 12 (2002) 598-605
    • (2002) Trends Cell Biol. , vol.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 26
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function
    • McGough A., Pope B., Chiu W., and Weeds A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138 (1997) 771-781
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 27
    • 0037416225 scopus 로고    scopus 로고
    • Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    • Gorlich D., Seewald M.J., and Ribbeck K. Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J. 22 (2003) 1088-1100
    • (2003) EMBO J. , vol.22 , pp. 1088-1100
    • Gorlich, D.1    Seewald, M.J.2    Ribbeck, K.3
  • 28
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., and Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112 (2003) 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 29
    • 34147105329 scopus 로고    scopus 로고
    • A novel role of the actin-nucleating Arp2/3 complex in the regulation of RNA polymerase II-dependent transcription
    • Yoo Y.D., Wu X.Y., and Guan J.L. A novel role of the actin-nucleating Arp2/3 complex in the regulation of RNA polymerase II-dependent transcription. J. Biol. Chem. 282 (2007) 7616-7623
    • (2007) J. Biol. Chem. , vol.282 , pp. 7616-7623
    • Yoo, Y.D.1    Wu, X.Y.2    Guan, J.L.3
  • 30
    • 33745762947 scopus 로고    scopus 로고
    • Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners
    • Wu X., Yoo Y., Okuhama N.N., Tucker P.W., Liu G., and Guan J.L. Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners. Nat. Cell Biol. 8 (2006) 756-763
    • (2006) Nat. Cell Biol. , vol.8 , pp. 756-763
    • Wu, X.1    Yoo, Y.2    Okuhama, N.N.3    Tucker, P.W.4    Liu, G.5    Guan, J.L.6
  • 32
    • 3142773420 scopus 로고    scopus 로고
    • Cytoplasmic nuclear transfer of the actin-capping protein tropomodulin
    • Kong K.Y., and Kedes L. Cytoplasmic nuclear transfer of the actin-capping protein tropomodulin. J. Biol. Chem. 279 (2004) 30856-30864
    • (2004) J. Biol. Chem. , vol.279 , pp. 30856-30864
    • Kong, K.Y.1    Kedes, L.2
  • 33
    • 19344378383 scopus 로고    scopus 로고
    • Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane
    • Holaska J.M., Kowalski A.K., and Wilson K.L. Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. PLoS Biol. 2 (2004) E231
    • (2004) PLoS Biol. , vol.2
    • Holaska, J.M.1    Kowalski, A.K.2    Wilson, K.L.3
  • 34
  • 36
    • 36148972458 scopus 로고    scopus 로고
    • Thymosin beta 4 expression and nuclear transport are regulated by hMLH1
    • Brieger A., Plotz G., Zeuzem S., and Trojan J. Thymosin beta 4 expression and nuclear transport are regulated by hMLH1. Biochem. Biophys. Res. Commun. 364 (2007) 731-736
    • (2007) Biochem. Biophys. Res. Commun. , vol.364 , pp. 731-736
    • Brieger, A.1    Plotz, G.2    Zeuzem, S.3    Trojan, J.4
  • 37
    • 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., and Karlsson R. Profilin I colocalizes with speckles and Cajal bodies: a possible role in pre-mRNA splicing. Exp. Cell Res. 286 (2003) 12-21
    • (2003) Exp. Cell Res. , vol.286 , pp. 12-21
    • Skare, P.1    Kreivi, J.P.2    Bergstrom, A.3    Karlsson, R.4
  • 38
    • 14044272875 scopus 로고    scopus 로고
    • Profilin regulates the activity of p42POP, a novel Myb-related transcription factor
    • Lederer M., Jockusch B.M., and Rothkegel M. Profilin regulates the activity of p42POP, a novel Myb-related transcription factor. J. Cell Sci. 118 (2005) 331-341
    • (2005) J. Cell Sci. , vol.118 , pp. 331-341
    • Lederer, M.1    Jockusch, B.M.2    Rothkegel, M.3
  • 40
    • 35648959758 scopus 로고    scopus 로고
    • CAP2, cyclase-associated protein 2, is a dual compartment protein
    • Peche V., et al. CAP2, cyclase-associated protein 2, is a dual compartment protein. Cell Mol. Life Sci. 64 (2007) 2702-2715
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 2702-2715
    • Peche, V.1
  • 41
    • 24144479246 scopus 로고    scopus 로고
    • Cofilin, actin and their complex observed in vivo using fluorescence resonance energy transfer
    • Chhabra D., and dos Remedios C.G. Cofilin, actin and their complex observed in vivo using fluorescence resonance energy transfer. Biophys. J. 89 (2005) 1902-1908
    • (2005) Biophys. J. , vol.89 , pp. 1902-1908
    • Chhabra, D.1    dos Remedios, C.G.2
  • 42
    • 17844390892 scopus 로고    scopus 로고
    • Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators
    • Archer S.K., Claudianos C., and Campbell H.D. Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators. Bioessays 27 (2005) 388-396
    • (2005) Bioessays , vol.27 , pp. 388-396
    • Archer, S.K.1    Claudianos, C.2    Campbell, H.D.3
  • 43
    • 2642517837 scopus 로고    scopus 로고
    • Actin monomer enhances supervillin-modulated androgen receptor transactivation
    • Ting H.J., Hu Y.C., and Chang C. Actin monomer enhances supervillin-modulated androgen receptor transactivation. Biochem. Biophys. Res. Commun. 319 (2004) 393-396
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 393-396
    • Ting, H.J.1    Hu, Y.C.2    Chang, C.3
  • 44
    • 14344265557 scopus 로고    scopus 로고
    • Spectrin repeat proteins in the nucleus
    • Young K.G., and Kothary R. Spectrin repeat proteins in the nucleus. Bioessays 27 (2005) 144-152
    • (2005) Bioessays , vol.27 , pp. 144-152
    • Young, K.G.1    Kothary, R.2
  • 47
    • 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., Wang W., Rando O.J., Xue Y., Swiderek K., Kuo A., and Crabtree G.R. Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell 95 (1998) 625-636
    • (1998) Cell , vol.95 , pp. 625-636
    • Zhao, K.1    Wang, W.2    Rando, O.J.3    Xue, Y.4    Swiderek, K.5    Kuo, A.6    Crabtree, G.R.7
  • 48
    • 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., and Crabtree G.R. Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex. Proc. Natl. Acad. Sci. USA 99 (2002) 2824-2829
    • (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
  • 50
    • 0142027035 scopus 로고    scopus 로고
    • The polybasic region of Ras and Rho family small GTPases: a regulator of protein interactions and membrane association and a site of nuclear localization signal sequences
    • Williams C.L. The polybasic region of Ras and Rho family small GTPases: a regulator of protein interactions and membrane association and a site of nuclear localization signal sequences. Cell Signal. 15 (2003) 1071-1080
    • (2003) Cell Signal. , vol.15 , pp. 1071-1080
    • Williams, C.L.1
  • 51
    • 33748757161 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of unique nuclear and nucleolar localization signals of LIM kinase 2 in endothelial cells
    • Goyal P., Pandey D., and Siess W. Phosphorylation-dependent regulation of unique nuclear and nucleolar localization signals of LIM kinase 2 in endothelial cells. J. Biol. Chem. 281 (2006) 25223-25230
    • (2006) J. Biol. Chem. , vol.281 , pp. 25223-25230
    • Goyal, P.1    Pandey, D.2    Siess, W.3
  • 53
    • 0036674866 scopus 로고    scopus 로고
    • NUANCE, a giant protein connecting the nucleus and actin cytoskeleton
    • Zhen Y.Y., Libotte T., Munck M., Noegel A.A., and Korenbaum E. NUANCE, a giant protein connecting the nucleus and actin cytoskeleton. J. Cell Sci. 115 (2002) 3207-3222
    • (2002) J. Cell Sci. , vol.115 , pp. 3207-3222
    • Zhen, Y.Y.1    Libotte, T.2    Munck, M.3    Noegel, A.A.4    Korenbaum, E.5
  • 54
    • 3042777656 scopus 로고    scopus 로고
    • Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei
    • Kiseleva E., Drummond S.P., Goldberg M.W., Rutherford S.A., Allen T.D., and Wilson K.L. Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei. J. Cell Sci. 117 (2004) 2481-2490
    • (2004) J. Cell Sci. , vol.117 , pp. 2481-2490
    • Kiseleva, E.1    Drummond, S.P.2    Goldberg, M.W.3    Rutherford, S.A.4    Allen, T.D.5    Wilson, K.L.6
  • 57
    • 35848966372 scopus 로고    scopus 로고
    • Cytoskeletal elements in bacteria
    • Graumann P.L. Cytoskeletal elements in bacteria. Annu. Rev. Microbiol. 61 (2007) 589-618
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 589-618
    • Graumann, P.L.1
  • 61
    • 0032478549 scopus 로고    scopus 로고
    • RNA polymerase as a molecular motor
    • Gelles J., and Landick R. RNA polymerase as a molecular motor. Cell 93 (1998) 13-16
    • (1998) Cell , vol.93 , pp. 13-16
    • Gelles, J.1    Landick, R.2
  • 62
    • 38949127670 scopus 로고    scopus 로고
    • Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription
    • Ye J., Zhao J., Hoffmann-Rohrer U., and Grummt I. Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription. Genes Dev. 22 (2008) 322-330
    • (2008) Genes Dev. , vol.22 , pp. 322-330
    • Ye, J.1    Zhao, J.2    Hoffmann-Rohrer, U.3    Grummt, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.