메뉴 건너뛰기




Volumn 50, Issue 5, 2008, Pages 394-405

Changes in Xenopus oocyte nucleus and cytoplasm organization after actin filaments depolymerization by latrunculin

Author keywords

Actin; Intranuclear filaments; Latrunculin; Nuclear matrix; Nucleus; Ultrastructure

Indexed keywords

ACTIN; FUSED HETEROCYCLIC RINGS; LATRUNCULIN A; THIAZOLIDINE DERIVATIVE; XENOPUS PROTEIN;

EID: 47749123489     PISSN: 00413771     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (4)

References (57)
  • 1
    • 47749138748 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 2
    • 47749091085 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 3
    • 47749154619 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 4
    • 47749105460 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 5
    • 0028361091 scopus 로고
    • Ultrastructural localization of filamentous actin within neuronal interphase nuclei in situ
    • Amankwah K. S., De Boni U. 1994. Ultrastructural localization of filamentous actin within neuronal interphase nuclei in situ. Exp. Cell Res. 210 : 315-325.
    • (1994) Exp. Cell Res , vol.210 , pp. 315-325
    • Amankwah, K.S.1    De Boni, U.2
  • 6
    • 0032419950 scopus 로고    scopus 로고
    • The nuclear basket of the nuclear pore complex is part of a higher-order filamentous network that is related to chromatin
    • Arlucea J., Andrade R., Alonso R., Arechaga J. 1998. The nuclear basket of the nuclear pore complex is part of a higher-order filamentous network that is related to chromatin. J. Struct. Biol. 1 : 51-58.
    • (1998) J. Struct. Biol , vol.1 , pp. 51-58
    • Arlucea, J.1    Andrade, R.2    Alonso, R.3    Arechaga, J.4
  • 7
    • 0031898609 scopus 로고    scopus 로고
    • Exocytosis in chromaffin cells of the adrenal medulla
    • Aunis D. 1998. Exocytosis in chromaffin cells of the adrenal medulla. Int. Rev. Cytol. 181 : 213-320.
    • (1998) Int. Rev. Cytol , vol.181 , pp. 213-320
    • Aunis, D.1
  • 8
    • 0031884084 scopus 로고    scopus 로고
    • Actin disassembles reversibly during electrically induced recycling of synaptic vesicles in cultured neurons
    • Bernstein B. W., DeWit M., Bamburg J. R. 1998. Actin disassembles reversibly during electrically induced recycling of synaptic vesicles in cultured neurons. Brain Res. Mol. Brain Res. 53 : 236-251.
    • (1998) Brain Res. Mol. Brain Res , vol.53 , pp. 236-251
    • Bernstein, B.W.1    DeWit, M.2    Bamburg, J.R.3
  • 10
    • 33644747345 scopus 로고    scopus 로고
    • A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    • Bohnsack M. T., Stüven T., Kuhn C., Cordes V. C., Gölich D. 2006. A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes. Nat. Cell Biol. 8 : 257-263.
    • (2006) Nat. Cell Biol , vol.8 , pp. 257-263
    • Bohnsack, M.T.1    Stüven, T.2    Kuhn, C.3    Cordes, V.C.4    Gölich, D.5
  • 11
    • 33750943167 scopus 로고    scopus 로고
    • Nuclear envelope transmembrane proteins (NETs) that are up-regulated during myogenesis
    • Chen I. H., Huber M., Guan T., Bubeck A., Gerace L. 2006. Nuclear envelope transmembrane proteins (NETs) that are up-regulated during myogenesis. BMC Cell Biol. 7 : 38-55.
    • (2006) BMC Cell Biol , vol.7 , pp. 38-55
    • Chen, I.H.1    Huber, M.2    Guan, T.3    Bubeck, A.4    Gerace, L.5
  • 13
    • 0018601589 scopus 로고
    • An actin filament matrix in hand-isolated nuclei of X. laevis oocytes
    • Clark T. G., Rosenbaum J. L. 1979. An actin filament matrix in hand-isolated nuclei of X. laevis oocytes. Cell. 18 : 1101-1108.
    • (1979) Cell , vol.18 , pp. 1101-1108
    • Clark, T.G.1    Rosenbaum, J.L.2
  • 14
    • 0141764733 scopus 로고    scopus 로고
    • Nuclear pore protein gp210 is essentialfor viability in HeLa cells and Caenorhabditis elegans
    • Cohen M., Feinstein N., Wilson K. L., Gruenbaum Y. 2003. Nuclear pore protein gp210 is essentialfor viability in HeLa cells and Caenorhabditis elegans. Mol. Cell. Biol. 14 : 4230-4237.
    • (2003) Mol. Cell. Biol , vol.14 , pp. 4230-4237
    • Cohen, M.1    Feinstein, N.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 15
    • 0015292069 scopus 로고
    • Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals
    • Dumont J. N. 1972. Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals. J. Morphol. 136 : 153-179.
    • (1972) J. Morphol , vol.136 , pp. 153-179
    • Dumont, J.N.1
  • 16
    • 34247227672 scopus 로고
    • Chromosomal physiology in relation to nuclear structure
    • Duryee W. 1950. Chromosomal physiology in relation to nuclear structure. Ann. N. Y. Acad. Sci. 50 : 920-924.
    • (1950) Ann. N. Y. Acad. Sci , vol.50 , pp. 920-924
    • Duryee, W.1
  • 17
    • 0036198747 scopus 로고    scopus 로고
    • Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast
    • Fehrenbacher K. L., Davis D., Wu M., Boldogh I., Pon L. A. 2002. Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast. Mol. Biol. Cell. 13 : 854-865.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 854-865
    • Fehrenbacher, K.L.1    Davis, D.2    Wu, M.3    Boldogh, I.4    Pon, L.A.5
  • 18
    • 17344368861 scopus 로고    scopus 로고
    • Active intranuclear movement of herpesvirus capsids
    • Forest T., Barnard S., Baines J. D. 2005. Active intranuclear movement of herpesvirus capsids. Nat. Cell Biol. 7 : 429-431.
    • (2005) Nat. Cell Biol , vol.7 , pp. 429-431
    • Forest, T.1    Barnard, S.2    Baines, J.D.3
  • 19
    • 20444420894 scopus 로고    scopus 로고
    • Diverted total synthesis: Preparation of a focused library of latrunculin analogues and evaluation of their actin-binding properties
    • Furstner A., Kirk D., Fenster M. D., Aissa C., De Souza D., Muller O. 2005. Diverted total synthesis: preparation of a focused library of latrunculin analogues and evaluation of their actin-binding properties. Proc. Nat. Acad. Sci. USA. 102 : 8103-8108.
    • (2005) Proc. Nat. Acad. Sci. USA , vol.102 , pp. 8103-8108
    • Furstner, A.1    Kirk, D.2    Fenster, M.D.3    Aissa, C.4    De Souza, D.5    Muller, O.6
  • 20
    • 33646073458 scopus 로고    scopus 로고
    • Exporting actin
    • Gall G. G. 2006. Exporting actin. Nat. Cell Biol. 8 : 205-207.
    • (2006) Nat. Cell Biol , vol.8 , pp. 205-207
    • Gall, G.G.1
  • 21
    • 0033558963 scopus 로고    scopus 로고
    • Confocal microscopy and 3-D reconstruction of the cytoskeleton of Xenopus oocytes
    • Gard D. L. 1999. Confocal microscopy and 3-D reconstruction of the cytoskeleton of Xenopus oocytes. Microsc. Res. Tech. 44 : 388-414.
    • (1999) Microsc. Res. Tech , vol.44 , pp. 388-414
    • Gard, D.L.1
  • 23
    • 0031056904 scopus 로고    scopus 로고
    • Dimples, pores, star-ring and thin rings on growing nuclear envelopes evidence for structure intermediates in nuclear pore complex assembly
    • Goldberg M. W., Weise P., Allen T. D., Wilson K. 1997. Dimples, pores, star-ring and thin rings on growing nuclear envelopes evidence for structure intermediates in nuclear pore complex assembly. J. Cell Sci. 110 : 409420.
    • (1997) J. Cell Sci , vol.110 , pp. 409420
    • Goldberg, M.W.1    Weise, P.2    Allen, T.D.3    Wilson, K.4
  • 24
    • 0019423975 scopus 로고
    • Involvement of contractile proteins in the changes in consistency of oocyte nucleoplasm of the newt Pleurodeles waltlii
    • Gounon P., Karsenti E. 1981. Involvement of contractile proteins in the changes in consistency of oocyte nucleoplasm of the newt Pleurodeles waltlii. J. Cell Biol. 88 : 410-421.
    • (1981) J. Cell Biol , vol.88 , pp. 410-421
    • Gounon, P.1    Karsenti, E.2
  • 25
    • 0030814006 scopus 로고    scopus 로고
    • Actin filament cables in Drosophila nurse cells are composed of modules that slide passively past one another during dumping
    • Guild G. M., Connelly P. S., Shaw M. K., Tilney L. G. 1997. Actin filament cables in Drosophila nurse cells are composed of modules that slide passively past one another during dumping. J. Cell Biol. 138 : 783-797.
    • (1997) J. Cell Biol , vol.138 , pp. 783-797
    • Guild, G.M.1    Connelly, P.S.2    Shaw, M.K.3    Tilney, L.G.4
  • 26
    • 33744511533 scopus 로고    scopus 로고
    • Endoplasmic reticulum targeted GFP reveals ER organization in tobacco NT-1 cells during cell division
    • Gupton S. L., Collings D. A., Allen N. S. 2006. Endoplasmic reticulum targeted GFP reveals ER organization in tobacco NT-1 cells during cell division. Plant Physiol. Biochem. 44 : 95-105.
    • (2006) Plant Physiol. Biochem , vol.44 , pp. 95-105
    • Gupton, S.L.1    Collings, D.A.2    Allen, N.S.3
  • 27
    • 33646555082 scopus 로고    scopus 로고
    • SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    • Haque F., Lloyd D. J., Smallwood D. T., Dent C. L., Shanahan C. M., Fry A. M., Trembath R. C., Shackleton S. 2006. SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton. Mol. Cell. Biol. 26 : 3738-3751.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 3738-3751
    • Haque, F.1    Lloyd, D.J.2    Smallwood, D.T.3    Dent, C.L.4    Shanahan, C.M.5    Fry, A.M.6    Trembath, R.C.7    Shackleton, S.8
  • 28
    • 32644449429 scopus 로고    scopus 로고
    • Nuclear actin: To polymerize or not to polymerize
    • Hofmann W. A., Lanerolle P. 2006. Nuclear actin: to polymerize or not to polymerize. J. Cell Biol. 172 : 127-135.
    • (2006) J. Cell Biol , vol.172 , pp. 127-135
    • Hofmann, W.A.1    Lanerolle, P.2
  • 30
    • 7944239067 scopus 로고    scopus 로고
    • Hofmann W. A., Stojiljkovic L., Fuchsova B., Vargas G. M., Mavrommatis E., Philimonenko V., Kysela K., Goodrich J. A., Lessard J. L., Hope T. J., Hozak P., de Lanerolle P. 2004. Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II. Nat. Cell Biol. 6 : 1094-1101.
    • Hofmann W. A., Stojiljkovic L., Fuchsova B., Vargas G. M., Mavrommatis E., Philimonenko V., Kysela K., Goodrich J. A., Lessard J. L., Hope T. J., Hozak P., de Lanerolle P. 2004. Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II. Nat. Cell Biol. 6 : 1094-1101.
  • 31
    • 10644294832 scopus 로고    scopus 로고
    • A role for beta-actin in RNA polymerase III transcription
    • Hu P., Wu S., Hernandez N. 2004. A role for beta-actin in RNA polymerase III transcription. Genes Develop. 15 : 3010-3015.
    • (2004) Genes Develop , vol.15 , pp. 3010-3015
    • Hu, P.1    Wu, S.2    Hernandez, N.3
  • 32
    • 0037205232 scopus 로고    scopus 로고
    • Chromatin boundaries in budding yeast: The nuclear pore connection
    • Ishii K., Arib G., Lin C., Van Houwe G., Laemmli U. K. 2002. Chromatin boundaries in budding yeast: the nuclear pore connection. Cell. 109 : 551-562.
    • (2002) Cell , vol.109 , pp. 551-562
    • Ishii, K.1    Arib, G.2    Lin, C.3    Van Houwe, G.4    Laemmli, U.K.5
  • 34
    • 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
    • Kimura T., Hashimoto I., Yamamoto A., Nishikawa M., Fujisawa J. I. 2000. 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 : 289-307.
    • (2000) Genes Cells , vol.5 , pp. 289-307
    • Kimura, T.1    Hashimoto, I.2    Yamamoto, A.3    Nishikawa, M.4    Fujisawa, J.I.5
  • 35
    • 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., Wilson K. L. 2004. Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei. J. Cell. Sci. 117 : 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
  • 36
    • 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. 2003. Nuclear actin and protein 4.1: essential interactions during nuclear assembly in vitro. Proc. Nat. Acad. Sci. USA. 100 : 10 752-10 757.
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100
    • Krauss, S.W.1    Chen, C.2    Penman, S.3    Heald, R.4
  • 37
    • 29944438325 scopus 로고    scopus 로고
    • Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli
    • Kruse T., Blagoe B., Lobner-Olesen A., Wachi M., Sasaki K., Iwai N., Mann M., Gerdes K. 2006. Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli. Genes Develop. 20 : 113-124.
    • (2006) Genes Develop , vol.20 , pp. 113-124
    • Kruse, T.1    Blagoe, B.2    Lobner-Olesen, A.3    Wachi, M.4    Sasaki, K.5    Iwai, N.6    Mann, M.7    Gerdes, K.8
  • 39
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze P., Fujimoto L. M., Yin H. L., Schmid S. L. 1997. The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J. Biol. Chem. 272 : 20 332-20 335.
    • (1997) J. Biol. Chem , vol.272
    • Lamaze, P.1    Fujimoto, L.M.2    Yin, H.L.3    Schmid, S.L.4
  • 40
    • 0034130493 scopus 로고    scopus 로고
    • Role of actin cortex in the subplasmalemmal transport of secretory granules in PC-12 cells
    • Lang T., Wacker I., Wunderlich I., Rohrbach A., Giese S., Soldati T., Almers W. 2000. Role of actin cortex in the subplasmalemmal transport of secretory granules in PC-12 cells. Biophys. J. 78 : 2863-2877.
    • (2000) Biophys. J , vol.78 , pp. 2863-2877
    • Lang, T.1    Wacker, I.2    Wunderlich, I.3    Rohrbach, A.4    Giese, S.5    Soldati, T.6    Almers, W.7
  • 44
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • Pederson T., Aebi U. 2002. Actin in the nucleus: what form and what for? J. Struct. Biol. 140 : 3-9.
    • (2002) J. Struct. Biol , vol.140 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 45
    • 27644506209 scopus 로고    scopus 로고
    • Nuclear actin extends, with no contraction in sight
    • Pederson T., Aebi U. 2005. Nuclear actin extends, with no contraction in sight. Mol. Biol. Cell. 16 : 5055-5060.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5055-5060
    • Pederson, T.1    Aebi, U.2
  • 48
    • 0033909431 scopus 로고    scopus 로고
    • Review: Movement of mRNA from transcription site to nuclear pores
    • Politz J. P., Pederson T. 2000. Review: movement of mRNA from transcription site to nuclear pores. J. Struct. Biol. 129 : 252-257.
    • (2000) J. Struct. Biol , vol.129 , pp. 252-257
    • Politz, J.P.1    Pederson, T.2
  • 49
    • 18244399835 scopus 로고    scopus 로고
    • Involvement of the actin cytoskeleton and homotypic membrane fusion in ER dynamics in Caenorhabditis elegans
    • Poteryaev D., Squirrell J. M., Campbell J. M., White J. G., Spang A. 2005. Involvement of the actin cytoskeleton and homotypic membrane fusion in ER dynamics in Caenorhabditis elegans. Mol. Biol. Cell. 16 : 2139-2153.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2139-2153
    • Poteryaev, D.1    Squirrell, J.M.2    Campbell, J.M.3    White, J.G.4    Spang, A.5
  • 51
    • 0032576766 scopus 로고    scopus 로고
    • Functional coordination of mucrotubule-based and actin-based motility in melanophores
    • Rodionov V., Hope A., Svitkina T., Borisy G. 1998. Functional coordination of mucrotubule-based and actin-based motility in melanophores. Curr. Biol. 8 : 165-168.
    • (1998) Curr. Biol , vol.8 , pp. 165-168
    • Rodionov, V.1    Hope, A.2    Svitkina, T.3    Borisy, G.4
  • 53
    • 0033960789 scopus 로고    scopus 로고
    • Membrane trafficking, organelle transport, and the cytoskeleton
    • Rogers S. L., Gelfand V. I. 2000. Membrane trafficking, organelle transport, and the cytoskeleton. Curr. Opin. Cell Biol. 12 : 57-62.
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 57-62
    • Rogers, S.L.1    Gelfand, V.I.2
  • 55
    • 33646188521 scopus 로고    scopus 로고
    • Nuclear actin: A lack of export allows formation of filaments
    • Schuh M., Ellenberg J. 2006. Nuclear actin: a lack of export allows formation of filaments. J. Curr. Biol. 16 : 321-323.
    • (2006) J. Curr. Biol , vol.16 , pp. 321-323
    • Schuh, M.1    Ellenberg, J.2
  • 56
    • 0030462308 scopus 로고    scopus 로고
    • Actin-based organelle movement
    • Simon V. R., Pon L. A. 1996. Actin-based organelle movement. Experientia. 52 : 1117-1122.
    • (1996) Experientia , vol.52 , pp. 1117-1122
    • Simon, V.R.1    Pon, L.A.2
  • 57
    • 0030794456 scopus 로고    scopus 로고
    • Nuclear envelope assembly in Xenopus extracts visualized by scanning EM reveals a transport-dependent envelope smoothing event
    • Wiese P., Goldberg M. W., Allen T. D., Wilson K. L. 1997. Nuclear envelope assembly in Xenopus extracts visualized by scanning EM reveals a transport-dependent «envelope smoothing» event. J. Cell Sci. 110 : 1489-1502.
    • (1997) J. Cell Sci , vol.110 , pp. 1489-1502
    • Wiese, P.1    Goldberg, M.W.2    Allen, T.D.3    Wilson, K.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.