메뉴 건너뛰기




Volumn 139, Issue 5, 1997, Pages 1243-1253

Capping protein terminates but does not initiate chemoattractant- induced actin assembly in Dictyostelium

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL PROTEIN; CHEMOATTRACTANT; RHODAMINE;

EID: 0030728491     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.5.1243     Document Type: Article
Times cited : (56)

References (44)
  • 1
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew, B., L. Minamide, and J. Hamburg. 1995. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270:17582-17587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.1    Minamide, L.2    Hamburg, J.3
  • 2
    • 0030033237 scopus 로고    scopus 로고
    • Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium
    • Aizawa, H., K. Sutoh, and I. Yahara. 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
  • 3
    • 0024632296 scopus 로고
    • A Dictyostelium mutant deficient in severin, an F-actin fragmenting protein, shows normal motility and chemotaxis
    • Andre, E., M. Brink, G. Gerisch, G. Isenberg, A. Noegel, M. Schleicher, J.E. Segall, and E. Wallraff. 1989. A Dictyostelium mutant deficient in severin, an F-actin fragmenting protein, shows normal motility and chemotaxis. J. Cell Biol. 108:985-995.
    • (1989) J. Cell Biol. , vol.108 , pp. 985-995
    • Andre, E.1    Brink, M.2    Gerisch, G.3    Isenberg, G.4    Noegel, A.5    Schleicher, M.6    Segall, J.E.7    Wallraff, E.8
  • 4
    • 0029954225 scopus 로고    scopus 로고
    • Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
    • Barkalow, K., W. Witke, D.J. Kwiatkowski, and J.H. Hartwig. 1996. Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J. Cell Biol. 134:389-399.
    • (1996) J. Cell Biol. , vol.134 , pp. 389-399
    • Barkalow, K.1    Witke, W.2    Kwiatkowski, D.J.3    Hartwig, J.H.4
  • 5
    • 0021326961 scopus 로고
    • Caffeine blocks activation of cyclic AMP synthesis in Dictyostelium discoideum
    • Brenner, M., and S.D. Thomas. 1980. Caffeine blocks activation of cyclic AMP synthesis in Dictyostelium discoideum. Dev. Biol. 101:136-146.
    • (1980) Dev. Biol. , vol.101 , pp. 136-146
    • Brenner, M.1    Thomas, S.D.2
  • 7
    • 0026045382 scopus 로고
    • Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution
    • Cano, M.L., D. Lauffenburger, and S.H. Zigmond. 1991. Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution. J. Cell Biol. 115:677-687.
    • (1991) J. Cell Biol. , vol.115 , pp. 677-687
    • Cano, M.L.1    Lauffenburger, D.2    Zigmond, S.H.3
  • 9
    • 0031908252 scopus 로고    scopus 로고
    • EGF stimulates an increase in actin nucleation and filament number at the tip of the lamellipod in mammary adenocarcinoma cells
    • In press
    • Chan, A.Y., S. Raft, M. Bailly, J.B. Wyckoff, J.E. Segall, and J.S. Condeelis. 1997. EGF stimulates an increase in actin nucleation and filament number at the tip of the lamellipod in mammary adenocarcinoma cells. J. Cell Sci. In press.
    • (1997) J. Cell Sci.
    • Chan, A.Y.1    Raft, S.2    Bailly, M.3    Wyckoff, J.B.4    Segall, J.E.5    Condeelis, J.S.6
  • 10
    • 0027333420 scopus 로고
    • Life at the leading edge: The formation of cells protrusions
    • Condeelis, J. 1993. Life at the leading edge: the formation of cells protrusions. Annu. Rev. Cell Biol. 9:411-444.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 11
    • 0028919541 scopus 로고
    • Genetic deletion of ABP-120 alters the three-dimensional organization of actin filaments in Dictyostelium pseudopods
    • Cox, D., J.A. Ridsdale, J. Condeelis, and J. Hartwig. 1995. Genetic deletion of ABP-120 alters the three-dimensional organization of actin filaments in Dictyostelium pseudopods. J. Cell Biol. 128:819-835.
    • (1995) J. Cell Biol. , vol.128 , pp. 819-835
    • Cox, D.1    Ridsdale, J.A.2    Condeelis, J.3    Hartwig, J.4
  • 12
    • 0001941269 scopus 로고
    • A novel technique for gentle lysis of eucaryotic cells: Isolation of plasma membranes from Dictyostelium discoideum
    • Das, O.P., and E.J. Henderson. 1983. A novel technique for gentle lysis of eucaryotic cells: isolation of plasma membranes from Dictyostelium discoideum. Biochim. Biophys. Acta. 736:45-56.
    • (1983) Biochim. Biophys. Acta , vol.736 , pp. 45-56
    • Das, O.P.1    Henderson, E.J.2
  • 13
    • 0024595208 scopus 로고
    • Changes in the association of actin-binding proteins with the actin cytoskeleton during chemotactic stimulation of Dictyostelium discoideum
    • Dharmawardhane, S., V. Warren, A. Hall, and J. Condeelis. 1989. Changes in the association of actin-binding proteins with the actin cytoskeleton during chemotactic stimulation of Dictyostelium discoideum. Cell Motil. Cytoskeleton. 13:57-63.
    • (1989) Cell Motil. Cytoskeleton , vol.13 , pp. 57-63
    • Dharmawardhane, S.1    Warren, V.2    Hall, A.3    Condeelis, J.4
  • 14
    • 0028882496 scopus 로고
    • Actin filament barbed end capping activity in neutrophil lysates: The role of capping protein beta-2
    • DiNubile, M., L. Cassimeris, M. Joyce, and S. Zigmond. 1995. Actin filament barbed end capping activity in neutrophil lysates: the role of capping protein beta-2. Mol. Biol. Cell. 6:1659-1671.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1659-1671
    • DiNubile, M.1    Cassimeris, L.2    Joyce, M.3    Zigmond, S.4
  • 15
    • 0027374495 scopus 로고
    • Aginactin, an agonist-regulated F-actin capping activity is associated with an Hsc70 in Dictyostelium
    • Eddy, R.J., R.A. Sauterer, and J.S. Condeelis. 1993. Aginactin, an agonist-regulated F-actin capping activity is associated with an Hsc70 in Dictyostelium. J. Biol. Chem. 268:23267-23274.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23267-23274
    • Eddy, R.J.1    Sauterer, R.A.2    Condeelis, J.S.3
  • 16
    • 0030581758 scopus 로고    scopus 로고
    • A major agonist-regulated capping activity in Dictyostelium is due the capping protein, cap32/ 34
    • Eddy, R.J., J. Han, R.A. Sauterer, and J.S. Condeelis. 1996. A major agonist-regulated capping activity in Dictyostelium is due the capping protein, cap32/ 34. Biochim. Biophys. Acta. 1314:247-259.
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 247-259
    • Eddy, R.J.1    Han, J.2    Sauterer, R.A.3    Condeelis, J.S.4
  • 17
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable helix
    • Egelman, E.H., N. Francis, and D.D. DeRosier. 1982. F-actin is a helix with a random variable helix. Nature. 289:131-135.
    • (1982) Nature , vol.289 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.D.3
  • 18
    • 0018502551 scopus 로고
    • Oscillations of cyclic nucleotide concentrations in relation to the excitability of Dictyostelium cells
    • Gerisch, G., D. Malchow, W. Roos, and U. Wick. 1979. Oscillations of cyclic nucleotide concentrations in relation to the excitability of Dictyostelium cells. J. Exp. Biol. 81:33-47.
    • (1979) J. Exp. Biol. , vol.81 , pp. 33-47
    • Gerisch, G.1    Malchow, D.2    Roos, W.3    Wick, U.4
  • 19
    • 0026803329 scopus 로고
    • Probing actin and liposome interaction of talin and talin-vinculin complexes: A kinetic, thermodynamic, and lipid labeling study
    • Goldman, W.H., V. Niggli, S. Kaufmann, and G. Isenberg. 1992. Probing actin and liposome interaction of talin and talin-vinculin complexes: a kinetic, thermodynamic, and lipid labeling study. Biochemistry. 31:7665-7671.
    • (1992) Biochemistry , vol.31 , pp. 7665-7671
    • Goldman, W.H.1    Niggli, V.2    Kaufmann, S.3    Isenberg, G.4
  • 20
    • 0024044667 scopus 로고
    • Relationship of pseudopod extension to chemotactic hormone-induced actin polymerization in amoeboid cells
    • Hall, A.L., A. Schlein, and J. Condeelis. 1988. Relationship of pseudopod extension to chemotactic hormone-induced actin polymerization in amoeboid cells. J. Cell. Biochem. 37:285-299.
    • (1988) J. Cell. Biochem. , vol.37 , pp. 285-299
    • Hall, A.L.1    Schlein, A.2    Condeelis, J.3
  • 21
    • 0024453412 scopus 로고
    • Identification of actin nucleation activity and polymerization inhibitor in amoeboid cells: Their regulation by chemotactic stimulation
    • Hall, A., V. Warren, S. Dharmawardhane, and J. Condeelis. 1989. Identification of actin nucleation activity and polymerization inhibitor in amoeboid cells: their regulation by chemotactic stimulation. J. Cell Biol. 109:2207-2213.
    • (1989) J. Cell Biol. , vol.109 , pp. 2207-2213
    • Hall, A.1    Warren, V.2    Dharmawardhane, S.3    Condeelis, J.4
  • 22
    • 0027317941 scopus 로고
    • The heat shock cognate protein from Dictyostelium affects actin polymerization through interaction with the actin-binding protein cap32/34
    • Haus, U., P. Trommler, P.R. Fisher, H. Hartmann, F. Lottspeich, A.A. Noegel, and M. Schleicher. 1993. The heat shock cognate protein from Dictyostelium affects actin polymerization through interaction with the actin-binding protein cap32/34. EMBO (Eur. Mol. Biol. Organ.) J. 12:3763-3771.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 3763-3771
    • Haus, U.1    Trommler, P.2    Fisher, P.R.3    Hartmann, H.4    Lottspeich, F.5    Noegel, A.A.6    Schleicher, M.7
  • 23
    • 0026783523 scopus 로고
    • Cap100, a novel phosphatidylinositol 4,5-bisphosphate-regulated protein that caps actin filaments but does not nucleate actin assembly
    • Hofmann, A., L. Eichinger, E. Andre, D. Rieger, and M. Schleicher. 1992. Cap100, a novel phosphatidylinositol 4,5-bisphosphate-regulated protein that caps actin filaments but does not nucleate actin assembly. Cell Motil. Cytoskeleton. 23:133-144.
    • (1992) Cell Motil. Cytoskeleton , vol.23 , pp. 133-144
    • Hofmann, A.1    Eichinger, L.2    Andre, E.3    Rieger, D.4    Schleicher, M.5
  • 24
  • 25
    • 0029065328 scopus 로고
    • Capping protein levels influence actin assembly and cell motility in Dictyostelium
    • Hug, C., P.Y. Jay, I. Reddy, J.G. McNally, P.C. Bridgman, E.L. Elson, and J.A. Cooper. 1995. Capping protein levels influence actin assembly and cell motility in Dictyostelium. Cell. 81:591-600.
    • (1995) Cell , vol.81 , pp. 591-600
    • Hug, C.1    Jay, P.Y.2    Reddy, I.3    McNally, J.G.4    Bridgman, P.C.5    Elson, E.L.6    Cooper, J.A.7
  • 26
    • 85012414651 scopus 로고
    • Electron microscopic studies on the structure of natural and synthetic protein filaments muscle
    • Huxley, H.E. 1963. Electron microscopic studies on the structure of natural and synthetic protein filaments muscle. J. Mol. Biol. 7:281-308.
    • (1963) J. Mol. Biol. , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 28
    • 0028919857 scopus 로고
    • A talin homologue of Dictyostelium rapidly assembles at the leading edge of cells in response to chemoattractant
    • Kreitmeier, M., G. Gerisch, C. Heizer, and A. Muller-Taubenberger. 1995. A talin homologue of Dictyostelium rapidly assembles at the leading edge of cells in response to chemoattractant. J. Cell Biol. 129:179-188.
    • (1995) J. Cell Biol. , vol.129 , pp. 179-188
    • Kreitmeier, M.1    Gerisch, G.2    Heizer, C.3    Muller-Taubenberger, A.4
  • 29
    • 0025993085 scopus 로고
    • Stopped-flow measurement of cytoskeletal contraction: Dictyostelium myosin II is specifically required for contraction of amoeba cytoskeletons
    • Kuczmarski, E.R., L. Palivos, C. Aguado, and Z.L. Yao. 1991. Stopped-flow measurement of cytoskeletal contraction: Dictyostelium myosin II is specifically required for contraction of amoeba cytoskeletons. J. Cell Biol. 114: 1191-1199.
    • (1991) J. Cell Biol. , vol.114 , pp. 1191-1199
    • Kuczmarski, E.R.1    Palivos, L.2    Aguado, C.3    Yao, Z.L.4
  • 31
    • 0020551238 scopus 로고
    • Changes in actin associated with the cytoskeleton following chemotactic stimulation of Dicyostelium discoideum
    • McRobbie, S.J., and P.C. Newell. 1983. Changes in actin associated with the cytoskeleton following chemotactic stimulation of Dicyostelium discoideum. Biochem. Biophys. Res. Commun. 115:351-359.
    • (1983) Biochem. Biophys. Res. Commun. , vol.115 , pp. 351-359
    • McRobbie, S.J.1    Newell, P.C.2
  • 32
    • 1842306167 scopus 로고
    • The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
    • Moon, A., and D.G. Drubin. 1995. The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol. Biol. Cell. 120:421-435.
    • (1995) Mol. Biol. Cell. , vol.120 , pp. 421-435
    • Moon, A.1    Drubin, D.G.2
  • 34
    • 0025099508 scopus 로고
    • Length distribution of F-actin in Dictyostelium discoideum
    • Podolski, J., and T. Steck. 1990. Length distribution of F-actin in Dictyostelium discoideum. J. Biol. Chem. 265:1312-1318.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1312-1318
    • Podolski, J.1    Steck, T.2
  • 35
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
    • Pollard, T.D., and J.A. Cooper. 1986. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem. 55:987-1035.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 36
    • 0027275348 scopus 로고
    • Distribution of F-actin elongation sites in lysed polymorphonuclear leukocytes parallels the distribution of endogenous F-actin
    • Redmond, T., and S.H. Zigmond. 1993. Distribution of F-actin elongation sites in lysed polymorphonuclear leukocytes parallels the distribution of endogenous F-actin. Cell Motil. Cytoskeleton. 26:7-18.
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 7-18
    • Redmond, T.1    Zigmond, S.H.2
  • 37
    • 0026332911 scopus 로고
    • Purification and characterization of aginactin, a newly identified agonist-regulated actin-capping protein from Dictyostelium
    • Sauterer, R.A., R.J. Eddy, A.L. Hall, and J.S. Condeelis. 1991. Purification and characterization of aginactin, a newly identified agonist-regulated actin-capping protein from Dictyostelium. J. Biol. Chem. 266:24533-24539.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24533-24539
    • Sauterer, R.A.1    Eddy, R.J.2    Hall, A.L.3    Condeelis, J.S.4
  • 40
    • 0025785552 scopus 로고
    • Control of actin polymerization in live and permeabilized fibroblasts
    • Symons, M., and T.J. Mitchison. 1991. Control of actin polymerization in live and permeabilized fibroblasts. J. Cell Biol. 114:503-513.
    • (1991) J. Cell Biol. , vol.114 , pp. 503-513
    • Symons, M.1    Mitchison, T.J.2
  • 41
    • 0028363603 scopus 로고
    • DNase 1 increases the rate constant of depolymerization at the pointed (-) end of actin filaments
    • Weber, A., C.R. Pennise, and M. Pring. 1994. DNase 1 increases the rate constant of depolymerization at the pointed (-) end of actin filaments. Biochemistry. 33:4780-4786.
    • (1994) Biochemistry , vol.33 , pp. 4780-4786
    • Weber, A.1    Pennise, C.R.2    Pring, M.3
  • 42
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M.D., A. Iwamatsu, and T.J. Mitchison. 1997. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature. 385:265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 43
    • 0024807220 scopus 로고
    • cAMP-mediated inhibition of intracellular particle movement and actin reorganization in Dictyostelium
    • Wessels, D., N.A. Schroeder, E. Voss, A.L. Hall, J. Condeelis, and D.R. Soll. 1989. cAMP-mediated inhibition of intracellular particle movement and actin reorganization in Dictyostelium. J. Cell Biol. 109:2841-2851.
    • (1989) J. Cell Biol. , vol.109 , pp. 2841-2851
    • Wessels, D.1    Schroeder, N.A.2    Voss, E.3    Hall, A.L.4    Condeelis, J.5    Soll, D.R.6
  • 44
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke, W., A.M. Sharpe, J.H. Hartwig, T. Azuma, T.P. Stossel, and D.J. Kwiatkowski. 1995. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell. 81:41-51.
    • (1995) Cell , vol.81 , pp. 41-51
    • Witke, W.1    Sharpe, A.M.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.