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Volumn 119, Issue 9, 2006, Pages 1947-1960

Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells

Author keywords

Actin bundling; CH domain; Fimbrin; Invasion; Motility

Indexed keywords

ALANINE; AMINO ACID; CALPONIN; COLLAGEN; DETERGENT; F ACTIN; GLUTAMINE; L PLASTIN PROTEIN; MEMBRANE PROTEIN; SERINE; UNCLASSIFIED DRUG;

EID: 33744536569     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.02874     Document Type: Article
Times cited : (91)

References (67)
  • 2
    • 0029084382 scopus 로고
    • Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily
    • Azim, A. C., Knoll, J. H., Beggs, A. H. and Chishti, A. H. (1995). Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily. J. Biol. Chem. 270, 17407-17413.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17407-17413
    • Azim, A.C.1    Knoll, J.H.2    Beggs, A.H.3    Chishti, A.H.4
  • 4
    • 0033981223 scopus 로고    scopus 로고
    • Parallel actin bundles and their multiple actin-bundling proteins
    • Bartles, J. R. (2000). Parallel actin bundles and their multiple actin-bundling proteins. Curr. Opin. Cell Biol. 12, 72-78.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 72-78
    • Bartles, J.R.1
  • 6
    • 0033527066 scopus 로고    scopus 로고
    • An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation
    • Bowden, E. T., Barth, M., Thomas, D., Glazer, R. I. and Mueller, S. C. (1999). An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation. Oncogene 18, 4440-4449.
    • (1999) Oncogene , vol.18 , pp. 4440-4449
    • Bowden, E.T.1    Barth, M.2    Thomas, D.3    Glazer, R.I.4    Mueller, S.C.5
  • 8
    • 0343980401 scopus 로고
    • Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro
    • Bretscher, A. (1981). Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro. Proc. Natl. Acad. Sci. USA 78, 6849-6853.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6849-6853
    • Bretscher, A.1
  • 9
  • 10
    • 3543114271 scopus 로고    scopus 로고
    • Foot and mouth: Podosomes, invadopodia and circular dorsal ruffles
    • Buccione, R., Orth, J. D. and McNiven, M. A. (2004). Foot and mouth: podosomes, invadopodia and circular dorsal ruffles. Nat. Rev. Mol. Cell. Biol. 5, 647-657.
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 647-657
    • Buccione, R.1    Orth, J.D.2    McNiven, M.A.3
  • 11
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen, C. A. and Okayama, H. (1988). Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. Biotechniques 6, 632-638.
    • (1988) Biotechniques , vol.6 , pp. 632-638
    • Chen, C.A.1    Okayama, H.2
  • 13
    • 4544371915 scopus 로고    scopus 로고
    • Phosphorylation of actopaxin regulates cell spreading and migration
    • Clarke, D. M., Brown, M. C., LaLonde, D. P. and Turner, C. E. (2004). Phosphorylation of actopaxin regulates cell spreading and migration. J. Cell Biol. 166, 901-912.
    • (2004) J. Cell Biol. , vol.166 , pp. 901-912
    • Clarke, D.M.1    Brown, M.C.2    LaLonde, D.P.3    Turner, C.E.4
  • 14
    • 0033598182 scopus 로고    scopus 로고
    • Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrin-vimentin complexes in macrophages
    • Correia, I., Chu, D., Chou, Y. H., Goldman, R. D. and Matsudaira, P. (1999). Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrin-vimentin complexes in macrophages. J. Cell Biol. 146, 831-842.
    • (1999) J. Cell Biol. , vol.146 , pp. 831-842
    • Correia, I.1    Chu, D.2    Chou, Y.H.3    Goldman, R.D.4    Matsudaira, P.5
  • 15
    • 0025091625 scopus 로고
    • Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins
    • de Arruda, M. V., Watson, S., Lin, C. S., Leavitt, J. and Matsudaira, P. (1990). Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins. J. Cell Biol. 111, 1069-1079.
    • (1990) J. Cell Biol. , vol.111 , pp. 1069-1079
    • de Arruda, M.V.1    Watson, S.2    Lin, C.S.3    Leavitt, J.4    Matsudaira, P.5
  • 17
    • 0037512351 scopus 로고    scopus 로고
    • Macrophage podosomes assemble at the leading lamella by growth and fragmentation
    • Evans, J. G., Correia, I., Krasavina, O., Watson, N. and Matsudaira, P. (2003). Macrophage podosomes assemble at the leading lamella by growth and fragmentation. J. Cell Biol. 161, 697-705.
    • (2003) J. Cell Biol. , vol.161 , pp. 697-705
    • Evans, J.G.1    Correia, I.2    Krasavina, O.3    Watson, N.4    Matsudaira, P.5
  • 19
    • 0024317269 scopus 로고
    • Villin induces microvilli growth and actin redistribution in transfected fibroblasts
    • Friederich, E., Huet, C., Arpin, M. and Louvard, D. (1989). Villin induces microvilli growth and actin redistribution in transfected fibroblasts. Cell 59, 461-475.
    • (1989) Cell , vol.59 , pp. 461-475
    • Friederich, E.1    Huet, C.2    Arpin, M.3    Louvard, D.4
  • 20
    • 0026773096 scopus 로고
    • An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
    • Friederich, E., Vancompernolle, K., Huet, C., Goethals, M., Finidori, J., Vandekerckhove, J. and Louvard, D. (1992). An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell 70, 81-92.
    • (1992) Cell , vol.70 , pp. 81-92
    • Friederich, E.1    Vancompernolle, K.2    Huet, C.3    Goethals, M.4    Finidori, J.5    Vandekerckhove, J.6    Louvard, D.7
  • 21
    • 0033578936 scopus 로고    scopus 로고
    • Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro
    • Friederich, E., Vancompernolle, K., Louvard, D. and Vandekerckhove, J. (1999). Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro. J. Biol. Chem. 274, 26751-26760.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26751-26760
    • Friederich, E.1    Vancompernolle, K.2    Louvard, D.3    Vandekerckhove, J.4
  • 22
    • 1642282882 scopus 로고    scopus 로고
    • Prespecification and plasticity: Shifting mechanisms of cell migration
    • Friedl, P. (2004). Prespecification and plasticity: shifting mechanisms of cell migration. Curr. Opin. Cell Biol. 16, 14-23.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 14-23
    • Friedl, P.1
  • 23
    • 0034631843 scopus 로고    scopus 로고
    • Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane
    • Gautreau, A., Louvard, D. and Arpin, M. (2000). Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane. J. Cell Biol. 150, 193-203.
    • (2000) J. Cell Biol. , vol.150 , pp. 193-203
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3
  • 24
    • 0642286487 scopus 로고    scopus 로고
    • The actin cytoskeleton as a therapeutic target: State of the art and future directions
    • Giganti, A. and Friederich, E. (2003). The actin cytoskeleton as a therapeutic target: state of the art and future directions. Prog. Cell Cycle Res. 5, 511-525.
    • (2003) Prog. Cell Cycle Res. , vol.5 , pp. 511-525
    • Giganti, A.1    Friederich, E.2
  • 27
    • 0019780969 scopus 로고
    • F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments
    • Glenney, J. R., Jr, Kaulfus, P., Matsudaira, P. and Weber, K. (1981). F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments. J. Biol. Chem. 256, 9283-9288.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9283-9288
    • Glenney Jr., J.R.1    Kaulfus, P.2    Matsudaira, P.3    Weber, K.4
  • 28
    • 0034880196 scopus 로고    scopus 로고
    • Phosphorylation of filamin (ABP-280) regulates the binding to the lipid membrane, integrin, and actin
    • Goldmann, W. H. (2001). Phosphorylation of filamin (ABP-280) regulates the binding to the lipid membrane, integrin, and actin. Cell Biol. Int. 25, 805-809.
    • (2001) Cell Biol. Int. , vol.25 , pp. 805-809
    • Goldmann, W.H.1
  • 29
    • 0022338863 scopus 로고
    • Abundant synthesis of the transformation-induced protein of neoplastic human fibroblasts, plastin, in normal lymphocytes
    • Goldstein, D., Djeu, J., Latter, G., Burbeck, S. and Leavitt, J. (1985). Abundant synthesis of the transformation-induced protein of neoplastic human fibroblasts, plastin, in normal lymphocytes. Cancer Res. 45, 5643-5647.
    • (1985) Cancer Res. , vol.45 , pp. 5643-5647
    • Goldstein, D.1    Djeu, J.2    Latter, G.3    Burbeck, S.4    Leavitt, J.5
  • 30
    • 0034613254 scopus 로고    scopus 로고
    • Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin
    • Harbeck, B., Huttelmaier, S., Schluter, K., Jockusch, B. M. and Menberger, S. (2000). Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin. J. Biol. Chem. 275, 30817-30825.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30817-30825
    • Harbeck, B.1    Huttelmaier, S.2    Schluter, K.3    Jockusch, B.M.4    Menberger, S.5
  • 31
    • 0028351807 scopus 로고
    • Serine phosphorylation of a 67-kDa protein in human T lymphocytes represents an accessory receptor-mediated signaling event
    • Henning, S. W., Meuer, S. C. and Samstag, Y. (1994). Serine phosphorylation of a 67-kDa protein in human T lymphocytes represents an accessory receptor-mediated signaling event. J. Immunol. 152, 4808-4815.
    • (1994) J. Immunol. , vol.152 , pp. 4808-4815
    • Henning, S.W.1    Meuer, S.C.2    Samstag, Y.3
  • 32
    • 3042794572 scopus 로고    scopus 로고
    • Regulation of actin-based cell migration by cAMP/PKA
    • Howe, A. K. (2004). Regulation of actin-based cell migration by cAMP/ PKA. Biochim. Biophys. Acta 1692, 159-174.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 159-174
    • Howe, A.K.1
  • 33
  • 34
    • 0035800777 scopus 로고    scopus 로고
    • The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylaLed on its actin-binding domain by the focal adhesion kinase
    • Izaguirre, G., Aguirre, L., Hu, Y. P., Lee, H. Y., Schlaepfer, D. D., Aneskievich, B. J. and Haimovich, B. (2001). The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylaLed on its actin-binding domain by the focal adhesion kinase. J. Biol. Chem. 276, 28676-28685.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28676-28685
    • Izaguirre, G.1    Aguirre, L.2    Hu, Y.P.3    Lee, H.Y.4    Schlaepfer, D.D.5    Aneskievich, B.J.6    Haimovich, B.7
  • 35
    • 0032882539 scopus 로고    scopus 로고
    • Autocrine TGF-beta-regulated expression of adhesion receptors and integrin-linked kinase in HT-144 melanoma cells correlates with their metastatic phenotype
    • Janji, B., Melchior, C., Gonna, V., Vallar, L. and Kieffer, N. (1999). Autocrine TGF-beta-regulated expression of adhesion receptors and integrin-linked kinase in HT-144 melanoma cells correlates with their metastatic phenotype. Int. J. Cancer 83, 255-262.
    • (1999) Int. J. Cancer , vol.83 , pp. 255-262
    • Janji, B.1    Melchior, C.2    Gonna, V.3    Vallar, L.4    Kieffer, N.5
  • 36
    • 0029666259 scopus 로고    scopus 로고
    • FcgammaRII-mediated adhesion and phagocytosis induce L-plastin pbosphorylation in human neutrophils
    • Jones, S. L. and Brown, E. J. (1996). FcgammaRII-mediated adhesion and phagocytosis induce L-plastin pbosphorylation in human neutrophils. J. Biol. Chem. 271, 14623-14630.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14623-14630
    • Jones, S.L.1    Brown, E.J.2
  • 37
    • 0032483008 scopus 로고    scopus 로고
    • A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function
    • Jones, S. L., Wang, J., Turck, C. W. and Brown, E. J. (1998). A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function. Proc. Natl. Acad. Sci. USA 95, 9331-9336.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9331-9336
    • Jones, S.L.1    Wang, J.2    Turck, C.W.3    Brown, E.J.4
  • 38
    • 0037205427 scopus 로고    scopus 로고
    • Macrophage/microglia-specific protein Iba1 enhances membrane ruffling and Rac activation via phospholipase C-gamma-dependent pathway
    • Kanazawa, H., Ohsawa, K., Sasaki, Y., Kohsaka, S. and Imai, Y. (2002). Macrophage/microglia-specific protein Iba1 enhances membrane ruffling and Rac activation via phospholipase C-gamma-dependent pathway. J. Biol. Chem. 277, 20026-20032.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20026-20032
    • Kanazawa, H.1    Ohsawa, K.2    Sasaki, Y.3    Kohsaka, S.4    Imai, Y.5
  • 39
    • 27844596295 scopus 로고    scopus 로고
    • Filamin is essential for shedding of the transmembrane serine protease, epithin
    • Kim, C., Cho, Y., Kang, C. H., Kim, M. G., Lee, H., Cho, E. G. and Park, D. (2005). Filamin is essential for shedding of the transmembrane serine protease, epithin. EMBO Rep. 6, 1045-1051.
    • (2005) EMBO Rep. , vol.6 , pp. 1045-1051
    • Kim, C.1    Cho, Y.2    Kang, C.H.3    Kim, M.G.4    Lee, H.5    Cho, E.G.6    Park, D.7
  • 42
    • 0027466284 scopus 로고
    • Characterization of the human L-plastin gene promoter in normal and neoplastic cells
    • Lin, C. S., Chen, Z. P., Park, T., Ghosh, K. and Leavitt, J. (1993a). Characterization of the human L-plastin gene promoter in normal and neoplastic cells. J. Biol. Chem. 268, 2793-2801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2793-2801
    • Lin, C.S.1    Chen, Z.P.2    Park, T.3    Ghosh, K.4    Leavitt, J.5
  • 43
    • 0027511422 scopus 로고
    • Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells
    • Lin, C. S., Park, T., Chen, Z. P. and Leavitt, J. (1993b). Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells. J. Biol. Chem. 268, 2781-2792.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2781-2792
    • Lin, C.S.1    Park, T.2    Chen, Z.P.3    Leavitt, J.4
  • 44
    • 0032442866 scopus 로고    scopus 로고
    • Analysis and mapping of plastin phosphorylation
    • Lin, C. S., Lau, A. and Lue, T. F. (1998). Analysis and mapping of plastin phosphorylation. DNA Cell Biol. 17, 1041-1046.
    • (1998) DNA Cell Biol. , vol.17 , pp. 1041-1046
    • Lin, C.S.1    Lau, A.2    Lue, T.F.3
  • 45
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: Adhesion hot-spots of invasive cells
    • Linder, S. and Aepfelbacher, M. (2003). Podosomes: adhesion hot-spots of invasive cells. Trends Cell. Biol. 13, 376-385.
    • (2003) Trends Cell. Biol. , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 46
    • 0346849715 scopus 로고    scopus 로고
    • Espin cross-links cause the elongation of microvillus-type parallel actin bundles in vivo
    • Loomis, P. A., Zheng, L., Sekerkova, G., Changyaleket, B., Mugnaini, E. and Bartles, J. R. (2003). Espin cross-links cause the elongation of microvillus-type parallel actin bundles in vivo. J. Cell Biol. 163, 1045-1055.
    • (2003) J. Cell Biol. , vol.163 , pp. 1045-1055
    • Loomis, P.A.1    Zheng, L.2    Sekerkova, G.3    Changyaleket, B.4    Mugnaini, E.5    Bartles, J.R.6
  • 47
    • 0023892762 scopus 로고
    • Purification and characterization of a cytosolic 65-kilodalton phosphoprotein in human leukocytes whose phosphorylation is augmented by stimulation with interleukin 1
    • Matsushima, K., Shiroo, M., Kung, H. F. and Copeland, T. D. (1988). Purification and characterization of a cytosolic 65-kilodalton phosphoprotein in human leukocytes whose phosphorylation is augmented by stimulation with interleukin 1. Biochemistry 27, 3765-3770.
    • (1988) Biochemistry , vol.27 , pp. 3765-3770
    • Matsushima, K.1    Shiroo, M.2    Kung, H.F.3    Copeland, T.D.4
  • 48
    • 0027324435 scopus 로고
    • Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages
    • Messier, J. M., Shaw, L. M., Chafel, M., Matsudaira, P. and Mercurio, A. M. (1993). Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages. Cell Motil. Cytoskeleton 25, 223-233.
    • (1993) Cell Motil. Cytoskeleton , vol.25 , pp. 223-233
    • Messier, J.M.1    Shaw, L.M.2    Chafel, M.3    Matsudaira, P.4    Mercurio, A.M.5
  • 49
    • 0036468250 scopus 로고    scopus 로고
    • Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts
    • Mizutani, K., Miki, H., He, H., Maruta, H. and Takenaws, T. (2002). Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts. Cancer Res. 62, 669-674.
    • (2002) Cancer Res. , vol.62 , pp. 669-674
    • Mizutani, K.1    Miki, H.2    He, H.3    Maruta, H.4    Takenaws, T.5
  • 50
    • 0026468443 scopus 로고
    • Human T cell L-plastin bundles actin filaments in a calcium-dependent manner
    • Namba, Y., Ito, M., Zu, Y., Shigesada, K. and Maruyama, K. (1992). Human T cell L-plastin bundles actin filaments in a calcium-dependent manner. J. Biochem. 112, 503-507.
    • (1992) J. Biochem. , vol.112 , pp. 503-507
    • Namba, Y.1    Ito, M.2    Zu, Y.3    Shigesada, K.4    Maruyama, K.5
  • 51
    • 1042301226 scopus 로고    scopus 로고
    • Microglia/macrophage-specific protein Iba1 binds to fimbrin and enhances its actin-bundling activity
    • Ohsawa, K., Imai, Y., Sasaki, Y. and Kohsaka, S. (2004). Microglia/ macrophage-specific protein Iba1 binds to fimbrin and enhances its actin-bundling activity. J. Neurochem. 88, 844-856.
    • (2004) J. Neurochem. , vol.88 , pp. 844-856
    • Ohsawa, K.1    Imai, Y.2    Sasaki, Y.3    Kohsaka, S.4
  • 52
    • 0942268724 scopus 로고    scopus 로고
    • N-Formy1 peptide receptor subtypes in human neutrophils activate L-plastin phosphorylation through different signal transduction intermediates
    • Paclet, M. H., Davis, C., Kotsonis, P., Godovac-Zimmermann, J., Segal, A. W. and Dekker, L. V. (2004). N-Formy1 peptide receptor subtypes in human neutrophils activate L-plastin phosphorylation through different signal transduction intermediates. Biochem. J. 377, 469-477.
    • (2004) Biochem. J. , vol.377 , pp. 469-477
    • Paclet, M.H.1    Davis, C.2    Kotsonis, P.3    Godovac-Zimmermann, J.4    Segal, A.W.5    Dekker, L.V.6
  • 53
    • 23444443067 scopus 로고
    • Activation of the leukocyte plastin gene occurs in most human cancer cells
    • Park, T., Chen, Z. P. and Leavitt, J. (1994). Activation of the leukocyte plastin gene occurs in most human cancer cells. Cancer Res. 54, 1775-1781.
    • (1994) Cancer Res. , vol.54 , pp. 1775-1781
    • Park, T.1    Chen, Z.P.2    Leavitt, J.3
  • 54
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D. and Borisy, G. G. (2003). Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 56
    • 0037244777 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in T lymphocyte activation and migration
    • Samstag, Y., Eibert, S. M., Klemke, M. and Wabnitz, G. H. (2003). Actin cytoskeletal dynamics in T lymphocyte activation and migration. J. Leukoc. Biol. 73, 30-48.
    • (2003) J. Leukoc. Biol. , vol.73 , pp. 30-48
    • Samstag, Y.1    Eibert, S.M.2    Klemke, M.3    Wabnitz, G.H.4
  • 57
    • 20444426470 scopus 로고    scopus 로고
    • The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia
    • Schirenbeck, A., Bretschneider, T., Arasada, R., Schleicher, M. and Faix, J. (2005). The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. Nat. Cell Biol. 7, 619-625.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 619-625
    • Schirenbeck, A.1    Bretschneider, T.2    Arasada, R.3    Schleicher, M.4    Faix, J.5
  • 58
    • 0027216620 scopus 로고
    • Characterization of a 64-kd protein phosphorylated during chemotactic activation with IL-8 and fMLP of human polymorphonuclear leukocytes. I. Phosphorylation of a 64-kd protein and other proteins
    • Shibata, M., Ohoka, T., Mizuno, S. and Suzuki, K. (1993). Characterization of a 64-kd protein phosphorylated during chemotactic activation with IL-8 and fMLP of human polymorphonuclear leukocytes. I. Phosphorylation of a 64-kd protein and other proteins. J. Leukoc. Biol. 54, 1-9.
    • (1993) J. Leukoc. Biol. , vol.54 , pp. 1-9
    • Shibata, M.1    Ohoka, T.2    Mizuno, S.3    Suzuki, K.4
  • 59
    • 0028933571 scopus 로고
    • Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide
    • Shinomiya, H., Hagi, A., Fukuzumi, M., Mizobuchi, M., Hirata, H. and Utsumi, S. (1995). Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide. J. Immunol. 154, 3471-3478.
    • (1995) J. Immunol. , vol.154 , pp. 3471-3478
    • Shinomiya, H.1    Hagi, A.2    Fukuzumi, M.3    Mizobuchi, M.4    Hirata, H.5    Utsumi, S.6
  • 60
    • 0020528725 scopus 로고
    • Immunohistochemical identification and localization of actin and fimbrin in vestibular hair cells in the normal guinea pig and in a strain of the waltzing guinea pig
    • Sobin, A. and Flock, A. (1983). Immunohistochemical identification and localization of actin and fimbrin in vestibular hair cells in the normal guinea pig and in a strain of the waltzing guinea pig. Acta Otolaryngol. 96, 407-412.
    • (1983) Acta Otolaryngol. , vol.96 , pp. 407-412
    • Sobin, A.1    Flock, A.2
  • 63
    • 0022656421 scopus 로고
    • Electric field-mediated DNA transfer: Transient and stable gene expression in human and mouse lymphoid cells
    • Toneguzzo, F., Hayday, A. C. and Keating, A. (1986). Electric field-mediated DNA transfer: transient and stable gene expression in human and mouse lymphoid cells. Mol. Cell. Biol. 6, 703-706.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 703-706
    • Toneguzzo, F.1    Hayday, A.C.2    Keating, A.3
  • 64
    • 0035947761 scopus 로고    scopus 로고
    • An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function
    • Volkmann, N., DeRosier, D., Matsudaira, P. and Hanein, D. (2001). An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function. J. Cell Biol. 153, 947-956.
    • (2001) J. Cell Biol. , vol.153 , pp. 947-956
    • Volkmann, N.1    DeRosier, D.2    Matsudaira, P.3    Hanein, D.4
  • 65
    • 0033588228 scopus 로고    scopus 로고
    • Immune complex-induced integrin activation and L-plastin phosphorylation require protein kinase A
    • Wang, J. and Brown, E. J. (1999). Immune complex-induced integrin activation and L-plastin phosphorylation require protein kinase A. J. Biol. Chem. 274, 24349-24356.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24349-24356
    • Wang, J.1    Brown, E.J.2
  • 66
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex
    • Weed, S. A., Karginov, A. V., Schafer, D. A., Weaver, A. M., Kinley, A. W., Cooper, J. A. and Parsons, J. T. (2000). Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex. J. Cell Biol. 151, 29-40.
    • (2000) J. Cell Biol. , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3    Weaver, A.M.4    Kinley, A.W.5    Cooper, J.A.6    Parsons, J.T.7
  • 67
    • 0033016391 scopus 로고    scopus 로고
    • Suppression of prostate carcinoma cell invasion by expression of antisense L-plastin gene
    • Zheng, J., Rudra-Ganguly, N., Powell, W. C. and Roy-Burman, P. (1999). Suppression of prostate carcinoma cell invasion by expression of antisense L-plastin gene. Am. J. Pathol. 155, 115-122.
    • (1999) Am. J. Pathol. , vol.155 , pp. 115-122
    • Zheng, J.1    Rudra-Ganguly, N.2    Powell, W.C.3    Roy-Burman, P.4


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