메뉴 건너뛰기




Volumn 66, Issue 3, 1996, Pages 980-988

Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones

Author keywords

Actin bundling; Drebrin; Fascin; Filopodia; Growth cone; Neurite outgrowth

Indexed keywords

ACTIN BINDING PROTEIN; DREBRIN;

EID: 0030040876     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66030980.x     Document Type: Article
Times cited : (102)

References (44)
  • 1
    • 0028238878 scopus 로고
    • Actin-binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation
    • Asada H., Uyemura K., and Shirao T. (1994) Actin-binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation. J. Neurosci. Res. 38, 149-159.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 149-159
    • Asada, H.1    Uyemura, K.2    Shirao, T.3
  • 2
    • 0023571668 scopus 로고
    • Distribution and cellular localization of actin depolymerizing factor
    • Bamburg J. R. and Bray D. (1987) Distribution and cellular localization of actin depolymerizing factor. J. Cell Biol. 105, 2817-2825
    • (1987) J. Cell Biol. , vol.105 , pp. 2817-2825
    • Bamburg, J.R.1    Bray, D.2
  • 3
    • 0023027034 scopus 로고
    • Disoriented pathfinding by pioneer neurone growth cones deprived of filopodia by cytochalasin treatment
    • Bentley D. and Toroian-Raymond A. (1986) Disoriented pathfinding by pioneer neurone growth cones deprived of filopodia by cytochalasin treatment. Nature 323, 712-715.
    • (1986) Nature , vol.323 , pp. 712-715
    • Bentley, D.1    Toroian-Raymond, A.2
  • 4
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein B. W and Bamburg J. R. (1982) Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil. 2, 1-8.
    • (1982) Cell Motil. , vol.2 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 5
    • 0000290454 scopus 로고
    • Quantitative electrophoresis in polyacrylamide gels of 2-40%
    • Blattler D. P., Garner F., Van Slyke K., and Bradley A. (1972) Quantitative electrophoresis in polyacrylamide gels of 2-40%. J. Chromatogr. 64, 147-155.
    • (1972) J. Chromatogr. , vol.64 , pp. 147-155
    • Blattler, D.P.1    Garner, F.2    Van Slyke, K.3    Bradley, A.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0022402406 scopus 로고
    • Analysis of microspike movements on the neuronal growth cone
    • Bray D. and Chapman K. (1985) Analysis of microspike movements on the neuronal growth cone. J. Neurosci. 5, 3204-3213.
    • (1985) J. Neurosci. , vol.5 , pp. 3204-3213
    • Bray, D.1    Chapman, K.2
  • 8
    • 0018068395 scopus 로고
    • Separation and interaction of the major components of sea urchin actin gel
    • Bryan J. and Kane R. E. (1978) Separation and interaction of the major components of sea urchin actin gel. J. Mol. Biol. 125, 207-224.
    • (1978) J. Mol. Biol. , vol.125 , pp. 207-224
    • Bryan, J.1    Kane, R.E.2
  • 9
    • 0027424655 scopus 로고
    • Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product
    • Bryan J., Edwards R., Matsudaira P., Otto J., and Wulfkuhle J. (1993) Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product. Proc. Natl. Acad. Sci. USA 90, 9115-9119.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9115-9119
    • Bryan, J.1    Edwards, R.2    Matsudaira, P.3    Otto, J.4    Wulfkuhle, J.5
  • 10
    • 0028269631 scopus 로고
    • Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension
    • Cant K., Knowles B. A., Mooseker M. S., and Cooley L. (1994) Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. J. Cell Biol. 125, 369-380.
    • (1994) J. Cell Biol. , vol.125 , pp. 369-380
    • Cant, K.1    Knowles, B.A.2    Mooseker, M.S.3    Cooley, L.4
  • 11
    • 0027327185 scopus 로고
    • Navigational errors made by growth cones without filopodia in the embryonic Xenopus brain
    • Chien C.-B., Rosenthal D. E., Harris W. A., and Holt C. E. (1993) Navigational errors made by growth cones without filopodia in the embryonic Xenopus brain. Neuron 11, 237-251.
    • (1993) Neuron , vol.11 , pp. 237-251
    • Chien, C.-B.1    Rosenthal, D.E.2    Harris, W.A.3    Holt, C.E.4
  • 12
    • 0019004592 scopus 로고
    • Evidence for fascin cross-links between the actin filaments in coelomocyte filopodia
    • DeRosier D. J. and Edds K. T. (1980) Evidence for fascin cross-links between the actin filaments in coelomocyte filopodia. Exp. Cell Res. 126, 490-494.
    • (1980) Exp. Cell Res. , vol.126 , pp. 490-494
    • DeRosier, D.J.1    Edds, K.T.2
  • 14
    • 0028902746 scopus 로고
    • Cloning and expression of a murine fascin homolog from mouse brain
    • Edwards R. A., Herrera-Sosa H., Otto J., and Bryan J. (1995) Cloning and expression of a murine fascin homolog from mouse brain. J. Biol. Chem. 270, 10764-10770.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10764-10770
    • Edwards, R.A.1    Herrera-Sosa, H.2    Otto, J.3    Bryan, J.4
  • 15
    • 0027192866 scopus 로고
    • The organization of F-actin and microtubules in growth cones exposed to brain-derived collapsing factor
    • Fan J., Mansfield S. G., Redmond T., Gordon-Weeks P. R., and Raper J. A. (1993) The organization of F-actin and microtubules in growth cones exposed to brain-derived collapsing factor. J. Cell Biol. 121, 867-878.
    • (1993) J. Cell Biol. , vol.121 , pp. 867-878
    • Fan, J.1    Mansfield, S.G.2    Redmond, T.3    Gordon-Weeks, P.R.4    Raper, J.A.5
  • 16
    • 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
  • 17
    • 0023618902 scopus 로고
    • Retinal axons with and without their somata, growing to and arborizing in the tectum of Xenopus embryos: A time-lapse video study of single fibers in vivo
    • Harris W. A., Holt C. E., and Bonhoeffer F. (1987) Retinal axons with and without their somata, growing to and arborizing in the tectum of Xenopus embryos: a time-lapse video study of single fibers in vivo. Development 101, 123-133.
    • (1987) Development , vol.101 , pp. 123-133
    • Harris, W.A.1    Holt, C.E.2    Bonhoeffer, F.3
  • 19
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin: Potentiation of protective ability of tiopomyosins by 83-kDa nonmuscle caldesmon
    • Ishikawa R., Yamashiro S., and Matsumura F. (1989a) Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin: potentiation of protective ability of tiopomyosins by 83-kDa nonmuscle caldesmon. J. Biol. Chem. 264, 7490-7497.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 21
    • 0028139040 scopus 로고
    • Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments
    • Ishikawa R., Hayashi K., Shirao T., Xue Y., Takagi T., Sasaki Y., and Kohama K. (1994) Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J. Biol. Chem. 269, 29928-29933.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29928-29933
    • Ishikawa, R.1    Hayashi, K.2    Shirao, T.3    Xue, Y.4    Takagi, T.5    Sasaki, Y.6    Kohama, K.7
  • 22
    • 0016537752 scopus 로고
    • Preparation and purification of polymerized actin from sea urchin egg extract
    • Kane R. E. (1975) Preparation and purification of polymerized actin from sea urchin egg extract. J. Cell Biol. 66, 305-315.
    • (1975) J. Cell Biol. , vol.66 , pp. 305-315
    • Kane, R.E.1
  • 23
    • 0017106964 scopus 로고
    • Actin polymerization and interaction with other proteins in temperature-induced gelation of sea urchin egg extracts
    • Kane R. E. (1976) Actin polymerization and interaction with other proteins in temperature-induced gelation of sea urchin egg extracts. J. Cell Biol. 71, 704-714.
    • (1976) J. Cell Biol. , vol.71 , pp. 704-714
    • Kane, R.E.1
  • 24
    • 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
  • 25
    • 0021092245 scopus 로고
    • Purification and partial characterization of a new protein in porcine brain which bundles actin filaments
    • Maekawa S., Endo S., and Sakai H. (1983) Purification and partial characterization of a new protein in porcine brain which bundles actin filaments. J. Biochem. (Tokyo) 94, 1329-1337.
    • (1983) J. Biochem. (Tokyo) , vol.94 , pp. 1329-1337
    • Maekawa, S.1    Endo, S.2    Sakai, H.3
  • 26
    • 0021680448 scopus 로고
    • Growth of neuntes without filopodial or lamellipodial activity in the presence of cytochalasin B
    • Marsh L. and Letourneau P. C. (1984) Growth of neuntes without filopodial or lamellipodial activity in the presence of cytochalasin B. J. Cell Biol. 99, 2041-2047.
    • (1984) J. Cell Biol. , vol.99 , pp. 2041-2047
    • Marsh, L.1    Letourneau, P.C.2
  • 27
    • 0020475453 scopus 로고
    • Visualization of monoclonal antibody banding to tropomyosin on native smooth muscle thin filament by electron microscopy
    • Matsumura F. and Lin J. J.-C. (1982) Visualization of monoclonal antibody banding to tropomyosin on native smooth muscle thin filament by electron microscopy. J. Mol. Biol. 157, 163-171.
    • (1982) J. Mol. Biol. , vol.157 , pp. 163-171
    • Matsumura, F.1    Lin, J.J.-C.2
  • 28
    • 0025339009 scopus 로고
    • Bundling of actin filaments by alpha-actinin depends on its molecular length
    • Meyer R. K. and Aebi U. (1990) Bundling of actin filaments by alpha-actinin depends on its molecular length. J. Cell Biol. 110, 2013-2024.
    • (1990) J. Cell Biol. , vol.110 , pp. 2013-2024
    • Meyer, R.K.1    Aebi, U.2
  • 29
    • 0027988578 scopus 로고
    • Epstein-Barr virus infection induces expression in B lymphocytes of a novel gene encoding an evolutionarily conserved 55-kilodalton actin-bundling protein
    • Mosialos G., Yamashiro S., Baughman R. W., Matsudaira P., Vara L., Matsumura F., Kieff E., and Birkenbach M. (1994) Epstein-Barr virus infection induces expression in B lymphocytes of a novel gene encoding an evolutionarily conserved 55-kilodalton actin-bundling protein. J. Virol. 68, 7320-7328.
    • (1994) J. Virol. , vol.68 , pp. 7320-7328
    • Mosialos, G.1    Yamashiro, S.2    Baughman, R.W.3    Matsudaira, P.4    Vara, L.5    Matsumura, F.6    Kieff, E.7    Birkenbach, M.8
  • 30
    • 0028035005 scopus 로고
    • Disruption of microfilaments in growth cones following depolarization and calcium influx
    • Neely M. D. and Gesemann M. (1994) Disruption of microfilaments in growth cones following depolarization and calcium influx. J. Neurosci. 14, 7511-7520.
    • (1994) J. Neurosci. , vol.14 , pp. 7511-7520
    • Neely, M.D.1    Gesemann, M.2
  • 31
    • 0025832505 scopus 로고
    • In vitro movement of actin filaments on gizzard smooth muscle myosin: Requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon
    • Okagaki T., Higashi-Fujime S., Ishikawa R., Takano-Ohmuro H., and Kohama K. (1991) In vitro movement of actin filaments on gizzard smooth muscle myosin: requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon. J. Biochem. (Tokyo) 109, 858-866.
    • (1991) J. Biochem. (Tokyo) , vol.109 , pp. 858-866
    • Okagaki, T.1    Higashi-Fujime, S.2    Ishikawa, R.3    Takano-Ohmuro, H.4    Kohama, K.5
  • 32
    • 0018483411 scopus 로고
    • Formation of filopodia in coelomocytes: Localization of fascin, a 58,000 dalton actin cross-linking protein
    • Otto J. J., Kane R. E., and Bryan J. (1979) Formation of filopodia in coelomocytes: localization of fascin, a 58,000 dalton actin cross-linking protein. Cell 17, 285-293.
    • (1979) Cell , vol.17 , pp. 285-293
    • Otto, J.J.1    Kane, R.E.2    Bryan, J.3
  • 33
    • 0021847778 scopus 로고
    • Purification and characterization of GP-55, a protein associated with actin-based cytoplasmic gels derived from brain tissue
    • Saborio J. L., Diaz-Barriga F., Duran G., Tsutsumi V., and Palmer E. (1985) Purification and characterization of GP-55, a protein associated with actin-based cytoplasmic gels derived from brain tissue. J. Biol. Chem. 260, 8627-8636.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8627-8636
    • Saborio, J.L.1    Diaz-Barriga, F.2    Duran, G.3    Tsutsumi, V.4    Palmer, E.5
  • 34
    • 85047673845 scopus 로고
    • The role of microfilament-associated proteins, drebrins, in brain morphogenesis: A review
    • Shirao T. (1995) The role of microfilament-associated proteins, drebrins, in brain morphogenesis: a review. J. Biochem. (Tokyo) 117, 231-236.
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 231-236
    • Shirao, T.1
  • 35
    • 0021964771 scopus 로고
    • Two acidic proteins associated with brain development in chick embryo
    • Shirao T. and Obata K. (1985) Two acidic proteins associated with brain development in chick embryo. J. Neurochem 44, 1210-1216.
    • (1985) J. Neurochem , vol.44 , pp. 1210-1216
    • Shirao, T.1    Obata, K.2
  • 36
    • 0026512294 scopus 로고
    • Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells
    • Shirao T., Kojima N., and Obata K. (1992) Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells. Neuroreport 3, 109-112.
    • (1992) Neuroreport , vol.3 , pp. 109-112
    • Shirao, T.1    Kojima, N.2    Obata, K.3
  • 37
    • 0027961093 scopus 로고
    • Formation of thick, curving bundles of actin by drebrin A expression in fibroblasts
    • Shirao T., Hayashi K., Ishikawa R., Isa K., Asada H., Ikeda K., and Uyemura K. (1994) Formation of thick, curving bundles of actin by drebrin A expression in fibroblasts. Exp. Cell Res. 215, 145-153.
    • (1994) Exp. Cell Res. , vol.215 , pp. 145-153
    • Shirao, T.1    Hayashi, K.2    Ishikawa, R.3    Isa, K.4    Asada, H.5    Ikeda, K.6    Uyemura, K.7
  • 38
    • 0024508661 scopus 로고
    • Axonal growth-associated proteins
    • Skene J. H. P. (1989) Axonal growth-associated proteins. Annu Rev. Neurosci. 12, 27-156.
    • (1989) Annu Rev. Neurosci. , vol.12 , pp. 27-156
    • Skene, J.H.P.1
  • 39
    • 0028115830 scopus 로고
    • Cytoskeletal movements and substrate interactions during initiation of neurite outgrowth by sympathetic neurons in vitro
    • Smith C. L. (1994) Cytoskeletal movements and substrate interactions during initiation of neurite outgrowth by sympathetic neurons in vitro. J. Neurosci. 14, 384-398.
    • (1994) J. Neurosci. , vol.14 , pp. 384-398
    • Smith, C.L.1
  • 40
    • 0024721756 scopus 로고
    • Alpha-actinins, calspectin (brain spectrin or fodorin), and actin participate in adhesion and movement of growth cones
    • Sobue K. and Kanda K. (1989) Alpha-actinins, calspectin (brain spectrin or fodorin), and actin participate in adhesion and movement of growth cones. Neuron 3, 311-319.
    • (1989) Neuron , vol.3 , pp. 311-319
    • Sobue, K.1    Kanda, K.2
  • 42
    • 0021827569 scopus 로고
    • Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells
    • Yamashiro-Matsumura S. and Matsumura F. (1985) Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells. J. Biol. Chem. 260, 5087-5097.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5087-5097
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 43
    • 0022535995 scopus 로고
    • Intracellular localization of the 55-kD actin-bundling protein in cultured cells: Spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin
    • Yamashiro-Matsumura S. and Matsumura F. (1986) Intracellular localization of the 55-kD actin-bundling protein in cultured cells: spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin. J. Cell Biol. 103, 631-640.
    • (1986) J. Cell Biol. , vol.103 , pp. 631-640
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 44
    • 0028567840 scopus 로고
    • Measurement of growth cone adhesion to culture surfaces by micromanipulation
    • Zheng J., Buxbaum R. E., and Heidemann S. R. (1994) Measurement of growth cone adhesion to culture surfaces by micromanipulation. J. Cell Biol. 127, 2049-2060.
    • (1994) J. Cell Biol. , vol.127 , pp. 2049-2060
    • Zheng, J.1    Buxbaum, R.E.2    Heidemann, S.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.