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Volumn 55, Issue 1, 1999, Pages 108-120

Regulation of cytokinesis

Author keywords

Contractile ring; Cytokinesis; Microtubules; Myosin; Rho

Indexed keywords

ACTIN; GUANINE NUCLEOTIDE BINDING PROTEIN; MYOSIN;

EID: 0032986685     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050274     Document Type: Review
Times cited : (20)

References (87)
  • 1
    • 0032482399 scopus 로고    scopus 로고
    • A cytokinesis checkpoint requiring the yeast homologue of an APC-binding protein
    • 1 Muhua L., Adames N. R., Murphy M. D., Shields C. R. and Cooper J. A. (1998) A cytokinesis checkpoint requiring the yeast homologue of an APC-binding protein. Nature 393: 487-491
    • (1998) Nature , vol.393 , pp. 487-491
    • Muhua, L.1    Adames, N.R.2    Murphy, M.D.3    Shields, C.R.4    Cooper, J.A.5
  • 2
    • 0029155542 scopus 로고
    • Spindle dynamics and cell cycle regulation of dynein in the budding yeast Saccharomyces cererisiae
    • 2 Yeh E., Skibbens R. V., Cheng J. W., Salmon E. D. and Bloom K. (1995) Spindle dynamics and cell cycle regulation of dynein in the budding yeast Saccharomyces cererisiae. J. Cell Biol. 130: 687-700
    • (1995) J. Cell Biol. , vol.130 , pp. 687-700
    • Yeh, E.1    Skibbens, R.V.2    Cheng, J.W.3    Salmon, E.D.4    Bloom, K.5
  • 3
    • 0030695874 scopus 로고    scopus 로고
    • The mechanism and control of cytokinesis
    • 3 Glotzer M. (1997) The mechanism and control of cytokinesis. Curr. Opin. Cell Biol. 9: 815-823
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 815-823
    • Glotzer, M.1
  • 6
    • 0030912088 scopus 로고    scopus 로고
    • Rappaport rules: Cleavage furrow induction in animal cells
    • 6 Oegema K. and Mitchison T. J. (1997) Rappaport rules: cleavage furrow induction in animal cells. Proc. Natl. Acad. Sci. USA 94: 4817-4820
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4817-4820
    • Oegema, K.1    Mitchison, T.J.2
  • 7
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • 7 Hall A. (1998) Rho GTPases and the actin cytoskeleton. Science 279: 509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 8
    • 0029786313 scopus 로고    scopus 로고
    • Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase)
    • 8 Amano M., Ito M., Kimura K., Fukata Y., Chihara K., Nakano T. et al. (1996) Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J. Biol. Chem. 271: 20246-20249
    • (1996) J. Biol. Chem. , vol.271 , pp. 20246-20249
    • Amano, M.1    Ito, M.2    Kimura, K.3    Fukata, Y.4    Chihara, K.5    Nakano, T.6
  • 9
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • 9 Chrzanowska-Wodnicka M. and Burridge K. (1996) Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133: 1403-1415
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 10
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rhokinase
    • 10 Amano M., Chihara K., Kimura K., Fukata Y., Nakamura N., Matsuura Y. et al. (1997) Formation of actin stress fibers and focal adhesions enhanced by Rhokinase. Science 275: 1308-1311
    • (1997) Science , vol.275 , pp. 1308-1311
    • Amano, M.1    Chihara, K.2    Kimura, K.3    Fukata, Y.4    Nakamura, N.5    Matsuura, Y.6
  • 11
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • 11 Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M. et al. (1996) Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science 273: 245-248
    • (1996) Science , vol.273 , pp. 245-248
    • Kimura, K.1    Ito, M.2    Amano, M.3    Chihara, K.4    Fukata, Y.5    Nakafuku, M.6
  • 12
    • 0026955927 scopus 로고
    • Rho, rac and the actin cytoskeleton
    • 12 Chrzanowska-Wodnicka M. and Burridge K. (1992) Rho, rac and the actin cytoskeleton. Bioessays 14: 777-778
    • (1992) Bioessays , vol.14 , pp. 777-778
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 13
    • 0027984138 scopus 로고
    • GAPs for rho-related GTPases
    • 13 Lamarche N. and Hall A. (1994) GAPs for rho-related GTPases. Trends Genet. 10: 436-440
    • (1994) Trends Genet. , vol.10 , pp. 436-440
    • Lamarche, N.1    Hall, A.2
  • 14
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: Cellular functions and signal transduction
    • 14 Narumiya S. (1996) The small GTPase Rho: cellular functions and signal transduction. J. Biochem. (Tokyo) 120: 215-228
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 15
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI)
    • 15 Kishi K., Sasaki T., Kuroda S., Itoh T. and Takai Y. (1993) Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J. Cell Biol. 120: 1187-1195
    • (1993) J. Cell Biol. , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 16
    • 0023779031 scopus 로고
    • Functional modification of a 21-kilodalton G protein when ADPribosylated by exoenzyme C3 of Clostridium botulinum
    • 16 Rubin E. J., Gill D. M., Boquet P. and Popoff M. R. (1988) Functional modification of a 21-kilodalton G protein when ADPribosylated by exoenzyme C3 of Clostridium botulinum. Mol. Cell. Biol. 8: 418-426
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 418-426
    • Rubin, E.J.1    Gill, D.M.2    Boquet, P.3    Popoff, M.R.4
  • 17
    • 0027691240 scopus 로고
    • A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • 17 Mabuchi I., Hamaguchi Y., Fujimoto H., Morii N., Mishima M. and Narumiya S. (1993) A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote 1: 325-331
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 18
    • 0029131982 scopus 로고
    • Translocation of activated rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • 18 Tukaishi K., Sasaki T., Kameyama T., Tsukita S. and Takai Y. (1995) Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene 11: 39-48
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Tukaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, S.4    Takai, Y.5
  • 19
    • 0028228614 scopus 로고
    • Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae
    • 19 Yamochi W., Tanaka K., Nonaka H., Maeda A., Musha T. and Takai Y. (1994) Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae. J. Cell Biol. 125: 1077-1093
    • (1994) J. Cell Biol. , vol.125 , pp. 1077-1093
    • Yamochi, W.1    Tanaka, K.2    Nonaka, H.3    Maeda, A.4    Musha, T.5    Takai, Y.6
  • 20
    • 0031037187 scopus 로고    scopus 로고
    • A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos
    • 20 Drechsel D. N., Hyman A. A., Hall A. and Glotzer M. (1997) A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos. Curr. Biol. 7: 12-23
    • (1997) Curr. Biol. , vol.7 , pp. 12-23
    • Drechsel, D.N.1    Hyman, A.A.2    Hall, A.3    Glotzer, M.4
  • 21
    • 0014995381 scopus 로고
    • Cytokinesis and cytochalasin-induccd furrow regression in the first-cleavage zygote of Xenopus laevis
    • 21 Bluemink J. G. (1971) Cytokinesis and cytochalasin-induccd furrow regression in the first-cleavage zygote of Xenopus laevis. Z. Zellforsch. Mikrosk. Anat. 121: 102-126
    • (1971) Z. Zellforsch. Mikrosk. Anat. , vol.121 , pp. 102-126
    • Bluemink, J.G.1
  • 22
    • 0017063599 scopus 로고
    • The effect of injected cytochalasin B on filament organization in the cleaving egg of Xenopus laevis
    • 22 Luchtel D., Bluemink J. G. and de Laat S. W. (1976) The effect of injected cytochalasin B on filament organization in the cleaving egg of Xenopus laevis. J. Ultrastruct. Res. 54: 406-419
    • (1976) J. Ultrastruct. Res. , vol.54 , pp. 406-419
    • Luchtel, D.1    Bluemink, J.G.2    De Laat, S.W.3
  • 23
    • 0032567760 scopus 로고    scopus 로고
    • Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis
    • 23 Lippincott J. and Li R. (1998) Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis. J. Cell Biol. 140: 355-366
    • (1998) J. Cell Biol. , vol.140 , pp. 355-366
    • Lippincott, J.1    Li, R.2
  • 24
    • 0032581530 scopus 로고    scopus 로고
    • Role of citron kinase as a target of the small GTPase Rho in cytokinesis
    • 24 Madaule P., Eda M., Watanabe N., Fujisawa K., Matsuoka T., Bito H. et al. (1998) Role of citron kinase as a target of the small GTPase Rho in cytokinesis. Nature 394: 491-494
    • (1998) Nature , vol.394 , pp. 491-494
    • Madaule, P.1    Eda, M.2    Watanabe, N.3    Fujisawa, K.4    Matsuoka, T.5    Bito, H.6
  • 25
    • 0032472918 scopus 로고    scopus 로고
    • Membrane-targeting of p21-activated kinase 1 (PAK1) induces neurite outgrowth from PC12 cells
    • 25 Daniels R. H., Hall P.S. and Bokoch G. M. (1998) Membrane-targeting of p21-activated kinase 1 (PAK1) induces neurite outgrowth from PC12 cells. EMBO J. 17: 754-764
    • (1998) EMBO J. , vol.17 , pp. 754-764
    • Daniels, R.H.1    Hall, P.S.2    Bokoch, G.M.3
  • 26
    • 0030772657 scopus 로고    scopus 로고
    • Localization of p21-activated kinase 1 (PAKI) to pinocytic vesicles and cortical actin structures in stimulated cells
    • 26 Dharmawardhane S., Sanders L. C., Martin S. S., Daniels R. H. and Bokoch G. M. (1997) Localization of p21-activated kinase 1 (PAKI) to pinocytic vesicles and cortical actin structures in stimulated cells. J. Cell Biol. 138: 1265-1278
    • (1997) J. Cell Biol. , vol.138 , pp. 1265-1278
    • Dharmawardhane, S.1    Sanders, L.C.2    Martin, S.S.3    Daniels, R.H.4    Bokoch, G.M.5
  • 27
    • 0031948850 scopus 로고    scopus 로고
    • A conserved negative regulatory region in α-PAK: Inhibition of PAK kinases reveals their morphological roles downstream of Cde42 and Rac1
    • 27 Zhao Z., Mauser E., Chen X., Chong C., Leung T. and Lim L. (1998) A conserved negative regulatory region in α-PAK: inhibition of PAK kinases reveals their morphological roles downstream of Cde42 and Rac1. Mol. Cell. Biol. 18: 2153-2163
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2153-2163
    • Zhao, Z.1    Mauser, E.2    Chen, X.3    Chong, C.4    Leung, T.5    Lim, L.6
  • 28
  • 29
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and local complexes
    • 29 Manser E., Huang H. Y., Loo T. H., Chen X. Q., Dong J. M., Leung T. et al. (1997) Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and local complexes. Mol. Cell. Biol. 17: 1129-1143
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1129-1143
    • Manser, E.1    Huang, H.Y.2    Loo, T.H.3    Chen, X.Q.4    Dong, J.M.5    Leung, T.6
  • 30
    • 0032438538 scopus 로고    scopus 로고
    • Phosphorylation of myosin II regulatory light chain by a member of the p21-activated kinase (PAK) family, γ-PAK
    • in press
    • 30 Chew T., Masaracchia R. and Wysolmerski R. (1998) Phosphorylation of myosin II regulatory light chain by a member of the p21-activated kinase (PAK) family, γ-PAK. J. Muscle Res. Cell Motil., in press
    • (1998) J. Muscle Res. Cell Motil.
    • Chew, T.1    Masaracchia, R.2    Wysolmerski, R.3
  • 31
    • 0020428977 scopus 로고
    • Phosphorylation of myosin light chain by protease activated kinase I
    • 31 Tuazon P. T., Skill J. T. and Traugh J. A. (1982) Phosphorylation of myosin light chain by protease activated kinase I. Biochem. Biophys. Res. Commun. 108: 910-917
    • (1982) Biochem. Biophys. Res. Commun. , vol.108 , pp. 910-917
    • Tuazon, P.T.1    Skill, J.T.2    Traugh, J.A.3
  • 32
    • 0020466944 scopus 로고
    • Phosphorylation of myosin light chain by a protease-activated kinase from rabbit skeletal muscle
    • 32 Tuazon P. T., Skill J. T. and Traugh J. A. (1982) Phosphorylation of myosin light chain by a protease-activated kinase from rabbit skeletal muscle. Eur. J. Biochem. 129: 205-209
    • (1982) Eur. J. Biochem. , vol.129 , pp. 205-209
    • Tuazon, P.T.1    Skill, J.T.2    Traugh, J.A.3
  • 33
    • 0031406397 scopus 로고    scopus 로고
    • Determinants for substrate phosphorylation by p21-activated protein kinase (gamma-PAK)
    • 33 Tuazon P. T., Spanos W. C., Gump E. L., Monnig C. A. and Traugh J. A. (1997) Determinants for substrate phosphorylation by p21-activated protein kinase (gamma-PAK). Biochemistry 36: 16059-16064
    • (1997) Biochemistry , vol.36 , pp. 16059-16064
    • Tuazon, P.T.1    Spanos, W.C.2    Gump, E.L.3    Monnig, C.A.4    Traugh, J.A.5
  • 34
    • 0031310102 scopus 로고    scopus 로고
    • Myosin phosphorylation by human cdc42-dependent S6/H4 kinase/gammaPAK from placenta and lymphoid cells
    • 34 Ramos E., Wysolmerski R. B. and Masaracchia R. A. (1997) Myosin phosphorylation by human cdc42-dependent S6/H4 kinase/gammaPAK from placenta and lymphoid cells. Recept. Signal Transduct. 7: 99-110
    • (1997) Recept. Signal Transduct. , vol.7 , pp. 99-110
    • Ramos, E.1    Wysolmerski, R.B.2    Masaracchia, R.A.3
  • 35
    • 0031026569 scopus 로고    scopus 로고
    • p21-activated kinase has substrate specificity similar to Acanthamoeba myosin I heavy chain kinase and activates Acanthamoeba myosin I
    • 35 Brzeska H., Knaus U. G., Wang Z. Y., Bokoch G. M. and Korn E. D. (1997) p21-activated kinase has substrate specificity similar to Acanthamoeba myosin I heavy chain kinase and activates Acanthamoeba myosin I. Proc. Natl. Acad. Sci. USA 94: 1092-1095
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1092-1095
    • Brzeska, H.1    Knaus, U.G.2    Wang, Z.Y.3    Bokoch, G.M.4    Korn, E.D.5
  • 36
    • 0029829898 scopus 로고    scopus 로고
    • Cleavage arrest of early frog embryos by the G protein-activated protein kinase PAK I
    • 36 Rooney R. D., Tuazon P. T., Meek W. E., Carroll E. J., Hagen J. J., Gump E. L. et al. (1996) Cleavage arrest of early frog embryos by the G protein-activated protein kinase PAK I. J. Biol. Chem. 271: 21498-21504
    • (1996) J. Biol. Chem. , vol.271 , pp. 21498-21504
    • Rooney, R.D.1    Tuazon, P.T.2    Meek, W.E.3    Carroll, E.J.4    Hagen, J.J.5    Gump, E.L.6
  • 37
    • 0030950580 scopus 로고    scopus 로고
    • Role of Dictyostelium racE in cytokinesis: Mutational analysis and localization studies by use of green fluorescent protein
    • 37 Larochelle D. A., Vithalani K. K. and De Lozanne A. (1997) Role of Dictyostelium racE in cytokinesis: mutational analysis and localization studies by use of green fluorescent protein. Mol. Biol. Cell 8: 935-944
    • (1997) Mol. Biol. Cell , vol.8 , pp. 935-944
    • Larochelle, D.A.1    Vithalani, K.K.2    De Lozanne, A.3
  • 39
    • 0031260461 scopus 로고    scopus 로고
    • Cytokinesis: A regulatory role for Ras-related proteins?
    • 39 Chisholm R. L. (1997) Cytokinesis: a regulatory role for Ras-related proteins? Curr. Biol. 7: R648-650
    • (1997) Curr. Biol. , vol.7
    • Chisholm, R.L.1
  • 40
    • 0032550181 scopus 로고    scopus 로고
    • A role for Dictyostelium racE in cortical tension and cleavage furrow progression
    • 40 Gerald N., Dai J., Ting-Beall H. P. and De Lozanne A. (1998) A role for Dictyostelium racE in cortical tension and cleavage furrow progression. J. Cell Biol. 141: 483-492
    • (1998) J. Cell Biol. , vol.141 , pp. 483-492
    • Gerald, N.1    Dai, J.2    Ting-Beall, H.P.3    De Lozanne, A.4
  • 41
    • 0031194074 scopus 로고    scopus 로고
    • Actin cytoskeleton: Are FH proteins local organizers?
    • 41 Frazier J. A. and Field C. M. (1997) Actin cytoskeleton: are FH proteins local organizers? Curr. Biol. 7: R414-417
    • (1997) Curr. Biol. , vol.7
    • Frazier, J.A.1    Field, C.M.2
  • 43
    • 0031444358 scopus 로고    scopus 로고
    • An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast
    • 43 Epp J. A. and Chant J. (1997) An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast. Curr. Biol. 7: 921-929
    • (1997) Curr. Biol. , vol.7 , pp. 921-929
    • Epp, J.A.1    Chant, J.2
  • 44
    • 0030929148 scopus 로고    scopus 로고
    • IQGAP1, a Rac-and Cdc42-binding protein, directly binds and cross-links microfilaments
    • 44 Bashour A. M., Fullerton A. T., Hart M. J. and Bloom G. S. (1997) IQGAP1, a Rac-and Cdc42-binding protein, directly binds and cross-links microfilaments. J. Cell Biol. 137: 1555-1566
    • (1997) J. Cell Biol. , vol.137 , pp. 1555-1566
    • Bashour, A.M.1    Fullerton, A.T.2    Hart, M.J.3    Bloom, G.S.4
  • 45
    • 0032572583 scopus 로고    scopus 로고
    • Iqg1p, a yeast homologue of the mammalian IQGAPs, mediates cdc42p effects on the actin cytoskeleton
    • 45 Osman M. A. and Cerione R. A. (1998) Iqg1p, a yeast homologue of the mammalian IQGAPs, mediates cdc42p effects on the actin cytoskeleton. J. Cell Biol. 142: 443-455
    • (1998) J. Cell Biol. , vol.142 , pp. 443-455
    • Osman, M.A.1    Cerione, R.A.2
  • 46
    • 0027360835 scopus 로고
    • Orientation and three-dimensional organization of actin filaments in dividing cultured cells
    • 46 Fishkind D. J. and Wang Y. L. (1993) Orientation and three-dimensional organization of actin filaments in dividing cultured cells. J. Cell Biol. 123: 837-848
    • (1993) J. Cell Biol. , vol.123 , pp. 837-848
    • Fishkind, D.J.1    Wang, Y.L.2
  • 47
    • 0031408781 scopus 로고    scopus 로고
    • Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells
    • 47 Neujahr R., Heizer C., Albrecht R., Ecke M., Schwartz J. M., Weber I, et al. (1997) Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells. J. Cell Biol. 139: 1793-1804
    • (1997) J. Cell Biol. , vol.139 , pp. 1793-1804
    • Neujahr, R.1    Heizer, C.2    Albrecht, R.3    Ecke, M.4    Schwartz, J.M.5    Weber, I.6
  • 49
    • 0030690360 scopus 로고    scopus 로고
    • On the role of myosin-11 in cytokine-sis: Division of Dictyostelium cells under adhesive and nonadhesive conditions
    • 49 Zang J. H., Cavet G., Sabry J. H., Wagner P., Moores S. L. and Spudich J. A. (1997) On the role of myosin-11 in cytokine-sis: division of Dictyostelium cells under adhesive and nonadhesive conditions. Mol. Biol. Cell 8: 2617-2629
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2617-2629
    • Zang, J.H.1    Cavet, G.2    Sabry, J.H.3    Wagner, P.4    Moores, S.L.5    Spudich, J.A.6
  • 50
    • 0030663097 scopus 로고    scopus 로고
    • Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells
    • 50 Sabry J. H., Moores S. L., Ryan S., Zang J. H. and Spudich J. A. (1997) Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells. Mol. Biol. Cell 8: 2605-2615
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2605-2615
    • Sabry, J.H.1    Moores, S.L.2    Ryan, S.3    Zang, J.H.4    Spudich, J.A.5
  • 51
    • 0031670169 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of actin concentration during cytokinesis and locomotion in Dictyostelium
    • 51 Yumura S. and Fukui Y. (1998) Spatiotemporal dynamics of actin concentration during cytokinesis and locomotion in Dictyostelium. J. Cell Sci. 111: 2097-2108
    • (1998) J. Cell Sci. , vol.111 , pp. 2097-2108
    • Yumura, S.1    Fukui, Y.2
  • 52
    • 0028577135 scopus 로고
    • Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells
    • 52 Ostrow B. D., Chen P. and Chisholm R. L. (1994) Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells. J. Cell Biol. 127: 1945-1955
    • (1994) J. Cell Biol. , vol.127 , pp. 1945-1955
    • Ostrow, B.D.1    Chen, P.2    Chisholm, R.L.3
  • 53
    • 0031416614 scopus 로고    scopus 로고
    • Myosin light chain-activating phosphorylation sites are required for oogenesis in Drosoplila
    • 53 Jordan P. and Karess R. (1997) Myosin light chain-activating phosphorylation sites are required for oogenesis in Drosoplila. J. Cell Biol. 139: 1805-1819
    • (1997) J. Cell Biol. , vol.139 , pp. 1805-1819
    • Jordan, P.1    Karess, R.2
  • 54
    • 0027372314 scopus 로고
    • Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo
    • 54 Egelhoff T. T., Lee R. J. and Spudich J. A. (1993) Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo. Cell 75: 363-371
    • (1993) Cell , vol.75 , pp. 363-371
    • Egelhoff, T.T.1    Lee, R.J.2    Spudich, J.A.3
  • 55
    • 0029945399 scopus 로고    scopus 로고
    • Myosin-based cortical tension in Dictyostelium resolved into heavy and light chain-regulated components
    • 55 Egelhoff T. T., Naismith T. V. and Brozovich F. V. (1996) Myosin-based cortical tension in Dictyostelium resolved into heavy and light chain-regulated components. J. Muscle Res. Cell Motil. 17: 269-274
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 269-274
    • Egelhoff, T.T.1    Naismith, T.V.2    Brozovich, F.V.3
  • 57
    • 0029779538 scopus 로고    scopus 로고
    • Myosin II transport organization and phosphorylation: Evidence for cortical flow/solation-contraction coupling during cytokinesis and cell locomotion
    • 57 DeBiasio R. L., LaRocca G. M., Post P. L. and Taylor D. L. (1996) Myosin II transport organization and phosphorylation: evidence for cortical flow/solation-contraction coupling during cytokinesis and cell locomotion. Mol. Biol. Cell 7: 1259-1282
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1259-1282
    • DeBiasio, R.L.1    LaRocca, G.M.2    Post, P.L.3    Taylor, D.L.4
  • 58
    • 0031917782 scopus 로고    scopus 로고
    • Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells
    • 58 Matsumura F., Ono S., Yamakita Y., Totsukawa G. and Yamashiro S. (1998) Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells. J. Cell Biol. 140: 119-129
    • (1998) J. Cell Biol. , vol.140 , pp. 119-129
    • Matsumura, F.1    Ono, S.2    Yamakita, Y.3    Totsukawa, G.4    Yamashiro, S.5
  • 59
    • 0021239913 scopus 로고
    • Protein kinase C modulates in vitro phosphorylation of the smooth muscle heavy meromyosin by myosin light chain kinase
    • 59 Nishikawa M., Sellers J. R., Adelstein R. S. and Hidaka H. (1984) Protein kinase C modulates in vitro phosphorylation of the smooth muscle heavy meromyosin by myosin light chain kinase. J. Biol. Chem. 259: 8808-8814
    • (1984) J. Biol. Chem. , vol.259 , pp. 8808-8814
    • Nishikawa, M.1    Sellers, J.R.2    Adelstein, R.S.3    Hidaka, H.4
  • 60
    • 0023645037 scopus 로고
    • Sequence of the sites phosphorylated by protein kinase C in the smooth muscle myosin light chain
    • 60 Bengur A. R., Robinson E. A., Appella E. and Sellers J. R. (1987) Sequence of the sites phosphorylated by protein kinase C in the smooth muscle myosin light chain. J. Biol. Chem. 262: 7613-7617
    • (1987) J. Biol. Chem. , vol.262 , pp. 7613-7617
    • Bengur, A.R.1    Robinson, E.A.2    Appella, E.3    Sellers, J.R.4
  • 61
    • 0025306169 scopus 로고
    • Phosphorylation of bovine platelet myosin by protein kinase C
    • 61 Ikebe M. and Reardon S. (1990) Phosphorylation of bovine platelet myosin by protein kinase C. Biochemistry 29: 2713-2720
    • (1990) Biochemistry , vol.29 , pp. 2713-2720
    • Ikebe, M.1    Reardon, S.2
  • 62
    • 0028123676 scopus 로고
    • In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells
    • 62 Yamakita Y., Yamashiro S. and Matsumura F. (1994) In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells. J. Cell Biol. 124: 129-137
    • (1994) J. Cell Biol. , vol.124 , pp. 129-137
    • Yamakita, Y.1    Yamashiro, S.2    Matsumura, F.3
  • 63
    • 0029898761 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of smooth muscle myosin light chain in sea urchin extracts
    • 63 Mishima M. and Mabuchi I. (1996) Cell cycle-dependent phosphorylation of smooth muscle myosin light chain in sea urchin extracts. J. Biochem. 119: 906-913
    • (1996) J. Biochem. , vol.119 , pp. 906-913
    • Mishima, M.1    Mabuchi, I.2
  • 64
    • 0030441292 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylalion of smooth muscle regulatory light chain of myosin II at Ser-1 and/or -2 and Thr-9 in sea urchin egg extract
    • 64 Totsukawa G., Himi-Nakamura E., Komatsu S., Iwata K., Tezuka A., Sakai H. et al. (1996) Mitosis-specific phosphorylalion of smooth muscle regulatory light chain of myosin II at Ser-1 and/or -2 and Thr-9 in sea urchin egg extract. Cell Struct. Fund. 21: 475-482
    • (1996) Cell Struct. Fund. , vol.21 , pp. 475-482
    • Totsukawa, G.1    Himi-Nakamura, E.2    Komatsu, S.3    Iwata, K.4    Tezuka, A.5    Sakai, H.6
  • 65
    • 0023250545 scopus 로고
    • Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination
    • 65 De Lozanne A. and Spudich J. A. (1987) Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236: 1086-1091
    • (1987) Science , vol.236 , pp. 1086-1091
    • De Lozanne, A.1    Spudich, J.A.2
  • 66
    • 0023189474 scopus 로고
    • Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum
    • 66 Knecht D. A. and Loomis W. F. (1987) Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. Science 236: 1081-1086
    • (1987) Science , vol.236 , pp. 1081-1086
    • Knecht, D.A.1    Loomis, W.F.2
  • 67
    • 0026776330 scopus 로고
    • The Dictyostelium essential light chain is required for myosin function
    • 67 Pollenz R. S., Chen T.-L. L., Trivinos-Lagos L. and Chisholm R. L. (1992) The Dictyostelium essential light chain is required for myosin function. Cell 69: 951-962
    • (1992) Cell , vol.69 , pp. 951-962
    • Pollenz, R.S.1    Chen, T.-L.L.2    Trivinos-Lagos, L.3    Chisholm, R.L.4
  • 68
    • 0029090145 scopus 로고
    • Targeted disruption of the Dictyostelium myosin essential light chain gene produces cells defective in cytokinesis and morphogenesis
    • 68 Chen T. L., Kowalcyzk P. A., Ho G. and Chisholm R. L. (1995) Targeted disruption of the Dictyostelium myosin essential light chain gene produces cells defective in cytokinesis and morphogenesis. J. Cell Sci. 108: 3207-3218
    • (1995) J. Cell Sci. , vol.108 , pp. 3207-3218
    • Chen, T.L.1    Kowalcyzk, P.A.2    Ho, G.3    Chisholm, R.L.4
  • 69
    • 0028607393 scopus 로고
    • Targeted disruption of the Dictyostelium RMLC gene produces cells defective in cytokinesis and development
    • 69 Chen P., Ostrow B. D., Tafuri S. R. and Chisholm R. L. (1994) Targeted disruption of the Dictyostelium RMLC gene produces cells defective in cytokinesis and development. J. Cell Biol. 127: 1933-1944
    • (1994) J. Cell Biol. , vol.127 , pp. 1933-1944
    • Chen, P.1    Ostrow, B.D.2    Tafuri, S.R.3    Chisholm, R.L.4
  • 70
    • 0025192475 scopus 로고
    • Structure and function of the cytoskeleton of a Dictyostelium myosin-defective mutant
    • 70 Fukui Y., De Lozanne A. and Spudich J. A. (1990) Structure and function of the cytoskeleton of a Dictyostelium myosin-defective mutant. J. Cell Biol. 110: 367-378
    • (1990) J. Cell Biol. , vol.110 , pp. 367-378
    • Fukui, Y.1    De Lozanne, A.2    Spudich, J.A.3
  • 71
    • 0031049976 scopus 로고    scopus 로고
    • Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: Redistribution of the nuclei, re-arrangement of the actin system and formation of the cleavage furrow
    • 71 Neujahr R., Heizer C. and Gerisch G. (1997) Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: redistribution of the nuclei, re-arrangement of the actin system and formation of the cleavage furrow. J. Cell Sci. 110: 123-137
    • (1997) J. Cell Sci. , vol.110 , pp. 123-137
    • Neujahr, R.1    Heizer, C.2    Gerisch, G.3
  • 72
    • 16044367114 scopus 로고    scopus 로고
    • Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail
    • 72 Faix J., Steinmetz M., Boves H., Kammerer R. A., Lottspeich F., Mintert U. et al. (1996) Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail. Cell 86: 631-642
    • (1996) Cell , vol.86 , pp. 631-642
    • Faix, J.1    Steinmetz, M.2    Boves, H.3    Kammerer, R.A.4    Lottspeich, F.5    Mintert, U.6
  • 73
    • 0031802611 scopus 로고    scopus 로고
    • Microtubule-mediated centrosome motility and the positioning of cleavage furrows in multinucleate myosin II-null cells
    • 73 Neujahr R., Albrecht R., Kohler J., Matzner M., Schwartz J. M., Westphal M. et al. (1998) Microtubule-mediated centrosome motility and the positioning of cleavage furrows in multinucleate myosin II-null cells. J. Cell Sci. 111: 1227-1240
    • (1998) J. Cell Sci. , vol.111 , pp. 1227-1240
    • Neujahr, R.1    Albrecht, R.2    Kohler, J.3    Matzner, M.4    Schwartz, J.M.5    Westphal, M.6
  • 74
    • 0031013074 scopus 로고    scopus 로고
    • Traction forces of cytokinesis measured with optically modified elastic substrata
    • 74 Burton K. and Taylor D. L. (1997) Traction forces of cytokinesis measured with optically modified elastic substrata. Nature 385: 450-454
    • (1997) Nature , vol.385 , pp. 450-454
    • Burton, K.1    Taylor, D.L.2
  • 75
    • 0022560284 scopus 로고
    • Biochemical aspects of cytokinesis
    • 75 Mabuchi I. (1986) Biochemical aspects of cytokinesis. Int. Rev. Cytol. 101: 175-213
    • (1986) Int. Rev. Cytol. , vol.101 , pp. 175-213
    • Mabuchi, I.1
  • 76
    • 0023020417 scopus 로고
    • Establishment of the mechanism of cytokinesis in animal cells
    • 76 Rappaport R. (1986) Establishment of the mechanism of cytokinesis in animal cells. Int. Rev. Cytol. 105: 245-281
    • (1986) Int. Rev. Cytol. , vol.105 , pp. 245-281
    • Rappaport, R.1
  • 77
    • 0023864930 scopus 로고
    • Cortical flow in animal cells
    • 77 Bray D. and White J. G. (1988) Cortical flow in animal cells. Science 239: 883-888
    • (1988) Science , vol.239 , pp. 883-888
    • Bray, D.1    White, J.G.2
  • 78
    • 0029845878 scopus 로고    scopus 로고
    • Midzone microtubule bundles are continuously required for cytokinesis in cultured epithelial cells
    • 78 Wheatley S. P. and Wang Y. (1996) Midzone microtubule bundles are continuously required for cytokinesis in cultured epithelial cells. J. Cell Biol. 135: 981-989
    • (1996) J. Cell Biol. , vol.135 , pp. 981-989
    • Wheatley, S.P.1    Wang, Y.2
  • 79
    • 0024429842 scopus 로고
    • Simulation testing of mechanisms for inducing the formation of the contractile ring in cytokinesis
    • 79 Harris A. K. and Gewalt S. L. (1989) Simulation testing of mechanisms for inducing the formation of the contractile ring in cytokinesis. J. Cell Biol. 109: 2215-2223
    • (1989) J. Cell Biol. , vol.109 , pp. 2215-2223
    • Harris, A.K.1    Gewalt, S.L.2
  • 80
    • 0032382987 scopus 로고    scopus 로고
    • Evidences for direct involvement of microtubules in cleavage furrow formation in newt eggs
    • 80 Sawai T. (1998) Evidences For direct involvement of microtubules in cleavage furrow formation in newt eggs. Zoolog. Sci. 15: 51-56
    • (1998) Zoolog. Sci. , vol.15 , pp. 51-56
    • Sawai, T.1
  • 81
    • 0031877351 scopus 로고    scopus 로고
    • Cytokinesis and midzone microtubule organization in Caenorhabditis elegans require the kinesin-like protein ZEN-4
    • 81 Raich W. B., Moran A. N., Rothman J. H. and Hardin J. (1998) Cytokinesis and midzone microtubule organization in Caenorhabditis elegans require the kinesin-like protein ZEN-4. Mol. Biol. Cell 9: 2037-2049
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2037-2049
    • Raich, W.B.1    Moran, A.N.2    Rothman, J.H.3    Hardin, J.4
  • 82
    • 0029813618 scopus 로고    scopus 로고
    • Function of spindle microtubules in directing cortical movement and actin filament organization in dividing cultured cells
    • 82 Fishkind D. J., Silverman J. D. and Wang Y. L. (1996) Function of spindle microtubules in directing cortical movement and actin filament organization in dividing cultured cells. J. Cell Sci. 109: 2041-2051
    • (1996) J. Cell Sci. , vol.109 , pp. 2041-2051
    • Fishkind, D.J.1    Silverman, J.D.2    Wang, Y.L.3
  • 83
    • 0030870182 scopus 로고    scopus 로고
    • Microtubules suppress actomyosin-based cortical flow in Xenopus oocytes
    • 83 Canman J. C. and Bement W. M. (1997) Microtubules suppress actomyosin-based cortical flow in Xenopus oocytes. J. Cell Sci. 110: 1907-1917
    • (1997) J. Cell Sci. , vol.110 , pp. 1907-1917
    • Canman, J.C.1    Bement, W.M.2
  • 84
    • 0024444322 scopus 로고
    • The cortical microfilament system of lymphoblasts displays a periodic oscillatory activity in the absence of microtubules: Implications for cell polarity
    • 84 Bornens M., Paintrand M. and Celati C. (1989) The cortical microfilament system of lymphoblasts displays a periodic oscillatory activity in the absence of microtubules: implications for cell polarity. J. Cell Biol. 109: 1071-1083
    • (1989) J. Cell Biol. , vol.109 , pp. 1071-1083
    • Bornens, M.1    Paintrand, M.2    Celati, C.3
  • 85
    • 0028081642 scopus 로고
    • How an actin network might cause fountain streaming and nuclear migration in the syncytial Drosophila embryo
    • 85 von Dassow G. and Schubiger G. (1994) How an actin network might cause fountain streaming and nuclear migration in the syncytial Drosophila embryo. J. Cell Biol. 127: 1637-1653
    • (1994) J. Cell Biol. , vol.127 , pp. 1637-1653
    • Von Dassow, G.1    Schubiger, G.2
  • 86
    • 0031858635 scopus 로고    scopus 로고
    • Inhibition of chromosomal separation provides insights into cleavage furrow stimulation in cultured epithelial cells
    • 86 Wheatley S. P., O'Connell C. B. and Wang Y. (1998) Inhibition of chromosomal separation provides insights into cleavage furrow stimulation in cultured epithelial cells. Mol. Biol. Cell 9: 2173-2184
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2173-2184
    • Wheatley, S.P.1    O'Connell, C.B.2    Wang, Y.3
  • 87
    • 0032006529 scopus 로고    scopus 로고
    • Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis
    • 87 Giansanti M. G., Bonaccorsi S., Williams B., Williams E. V., Santolamazza C., Goldberg M. L. et al. (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev. 12: 396-410
    • (1998) Genes Dev. , vol.12 , pp. 396-410
    • Giansanti, M.G.1    Bonaccorsi, S.2    Williams, B.3    Williams, E.V.4    Santolamazza, C.5    Goldberg, M.L.6


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