메뉴 건너뛰기




Volumn 22, Issue 3, 1997, Pages 335-345

A green fluorescent protein-actin fusion protein dominantly inhibits cytokinesis, cell spreading, and locomotion in Dictyostelium

Author keywords

Actin; Cell movement; Cytokinesis; Dominant negative; Green fluorescent protein

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; MYOSIN HEAVY CHAIN;

EID: 0030859055     PISSN: 03867196     EISSN: None     Source Type: Journal    
DOI: 10.1247/csf.22.335     Document Type: Article
Times cited : (58)

References (34)
  • 1
    • 0025782209 scopus 로고
    • Cell locomotion: New research tests old ideas on membrane and cytoskeletal flow
    • HEATH, J.P. and HOLIFIELD, B.F. 1991. Cell locomotion: new research tests old ideas on membrane and cytoskeletal flow. Cell Motil. Cytoskel., 18: 245-257.
    • (1991) Cell Motil. Cytoskel. , vol.18 , pp. 245-257
    • Heath, J.P.1    Holifield, B.F.2
  • 2
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • STOSSEL, T.P. 1993. On the crawling of animal cells. Science, 260: 1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 3
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • COOPER, J.A. 1987. Effects of cytochalasin and phalloidin on actin. J. Cell Biol., 105: 1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 4
    • 0024095187 scopus 로고
    • Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone
    • FORSCHER, P. and SMITH, S.J. 1988. Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol., 107: 1505-1516.
    • (1988) J. Cell Biol. , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 6
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • BRETSCHER, A. 1991. Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol., 7: 377-374.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 377-1374
    • Bretscher, A.1
  • 8
    • 0021944590 scopus 로고
    • Structure of muscle filaments studied by electron microscopy
    • AMOS, L.A. 1985. Structure of muscle filaments studied by electron microscopy. Annu. Rev. Biophys. Biophys. Chem., 14: 291-313.
    • (1985) Annu. Rev. Biophys. Biophys. Chem. , vol.14 , pp. 291-313
    • Amos, L.A.1
  • 10
    • 0027508997 scopus 로고
    • Determination of cleavage planes
    • STROME, S. 1993. Determination of cleavage planes. Cell, 72: 3-6.
    • (1993) Cell , vol.72 , pp. 3-6
    • Strome, S.1
  • 11
    • 0017691824 scopus 로고
    • The effect of myosin antibody on the division of starfish blastomeres
    • MABUCHI, I. and OKUNO, M. 1977. The effect of myosin antibody on the division of starfish blastomeres. J. Cell Biol., 74: 251-263.
    • (1977) J. Cell Biol. , vol.74 , pp. 251-263
    • Mabuchi, I.1    Okuno, M.2
  • 12
    • 0023250545 scopus 로고
    • Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination
    • LOZANNE, A.D. and SPUDICH, J.A. 1987. Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science, 236: 1086-1090.
    • (1987) Science , vol.236 , pp. 1086-1090
    • Lozanne, A.D.1    Spudich, J.A.2
  • 13
    • 0023924075 scopus 로고
    • Cell motility and chemotaxis in Dictyostelium amoeba lacking myosin heavy chain
    • WESSELS, D., SOLL, D.R., KNECHT, D., LOOMIS, W.F., LOZANNE, A.D., and SPUDICH, J.A. 1988. Cell motility and chemotaxis in Dictyostelium amoeba lacking myosin heavy chain. Dev. Biol., 128: 164-177.
    • (1988) Dev. Biol. , vol.128 , pp. 164-177
    • Wessels, D.1    Soll, D.R.2    Knecht, D.3    Loomis, W.F.4    Lozanne, A.D.5    Spudich, J.A.6
  • 14
    • 0024436810 scopus 로고
    • Capping of surface receptors and concomitant cortical tension are generated by conventional myosin
    • PASTERNAK, C., SPUDICH, J.A., and ELSON, E.L. 1989. Capping of surface receptors and concomitant cortical tension are generated by conventional myosin. Nature, 341: 549-551.
    • (1989) Nature , vol.341 , pp. 549-551
    • Pasternak, C.1    Spudich, J.A.2    Elson, E.L.3
  • 19
    • 0021148863 scopus 로고
    • Localization of actin and myosin for the study of ameboid movement in Dictyostelium using improved immunofluorescence
    • YUMURA, S., MORI, H., and FUKUI, Y. 1984. Localization of actin and myosin for the study of ameboid movement in Dictyostelium using improved immunofluorescence. J. Cell Biol., 99: 894-899.
    • (1984) J. Cell Biol. , vol.99 , pp. 894-899
    • Yumura, S.1    Mori, H.2    Fukui, Y.3
  • 20
    • 0021982858 scopus 로고
    • Reversible cyclic AMP-dependent change in distribution of myosin thick filaments in Dictyostelium
    • YUMURA, S. and FUKUI, Y. 1985. Reversible cyclic AMP-dependent change in distribution of myosin thick filaments in Dictyostelium. Nature, 314: 194-196.
    • (1985) Nature , vol.314 , pp. 194-196
    • Yumura, S.1    Fukui, Y.2
  • 21
    • 0024956931 scopus 로고
    • Myosin I is located at the leading edges of locomoting Dictyostelium amoeba
    • FUKUI, Y., LYNCH, T.J., BRZESKA, H., and KORN, E.D. 1989. Myosin I is located at the leading edges of locomoting Dictyostelium amoeba. Nature, 341: 328-331.
    • (1989) Nature , vol.341 , pp. 328-331
    • Fukui, Y.1    Lynch, T.J.2    Brzeska, H.3    Korn, E.D.4
  • 22
    • 0025371423 scopus 로고
    • Generation and characterization of Dictyostelium cells deficient in a myosin I heavy chain isoform
    • JUNG, G. and HAMMER, J.A. 1990. Generation and characterization of Dictyostelium cells deficient in a myosin I heavy chain isoform. J. Cell Biol., 110: 1955-1964.
    • (1990) J. Cell Biol. , vol.110 , pp. 1955-1964
    • Jung, G.1    Hammer, J.A.2
  • 23
    • 0026332426 scopus 로고
    • Myosin IB null mutants of Dictyostelium exhibit abnormalities in motility
    • WESSELS, D., MURRAY, J.M., JUNG, G., HAMMER, J.A., and SOLL, D.R. 1991. Myosin IB null mutants of Dictyostelium exhibit abnormalities in motility. Cell Motil. Cytoskel., 20: 301-315.
    • (1991) Cell Motil. Cytoskel. , vol.20 , pp. 301-315
    • Wessels, D.1    Murray, J.M.2    Jung, G.3    Hammer, J.A.4    Soll, D.R.5
  • 24
    • 0028921277 scopus 로고
    • Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum
    • AIZAWA, H., SUTOH, K., TSUBUKI, S., KAWASHIMA, S., ISHII, A., and YAHARA, I. 1995. Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum. J. Biol. Chem., 270: 109223-10932.
    • (1995) J. Biol. Chem. , vol.270 , pp. 109223-110932
    • Aizawa, H.1    Sutoh, K.2    Tsubuki, S.3    Kawashima, S.4    Ishii, A.5    Yahara, I.6
  • 25
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimeric substitution at the actin-binding face of myosin
    • UYEDA, T.Q., RUPPEL, K.M., and SPUDICH, J.A. 1994. Enzymatic activities correlate with chimeric substitution at the actin-binding face of myosin. Nature, 368: 567-569.
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.1    Ruppel, K.M.2    Spudich, J.A.3
  • 26
    • 0027217068 scopus 로고
    • A transformation vector for Dictyostelium discoideum with a new selectable marker bsr
    • SUTOH, K. 1993. A transformation vector for Dictyostelium discoideum with a new selectable marker bsr. Plasmid, 30: 150-154.
    • (1993) Plasmid , vol.30 , pp. 150-154
    • Sutoh, K.1
  • 27
    • 0030033237 scopus 로고    scopus 로고
    • Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium
    • AIZAWA, H., SUTOH, K., and YAHARA, I. 1996. Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium. J. Cell Biol., 132: 335-344.
    • (1996) J. Cell Biol. , vol.132 , pp. 335-344
    • Aizawa, H.1    Sutoh, K.2    Yahara, I.3
  • 28
    • 0016198345 scopus 로고
    • Biochemical and structural studies of actomyosin-like proteins from non-muscle cells
    • CLARKE, M. and SPUDICH, J.A. 1974. Biochemical and structural studies of actomyosin-like proteins from non-muscle cells. J. Mol. Biol., 86: 209-222.
    • (1974) J. Mol. Biol. , vol.86 , pp. 209-222
    • Clarke, M.1    Spudich, J.A.2
  • 29
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-toroponin complex with actin and the proteolytic fragments of myosin
    • SPUDICH, J.A. and WATT, S. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-toroponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem., 246: 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 30
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments
    • MARGOSSIAN, S.S. and LOWEY, S. 1982. Preparation of myosin and its subfragments. Methods in Enzymology, 85: 55-71.
    • (1982) Methods in Enzymology , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • LAEMMLI, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0029824521 scopus 로고    scopus 로고
    • Spatial distribution of fluorescently labeled actin in living Dictyostelium amoeba
    • YUMURA, S. 1996. Spatial distribution of fluorescently labeled actin in living Dictyostelium amoeba. Cell Struc. Funct., 21: 189-197.
    • (1996) Cell Struc. Funct. , vol.21 , pp. 189-197
    • Yumura, S.1
  • 34
    • 0024215605 scopus 로고
    • Differential arrest of secretory protein transport in cultured rat hepatocytes by azide treatment
    • PERSSON, R., AHLSTROM, E., and FRIES, E. 1988. Differential arrest of secretory protein transport in cultured rat hepatocytes by azide treatment. J. Cell Biol., 107: 2503-2510.
    • (1988) J. Cell Biol. , vol.107 , pp. 2503-2510
    • Persson, R.1    Ahlstrom, E.2    Fries, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.