메뉴 건너뛰기




Volumn 56, Issue , 1994, Pages 169-191

Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly

Author keywords

actin; actin binding proteins; Ca2+; cytoskeleton; phosphoinositide; PIP2; polymerization

Indexed keywords

ACTIN BINDING PROTEIN; CALCIUM; PHOSPHATIDYLINOSITIDE;

EID: 0028274104     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.ph.56.030194.001125     Document Type: Review
Times cited : (476)

References (143)
  • 1
    • 0025983823 scopus 로고
    • Requirement of yeast fimbrin for actin organization and morphogenesis in vivo
    • Adams AE, Botstein D, Drubin DG. 1991. Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature 354:404-8
    • (1991) Nature , vol.354 , pp. 404-408
    • Adams, A.E.1    Botstein, D.2    Drubin, D.G.3
  • 2
    • 0024346185 scopus 로고
    • Binding of myosin I to membrane lipids
    • Adams RJ, Pollard TD. 1989. Binding of myosin I to membrane lipids. Nature 340:565-68
    • (1989) Nature , vol.340 , pp. 565-568
    • Adams, R.J.1    Pollard, T.D.2
  • 3
    • 0022344815 scopus 로고
    • Effect of actin filament length and filament number concentration on the actin-activated ATPase activity of Acanthamoeba myosin I
    • Albanesi JP, Coue M, Fujisaki H, Korn ED. 1985. Effect of actin filament length and filament number concentration on the actin-activated ATPase activity of Acanthamoeba myosin I. J. Biol. Chem. 260:13276-80
    • (1985) J. Biol. Chem. , vol.260 , pp. 13276-13280
    • Albanesi, J.P.1    Coue, M.2    Fujisaki, H.3    Korn, E.D.4
  • 4
    • 0027058138 scopus 로고
    • Range of messenger action of calcium ion and inositol 1,4,5-trisphosphate
    • Allbritton NL, Meyer T, Stryer L. 1992. Range of messenger action of calcium ion and inositol 1,4,5-trisphosphate. Science 258:1812-15
    • (1992) Science , vol.258 , pp. 1812-1815
    • Allbritton, N.L.1    Meyer, T.2    Stryer, L.3
  • 5
    • 0022430243 scopus 로고
    • Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide
    • Anderson RA, Marchesi VT. 1985. Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide. Nature 318:295-98
    • (1985) Nature , vol.318 , pp. 295-298
    • Anderson, R.A.1    Marchesi, V.T.2
  • 6
    • 0024977497 scopus 로고
    • 2+/calmodulin-dependent actin-binding proteins from squid retina
    • 2+/calmodulin-dependent actin-binding proteins from squid retina. FEBS Lett. 247:377-80
    • (1989) FEBS Lett. , vol.247 , pp. 377-380
    • Asai, H.1    Arai, T.2    Fujii, T.3    Matsumoto, G.4
  • 7
    • 0023571668 scopus 로고
    • Distribution and cellular localization of actin depolymerizing factor
    • Bamburg J, Bray D. 1987. Distribution and cellular localization of actin depolymerizing factor. J. Cell Biol. 105: 2817-25
    • (1987) J. Cell Biol. , vol.105 , pp. 2817-2825
    • Bamburg, J.1    Bray, D.2
  • 8
    • 0026703001 scopus 로고
    • Effects of gelsolin on human platelet cytosolic phosphoinositide-phospholipase C isozymes
    • Banno Y, Nakashima T, Kumada T, Ebisawa K, Nonomura Y, et al. 1992. Effects of gelsolin on human platelet cytosolic phosphoinositide-phospholipase C isozymes. J. Biol. Chem. 267: 6488-94
    • (1992) J. Biol. Chem. , vol.267 , pp. 6488-6494
    • Banno, Y.1    Nakashima, T.2    Kumada, T.3    Ebisawa, K.4    Nonomura, Y.5
  • 9
    • 0024210679 scopus 로고
    • Increased breakdown of phosphatidylinositol 4,5-bisphosphate is not an initiating factor for actin assembly in human neutrophils
    • Bengtsson T, Rundquist I, Stendahl O, Wymann MP, Andersson T. 1988. Increased breakdown of phosphatidylinositol 4,5-bisphosphate is not an initiating factor for actin assembly in human neutrophils. J. Biol. Chem. 263:17385-89
    • (1988) J. Biol. Chem. , vol.263 , pp. 17385-17389
    • Bengtsson, T.1    Rundquist, I.2    Stendahl, O.3    Wymann, M.P.4    Andersson, T.5
  • 10
    • 0026341510 scopus 로고
    • Calcium gradients underlying polarization and chemotaxis of eosinophils
    • Brundage RA, Fogarty KE, Tuft RA, Fay FS. 1991. Calcium gradients underlying polarization and chemotaxis of eosinophils. Science 254:703-6
    • (1991) Science , vol.254 , pp. 703-706
    • Brundage, R.A.1    Fogarty, K.E.2    Tuft, R.A.3    Fay, F.S.4
  • 11
    • 0023894120 scopus 로고
    • Gelsolin has three actin-binding sites
    • Bryan J. 1988. Gelsolin has three actin-binding sites. J. Cell Biol. 106: 1553-62
    • (1988) J. Cell Biol. , vol.106 , pp. 1553-1562
    • Bryan, J.1
  • 12
    • 0026060508 scopus 로고
    • Calcium, the cytoskeleton and calpactin (annexin II) in exocytotic secretion from adrenal chromaffin and mammary epithelial cells
    • Burgoyne RD, Handel SE, Morgan A, Rennison ME, Turner MD, et al. 1991. Calcium, the cytoskeleton and calpactin (annexin II) in exocytotic secretion from adrenal chromaffin and mammary epithelial cells. Biochem. Soc. Trans. 19:1085-90
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 1085-1090
    • Burgoyne, R.D.1    Handel, S.E.2    Morgan, A.3    Rennison, M.E.4    Turner, M.D.5
  • 13
    • 0023837782 scopus 로고
    • Phosphatidylinositol cycle and its possible involvement in the regulation of cytoskeleton-membrane interactions
    • Burn P. 1988. Phosphatidylinositol cycle and its possible involvement in the regulation of cytoskeleton-membrane interactions. J. Cell. Biochem. 36:15-24
    • (1988) J. Cell. Biochem. , vol.36 , pp. 15-24
    • Burn, P.1
  • 14
    • 0021923779 scopus 로고
    • Diacylglycerol in large alpha-actinin/actin complexes and in the cytoskeleton of activated platelets
    • Burn P, Rotman A, Meyer RK, Burger MM. 1985. Diacylglycerol in large alpha-actinin/actin complexes and in the cytoskeleton of activated platelets. Nature 314:469-72
    • (1985) Nature , vol.314 , pp. 469-472
    • Burn, P.1    Rotman, A.2    Meyer, R.K.3    Burger, M.M.4
  • 15
    • 0002218364 scopus 로고
    • Profilin, a low molecular weight protein controlling actin polymerisabiiity
    • ed. SV Perry, A Margreth, RS Adelstein, Amsterdam: Elsevier/North-Holland
    • Carlsson L, Nystrom LE, Sundkvist I, Markey F, Lindberg U. 1976. Profilin, a low molecular weight protein controlling actin polymerisabiiity. In Contractile Systems in Non-muscle Tissues, ed. SV Perry, A Margreth, RS Adelstein, pp. 39-49. Amsterdam: Elsevier/North-Holland
    • (1976) Contractile Systems in Non-muscle Tissues , pp. 39-49
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 16
    • 0023008203 scopus 로고
    • The actin filament-severing domain of plasma gelsolin
    • Chaponnier C, Janmey PA, Yin HL. 1986. The actin filament-severing domain of plasma gelsolin. J. Cell Biol. 103:1473-81
    • (1986) J. Cell Biol. , vol.103 , pp. 1473-1481
    • Chaponnier, C.1    Janmey, P.A.2    Yin, H.L.3
  • 18
    • 0025984501 scopus 로고
    • Myosin I: A new insight into the mechanism and cellular significance of actin-based motility
    • Collins K, Sellers J, Matsudaira P. 1991. Myosin I: a new insight into the mechanism and cellular significance of actin-based motility. Adv. Biophys. 27:221-26
    • (1991) Adv. Biophys. , vol.27 , pp. 221-226
    • Collins, K.1    Sellers, J.2    Matsudaira, P.3
  • 19
    • 0022619258 scopus 로고
    • Purification and characterization of actophorin, a new 15,000-dalton actin-hinding protein from Acanthamoeba castellinii
    • Cooper JA, Blum JD, Williams RC, Pollard TD. 1986. Purification and characterization of actophorin, a new 15,000-dalton actin-hinding protein from Acanthamoeba castellinii. J. Biol. Chem. 261:477-85
    • (1986) J. Biol. Chem. , vol.261 , pp. 477-485
    • Cooper, J.A.1    Blum, J.D.2    Williams, R.C.3    Pollard, T.D.4
  • 20
    • 0026768703 scopus 로고
    • Molecular cloning of human macrophage capping protein cDNA. A unique member of the gelsolin/villin family expressed primarily in macrophages
    • Dabiri GA, Young CL, Rosenbloom J, Southwick FS. 1992. Molecular cloning of human macrophage capping protein cDNA. A unique member of the gelsolin/villin family expressed primarily in macrophages. J. Biol. Chem. 267:16545-52
    • (1992) J. Biol. Chem. , vol.267 , pp. 16545-16552
    • Dabiri, G.A.1    Young, C.L.2    Rosenbloom, J.3    Southwick, F.S.4
  • 21
    • 0025973225 scopus 로고
    • Lack of correlation between changes in polyphosphoinositide levels and actin/gelsolin complexes in A431 cells treated with epidermal growth factor
    • Dadahay CY, Patton E, Cooper JA, Pike LJ. 1991. Lack of correlation between changes in polyphosphoinositide levels and actin/gelsolin complexes in A431 cells treated with epidermal growth factor. J. Cell Biol. 112:1151-56
    • (1991) J. Cell Biol. , vol.112 , pp. 1151-1156
    • Dadahay, C.Y.1    Patton, E.2    Cooper, J.A.3    Pike, L.J.4
  • 22
    • 67649877947 scopus 로고
    • 'Phosphatidopeptide'-like complexes formed by the interaction of calcium triphosphoinositide with protein
    • Dawson RMC. 1965. 'Phosphatidopeptide'-like complexes formed by the interaction of calcium triphosphoinositide with protein. Biochem. J. 97:134-38
    • (1965) Biochem. J. , vol.97 , pp. 134-138
    • Dawson, R.M.C.1
  • 23
    • 0013800440 scopus 로고
    • Diphosphoinositide and triphosphoinositide in animal tissues. Extraction, estimation and changes post mortem
    • Dawson RMC, Eichberg J. 1965. Diphosphoinositide and triphosphoinositide in animal tissues. Extraction, estimation and changes post mortem. Biochem. J. 96:634-43
    • (1965) Biochem. J. , vol.96 , pp. 634-643
    • Dawson, R.M.C.1    Eichberg, J.2
  • 24
    • 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, Watson S, Lin C-S, Leavitt J, 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: 1069-79
    • (1990) J. Cell Biol. , vol.111 , pp. 1069-1079
    • De Arruda, M.1    Watson, S.2    Lin, C.-S.3    Leavitt, J.4    Matsudaira, P.5
  • 25
    • 0023727414 scopus 로고
    • 2+ -dependent effects of caldesmon-tropomyosin-calmodulin and troponin-tropomyosin complexes on the structure of F-actin in ghost fibers and its interaction with myosin heads
    • 2+ -dependent effects of caldesmon-tropomyosin-calmodulin and troponin-tropomyosin complexes on the structure of F-actin in ghost fibers and its interaction with myosin heads. Biochim. Biophys. Acta 956:140-50
    • (1988) Biochim. Biophys. Acta , vol.956 , pp. 140-150
    • Dobrowolski, Z.1    Borovikov, Y.S.2    Nowak, E.3    Galazkiewicz, B.4    Dabrowska, R.5
  • 26
    • 0026795843 scopus 로고
    • Interaction of gelsolin with covalently cross-linked actin dimer
    • Doi Y. 1992. Interaction of gelsolin with covalently cross-linked actin dimer. Biochemistry 31:10061-69
    • (1992) Biochemistry , vol.31 , pp. 10061-10069
    • Doi, Y.1
  • 27
    • 0025733241 scopus 로고
    • Modification of gelsolin with 4-fluoro-7-nitrobenz-2-oxa-1.3-diazole
    • Doi Y, Hashimoto T, Yamaguchi H, Vertut DA. 1991. Modification of gelsolin with 4-fluoro-7-nitrobenz-2-oxa-1.3-diazole. Eur. J. Biochem. 199: 277-83
    • (1991) Eur. J. Biochem. , vol.199 , pp. 277-283
    • Doi, Y.1    Hashimoto, T.2    Yamaguchi, H.3    Vertut, D.A.4
  • 28
    • 0025314493 scopus 로고
    • Actin assembly in electropermeabilized neutrophils: Role of intracellular calcium
    • Downey GP, Chan CK, Trudel S, Grinstein S. 1990. Actin assembly in electropermeabilized neutrophils: role of intracellular calcium. J. Cell Biol. 110:1975-82
    • (1990) J. Cell Biol. , vol.110 , pp. 1975-1982
    • Downey, G.P.1    Chan, C.K.2    Trudel, S.3    Grinstein, S.4
  • 29
    • 0023818448 scopus 로고
    • Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
    • Drust DS, Creutz CE. 1988. Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature 331:88-91
    • (1988) Nature , vol.331 , pp. 88-91
    • Drust, D.S.1    Creutz, C.E.2
  • 30
    • 0026078290 scopus 로고
    • Domain structure in actin-binding proteins: Expression and functional characterization of truncated severin
    • Eichinger L, Noegel AA, Schleicher M. 1991. Domain structure in actin-binding proteins: expression and functional characterization of truncated severin. J. Cell Biol. 112:665-76
    • (1991) J. Cell Biol. , vol.112 , pp. 665-676
    • Eichinger, L.1    Noegel, A.A.2    Schleicher, M.3
  • 31
    • 0026638337 scopus 로고
    • Characterization of actin- And lipid-binding domains in severin. a Ca(2+)-dependent F-actin fragmenting protein
    • Eichinger L, Schleicher M. 1992. Characterization of actin- and lipid-binding domains in severin. a Ca(2+)-dependent F-actin fragmenting protein. Biochemistry 31:4779-87
    • (1992) Biochemistry , vol.31 , pp. 4779-4787
    • Eichinger, L.1    Schleicher, M.2
  • 32
    • 0023785596 scopus 로고
    • Cellular mechanics as an indicator of cytoskeletal structure and Junction
    • Elson E. 1988. Cellular mechanics as an indicator of cytoskeletal structure and Junction. Annu. Rev. Biophys. Biochem. 17:397-430
    • (1988) Annu. Rev. Biophys. Biochem. , vol.17 , pp. 397-430
    • Elson, E.1
  • 33
    • 0026642525 scopus 로고
    • Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: A novel calmodulin-binding myosin
    • Espindola FS, Espreafico EM, Coelho MV, Martins AR, Costa FR, et al. 1992. Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin. J. Cell Biol. 118:359-68
    • (1992) J. Cell Biol. , vol.118 , pp. 359-368
    • Espindola, F.S.1    Espreafico, E.M.2    Coelho, M.V.3    Martins, A.R.4    Costa, F.R.5
  • 34
    • 0027397491 scopus 로고
    • A 27,000-D core of the Dictyostelium 34,000-D protein retains Ca(2+)-regulated actin cross-linking but lacks bundling activity
    • Fechheimer M, Furukawa R. 1993. A 27,000-D core of the Dictyostelium 34,000-D protein retains Ca(2+)-regulated actin cross-linking but lacks bundling activity. J. Cell Biol. 120: 1169-76
    • (1993) J. Cell Biol. , vol.120 , pp. 1169-1176
    • Fechheimer, M.1    Furukawa, R.2
  • 36
    • 0024095187 scopus 로고
    • Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone
    • Forscher P, Smith SJ, 1988. Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol. 107:1505-16
    • (1988) J. Cell Biol. , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 37
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function
    • Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, et al. 1992. Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function. Nature 359:150-52
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5
  • 38
    • 0024956931 scopus 로고
    • Myosin I is located at the leading edges of locomoting Dictyostelium amoebae
    • Fukui Y, Lynch TJ, Brzeska H, Korn ED. 1989. Myosin I is located at the leading edges of locomoting Dictyostelium amoebae. Nature 341:328-31
    • (1989) Nature , vol.341 , pp. 328-331
    • Fukui, Y.1    Lynch, T.J.2    Brzeska, H.3    Korn, E.D.4
  • 39
    • 0026521583 scopus 로고
    • Actin kinase: A protein kinase that phosphorylates actin of fragmin-actin complex
    • Furuhashi K, Hatano S. 1992. Actin kinase: a protein kinase that phosphorylates actin of fragmin-actin complex. J. Biochem. 111:366-70
    • (1992) J. Biochem. , vol.111 , pp. 366-370
    • Furuhashi, K.1    Hatano, S.2
  • 41
    • 0026683647 scopus 로고
    • Inositol phospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin
    • Furuhashi K, Inagaki M, Hatano S, Fukami K, Takenawa T. 1992. Inositol phospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin. Biochem. Biophys. Res. Commun. 184:1261-65
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1261-1265
    • Furuhashi, K.1    Inagaki, M.2    Hatano, S.3    Fukami, K.4    Takenawa, T.5
  • 42
    • 0026543510 scopus 로고
    • ASP-56, a new actin sequestering protein from pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast
    • Gieselmann R, Mann K, 1992. ASP-56, a new actin sequestering protein from pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast. FEBS Lett. 298: 149-53
    • (1992) FEBS Lett. , vol.298 , pp. 149-153
    • Gieselmann, R.1    Mann, K.2
  • 43
    • 0019569461 scopus 로고
    • Calcium control of microfilaments: Uncoupling of the F-actin severing and -bundling activity of villin by limited proteolysis in vitro
    • Glenney JR, Weber K. 1981. Calcium control of microfilaments: uncoupling of the F-actin severing and -bundling activity of villin by limited proteolysis in vitro. Proc. Natl. Acad. Sci. USA 78:2810-14
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2810-2814
    • Glenney, J.R.1    Weber, K.2
  • 46
    • 0025239385 scopus 로고
    • Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin
    • Harris AS, Morrow JS. 1990. Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin. Proc. Natl. Acad. Sci. USA 87:3009-13
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3009-3013
    • Harris, A.S.1    Morrow, J.S.2
  • 47
    • 0026784141 scopus 로고
    • Mechanisms of actin rearrangements mediating platelet activation
    • Hartwig JH. 1992. Mechanisms of actin rearrangements mediating platelet activation. J. Cell Biol. 118:1421-42
    • (1992) J. Cell Biol. , vol.118 , pp. 1421-1442
    • Hartwig, J.H.1
  • 48
    • 0026513601 scopus 로고
    • MARCKS is an actin filament cross-linking protein regulated by protein kinase C and calcium-calmodulin
    • Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, et al. 1992. MARCKS is an actin filament cross-linking protein regulated by protein kinase C and calcium-calmodulin. Nature 356:618-22
    • (1992) Nature , vol.356 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5
  • 49
    • 0019165091 scopus 로고
    • Fragmin: A calcium ion sensitive regulatory factor on the formation of actin filaments
    • Hasegawa T, Takahashi S, Hayashi H, Hatano S. 1980. Fragmin: a calcium ion sensitive regulatory factor on the formation of actin filaments. Biochemistry 19:2677-83
    • (1980) Biochemistry , vol.19 , pp. 2677-2683
    • Hasegawa, T.1    Takahashi, S.2    Hayashi, H.3    Hatano, S.4
  • 51
    • 0025365190 scopus 로고
    • Binding of brush border myosin I to phospholipid vesicles
    • Hayden SM, Wolenski JS, Mooseker MS. 1990. Binding of brush border myosin I to phospholipid vesicles. J. Cell Biol. 111:443-51
    • (1990) J. Cell Biol. , vol.111 , pp. 443-451
    • Hayden, S.M.1    Wolenski, J.S.2    Mooseker, M.S.3
  • 53
    • 0026011235 scopus 로고
    • Human platelet P-235, a talin-like actin binding protein, binds selectively to mixed lipid bilayers
    • Heise H, Bayerl T, Isenberg G, Sackmann E. 1991. Human platelet P-235, a talin-like actin binding protein, binds selectively to mixed lipid bilayers. Biochim. Biophys. Acta 106 1:121-31
    • (1991) Biochim. Biophys. Acta , vol.106 , Issue.1 , pp. 121-131
    • Heise, H.1    Bayerl, T.2    Isenberg, G.3    Sackmann, E.4
  • 54
    • 0025748580 scopus 로고
    • Regulation of CapZ, an actin capping protein of chicken muscle, by anionic phospholipids
    • Heiss SG, Cooper JA. 1991. Regulation of CapZ, an actin capping protein of chicken muscle, by anionic phospholipids. Biochemistry 30:8753-58
    • (1991) Biochemistry , vol.30 , pp. 8753-8758
    • Heiss, S.G.1    Cooper, J.A.2
  • 55
    • 0022483306 scopus 로고
    • Isolation of a domain of villin retaining calcium-dependent interaction with F-actin, but devoid of F-actin fragmenting activity
    • Hesterberg LK, Weber K. 1986. Isolation of a domain of villin retaining calcium-dependent interaction with F-actin, but devoid of F-actin fragmenting activity. Eur. J. Biochem. 154: 135-40
    • (1986) Eur. J. Biochem. , vol.154 , pp. 135-140
    • Hesterberg, L.K.1    Weber, K.2
  • 56
    • 0026783523 scopus 로고
    • Cap100, a novel phosphatidylinositol 4,5-bisphosphate-regulated protein that caps actin filaments but does not nucleate actin assembly
    • Hofmann A, Eichinger L, Andre E, Rieger D, Schleicher M. 1992. Cap100, a novel phosphatidylinositol 4,5-bisphosphate-regulated protein that caps actin filaments but does not nucleate actin assembly. Cell Motil. Cytoskeleton 23:133-44
    • (1992) Cell Motil. Cytoskeleton , vol.23 , pp. 133-144
    • Hofmann, A.1    Eichinger, L.2    Andre, E.3    Rieger, D.4    Schleicher, M.5
  • 57
    • 0026708526 scopus 로고
    • Ca(2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: Identification as a homologue for annexin VI and intracellular localization
    • Hosoya H, Kobayashi R, Tsukita S, Matsumura F. 1992. Ca(2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: identification as a homologue for annexin VI and intracellular localization. Cell Motil. Cytoskeleton 22:200-10
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 200-210
    • Hosoya, H.1    Kobayashi, R.2    Tsukita, S.3    Matsumura, F.4
  • 58
    • 0025215463 scopus 로고
    • Calcium-dependent regulation of actin filament bundling by lipocortin-85
    • Ikebuchi NW, Waisman DM, 1990. Calcium-dependent regulation of actin filament bundling by lipocortin-85. J. Biol. Chem. 265:3392-400
    • (1990) J. Biol. Chem. , vol.265 , pp. 3392-3400
    • Ikebuchi, N.W.1    Waisman, D.M.2
  • 59
    • 0025728518 scopus 로고
    • Actin-binding protein - Lipid interactions
    • Isenberg G. 1991. Actin-binding protein - lipid interactions. Cell Motil. Cytoskeleton 12:136-44
    • (1991) Cell Motil. Cytoskeleton , vol.12 , pp. 136-144
    • Isenberg, G.1
  • 61
    • 0026748742 scopus 로고
    • Thrombin receptor activation causes rapid neural cell rounding and neurite retraction independent of classic second messengers
    • Jalink K, Moolenaar WH. 1992. Thrombin receptor activation causes rapid neural cell rounding and neurite retraction independent of classic second messengers. J. Cell Biol. 118:411-19
    • (1992) J. Cell Biol. , vol.118 , pp. 411-419
    • Jalink, K.1    Moolenaar, W.H.2
  • 62
    • 0021801388 scopus 로고
    • Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking
    • Janmey PA, Chaponnier C, Lind SE, Zaner KS, Stossel TP, et al. 1985. Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking. Biochemistry 24:3714-23
    • (1985) Biochemistry , vol.24 , pp. 3714-3723
    • Janmey, P.A.1    Chaponnier, C.2    Lind, S.E.3    Zaner, K.S.4    Stossel, T.P.5
  • 63
    • 0023199043 scopus 로고
    • Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin
    • Janmey PA, Iida K, Yin HL, Stossel TP. 1987. Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin. J. Biol. Chem. 262:12228-36
    • (1987) J. Biol. Chem. , vol.262 , pp. 12228-12236
    • Janmey, P.A.1    Iida, K.2    Yin, H.L.3    Stossel, T.P.4
  • 64
    • 0026724890 scopus 로고
    • Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin
    • Janmey PA, Lamb J, Allen PG, Matsudaira PT. 1992. Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin. J. Biol. Chem. 267:11818-23
    • (1992) J. Biol. Chem. , vol.267 , pp. 11818-11823
    • Janmey, P.A.1    Lamb, J.2    Allen, P.G.3    Matsudaira, P.T.4
  • 66
    • 0024567044 scopus 로고
    • Gelsolin-polyphosphoinositide interaction. Full expression of gelsolin-inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation, or masking of the inositol head group
    • Janmey PA, Stossel TP. 1989. Gelsolin-polyphosphoinositide interaction. Full expression of gelsolin-inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation, or masking of the inositol head group. J. Biol. Chem. 264:4825-31
    • (1989) J. Biol. Chem. , vol.264 , pp. 4825-4831
    • Janmey, P.A.1    Stossel, T.P.2
  • 67
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey PA, Stossel TP. 1987. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 325:362-64
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 68
    • 0026681043 scopus 로고
    • Actin-binding proteins regulate the work performed by myosin II motors on single actin filaments
    • Janson LW, Sellers JR, Taylor DL. 1992. Actin-binding proteins regulate the work performed by myosin II motors on single actin filaments. Cell Motil. Cytoskeleton 22:274-80
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 274-280
    • Janson, L.W.1    Sellers, J.R.2    Taylor, D.L.3
  • 69
    • 0026623535 scopus 로고
    • A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling
    • Jones PG, Moore GJ, Waisman DM. 1992. A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling. J. Biol. Chem. 267:13993-97
    • (1992) J. Biol. Chem. , vol.267 , pp. 13993-13997
    • Jones, P.G.1    Moore, G.J.2    Waisman, D.M.3
  • 72
    • 0022235642 scopus 로고
    • Calmodulin inhibits interaction of actin with MAP2 and tau, two major microtubule-associated proteins
    • Kotani S, Nishida E, Kumagai J, Sakai H. 1985. Calmodulin inhibits interaction of actin with MAP2 and tau, two major microtubule-associated proteins. J. Biol. Chem. 260:10779-83
    • (1985) J. Biol. Chem. , vol.260 , pp. 10779-10783
    • Kotani, S.1    Nishida, E.2    Kumagai, J.3    Sakai, H.4
  • 74
    • 0021275334 scopus 로고
    • Platelet activation induces the formation of a stable gelsolin-actin complex from monomeric gelsolin
    • Kurth MC, Bryan J. 1984. Platelet activation induces the formation of a stable gelsolin-actin complex from monomeric gelsolin. J. Biol. Chem. 259: 7473-79
    • (1984) J. Biol. Chem. , vol.259 , pp. 7473-7479
    • Kurth, M.C.1    Bryan, J.2
  • 75
    • 0024566030 scopus 로고
    • Identification of critical functional and regulatory domains in gelsolin
    • Kwiatkowski DJ, Janmey PA, Yin HL. 1989. Identification of critical functional and regulatory domains in gelsolin. J. Cell Biol. 108:1717-26
    • (1989) J. Cell Biol. , vol.108 , pp. 1717-1726
    • Kwiatkowski, D.J.1    Janmey, P.A.2    Yin, H.L.3
  • 76
    • 0023609425 scopus 로고
    • Molecular biology of gelsolin, a calcium- Regulated actin filament severing protein
    • Kwiatkowski DJ, Yin HL. 1987. Molecular biology of gelsolin, a calcium- regulated actin filament severing protein. Biorheology 24:643-47
    • (1987) Biorheology , vol.24 , pp. 643-647
    • Kwiatkowski, D.J.1    Yin, H.L.2
  • 78
    • 0023854786 scopus 로고
    • Evidence that the phosphatidylinositol cycle is linked to cell motility
    • Lassing I, Lindberg U. 1988. Evidence that the phosphatidylinositol cycle is linked to cell motility. Exp. Cell Res. 174:1-15
    • (1988) Exp. Cell Res. , vol.174 , pp. 1-15
    • Lassing, I.1    Lindberg, U.2
  • 79
    • 0025214940 scopus 로고
    • Polyphosphoinositide synthesis in platelets stimulated with low concentrations of thrombin is enhanced before the activation of phospholipase C
    • Lassing I, Lindberg U. 1990. Polyphosphoinositide synthesis in platelets stimulated with low concentrations of thrombin is enhanced before the activation of phospholipase C. FEBS Lett. 262:231-33
    • (1990) FEBS Lett. , vol.262 , pp. 231-233
    • Lassing, I.1    Lindberg, U.2
  • 80
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin
    • Lassing I, Lindberg U. 1985. Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin. Nature 314:472-74
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 81
    • 0023940928 scopus 로고
    • Specificity of the interaction between phosphatidylinositol 4,5-bisphosphate and the profilin:actin complex
    • Lassing I, Lindberg U. 1988. Specificity of the interaction between phosphatidylinositol 4,5-bisphosphate and the profilin:actin complex. J. Cell. Biochem. 37:255-67
    • (1988) J. Cell. Biochem. , vol.37 , pp. 255-267
    • Lassing, I.1    Lindberg, U.2
  • 82
    • 0023689934 scopus 로고
    • Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts
    • Lin C-S, Aebersold R, Kent S, Varma M, Leavitt J. 1988. Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts. Mol. Cell. Biol. 8:4659-68
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4659-4668
    • Lin, C.-S.1    Aebersold, R.2    Kent, S.3    Varma, M.4    Leavitt, J.5
  • 83
    • 0026638325 scopus 로고
    • A novel regulatory protein that affects the functions of caldesmon and myosin light chain kinase
    • Lin Y, Ishikawa R, Kohama K. 1992. A novel regulatory protein that affects the functions of caldesmon and myosin light chain kinase. Biochem. Biophys. Res. Commun. 184:1212-18
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1212-1218
    • Lin, Y.1    Ishikawa, R.2    Kohama, K.3
  • 84
    • 0023583703 scopus 로고
    • Reversible binding of actin to gelsolin and profilin in human platelet extracts
    • Lind SE, Janmey PA, Chaponnier C, Herbert T, Stossel TP. 1987. Reversible binding of actin to gelsolin and profilin in human platelet extracts. J. Cell Biol. 105:833-42
    • (1987) J. Cell Biol. , vol.105 , pp. 833-842
    • Lind, S.E.1    Janmey, P.A.2    Chaponnier, C.3    Herbert, T.4    Stossel, T.P.5
  • 85
    • 0021041789 scopus 로고
    • An actin-depolymerizing protein (depactin) from starfish oocytes: Properties and interaction with actin
    • Mabuchi I. 1983. An actin-depolymerizing protein (depactin) from starfish oocytes: properties and interaction with actin. J. Cell Biol. 97:1612-21
    • (1983) J. Cell Biol. , vol.97 , pp. 1612-1621
    • Mabuchi, I.1
  • 86
    • 0025517560 scopus 로고
    • The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C
    • Machesky LM, Goldschmidt-Clermont PJ, Pollard TD. 1990. The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C. Cell Reg. 1:937-50
    • (1990) Cell Reg. , vol.1 , pp. 937-950
    • Machesky, L.M.1    Goldschmidt-Clermont, P.J.2    Pollard, T.D.3
  • 87
    • 0025337187 scopus 로고
    • Inhibition of actin regulatory activity of the 74-kDa protein from bovine adrenal medulla (Adseverin) by some phospholipids
    • Maekawa S, Sakai H. 1990. Inhibition of actin regulatory activity of the 74-kDa protein from bovine adrenal medulla (Adseverin) by some phospholipids. J. Biol. Chem. 265:10940-42
    • (1990) J. Biol. Chem. , vol.265 , pp. 10940-10942
    • Maekawa, S.1    Sakai, H.2
  • 89
    • 0026472151 scopus 로고
    • Calcium-dependent regulation of caldesmon by an 11-kDa smooth muscle calcium-binding protein, caltropin
    • Mani RS, McCubbin WD, Kay CM. 1992. Calcium-dependent regulation of caldesmon by an 11-kDa smooth muscle calcium-binding protein, caltropin. Biochemistry 31:11896-901
    • (1992) Biochemistry , vol.31 , pp. 11896-11901
    • Mani, R.S.1    McCubbin, W.D.2    Kay, C.M.3
  • 90
    • 0025931128 scopus 로고
    • Calcium-induced degradation of the lens cytoskeleton
    • Marcantonio JM, Duncan G. 1991. Calcium-induced degradation of the lens cytoskeleton. Biochem. Soc. Trans. 19:1148-50
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 1148-1150
    • Marcantonio, J.M.1    Duncan, G.2
  • 91
    • 0019364580 scopus 로고
    • Characterization of platelet extracts before and after stimulation with respect to the possible role of profilactin as microfilament precursor
    • Markey F, Persson T, Lindberg U. 1981. Characterization of platelet extracts before and after stimulation with respect to the possible role of profilactin as microfilament precursor. Cell 23: 145-53
    • (1981) Cell , vol.23 , pp. 145-153
    • Markey, F.1    Persson, T.2    Lindberg, U.3
  • 92
    • 0025122019 scopus 로고
    • Transient increases in cytosolic free calcium appear to be required for the migration of adherent human neutrophils
    • Marks P, Maxfield F. 1990. Transient increases in cytosolic free calcium appear to be required for the migration of adherent human neutrophils. J. Cell Biol. 110:43-52
    • (1990) J. Cell Biol. , vol.110 , pp. 43-52
    • Marks, P.1    Maxfield, F.2
  • 95
    • 0026349379 scopus 로고
    • Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons
    • Mattson MP, Engle MG, Rychlik B. 1991. Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons. Mol. Chem. Neuropathol. 15:117-42
    • (1991) Mol. Chem. Neuropathol. , vol.15 , pp. 117-142
    • Mattson, M.P.1    Engle, M.G.2    Rychlik, B.3
  • 96
    • 0025339009 scopus 로고
    • Bundling of actin filaments by α-actinin depends on its molecular length
    • Meyer R, Aebi U. 1990. Bundling of actin filaments by α-actinin depends on its molecular length. J. Cell Biol. 110:2013-24
    • (1990) J. Cell Biol. , vol.110 , pp. 2013-2024
    • Meyer, R.1    Aebi, U.2
  • 97
    • 0027229126 scopus 로고
    • Changes in mobility of chromaffin granules in actin network with its assembly and Ca(2+)-dependent disassembly by gelsolin
    • 96a. Miyamoto S, Funatsu T, Ishiwata S, Fujime S. 1993. Changes in mobility of chromaffin granules in actin network with its assembly and Ca(2+)-dependent disassembly by gelsolin. Biophys. J. 64:1139-49
    • (1993) Biophys. J. , vol.64 , pp. 1139-1149
    • Miyamoto, S.1    Funatsu, T.2    Ishiwata, S.3    Fujime, S.4
  • 98
    • 0024312342 scopus 로고
    • The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme
    • Mooseker MS, Coleman TR. 1989. The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme. J. Cell Biol. 108:2395-400
    • (1989) J. Cell Biol. , vol.108 , pp. 2395-2400
    • Mooseker, M.S.1    Coleman, T.R.2
  • 99
    • 0026726153 scopus 로고
    • Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin
    • Moriyama K, Yonezawa N, Sakai H, Yahara I, Nishida E. 1992. Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin. J. Biol. Chem. 267:7240-44
    • (1992) J. Biol. Chem. , vol.267 , pp. 7240-7244
    • Moriyama, K.1    Yonezawa, N.2    Sakai, H.3    Yahara, I.4    Nishida, E.5
  • 100
    • 0026468443 scopus 로고
    • Human T cell L-plastin bundles actin filaments in a calcium-dependent manner
    • Namba Y, Ito M, Zu Y, Shigesada K, Maruyama K. 1992. Human T cell L-plastin bundles actin filaments in a calcium-dependent manner. J. Biochem. 112:503-7
    • (1992) J. Biochem. , vol.112 , pp. 503-507
    • Namba, Y.1    Ito, M.2    Zu, Y.3    Shigesada, K.4    Maruyama, K.5
  • 101
    • 0027921664 scopus 로고
    • Lipid-cytoskeleton interactions
    • Niggli V. 1993. Lipid-cytoskeleton interactions. Nature 361:214
    • (1993) Nature , vol.361 , pp. 214
    • Niggli, V.1
  • 102
    • 0023653358 scopus 로고
    • Calcium-sensitive nonmuscle α-actinin contains EF-hand structures and highly conserved regions
    • Noegel A, Witke W, Schleicher M. 1987. Calcium-sensitive nonmuscle α-actinin contains EF-hand structures and highly conserved regions. FEBS Lett. 221:391-96
    • (1987) FEBS Lett. , vol.221 , pp. 391-396
    • Noegel, A.1    Witke, W.2    Schleicher, M.3
  • 105
    • 0023762042 scopus 로고
    • Biophysics of the leading lamella
    • Oster G. 1988. Biophysics of the leading lamella. Cell Motil. Cytoskeleton 10:164-71
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 164-171
    • Oster, G.1
  • 106
    • 0027390673 scopus 로고
    • Macrophage alpha-actinin is not a calcium-modulated actin-binding protein
    • Pacaud M, Harricane MC. 1993. Macrophage alpha-actinin is not a calcium-modulated actin-binding protein. Biochemistry 32:363-74
    • (1993) Biochemistry , vol.32 , pp. 363-374
    • Pacaud, M.1    Harricane, M.C.2
  • 107
    • 0025734407 scopus 로고
    • Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin
    • Pavalko FM, Burridge K. 1991. Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin. J. Cell Biol. 114:481-91
    • (1991) J. Cell Biol. , vol.114 , pp. 481-491
    • Pavalko, F.M.1    Burridge, K.2
  • 108
    • 0025990831 scopus 로고
    • Phosphoinositide kinase, diacylglycerol kinase, and phospholipase C activities associated to the cytoskeleton: Effect of epidermal growth factor
    • Payrastre B, van Bergen en Henegouwen PM, Breton M, Denhartigh JC, Plantavid M, et al. 1991. Phosphoinositide kinase, diacylglycerol kinase, and phospholipase C activities associated to the cytoskeleton: effect of epidermal growth factor. J. Cell Biol. 115:121-28
    • (1991) J. Cell Biol. , vol.115 , pp. 121-128
    • Payrastre, B.1    Van Bergen En Henegouwen, P.M.2    Breton, M.3    Denhartigh, J.C.4    Plantavid, M.5
  • 109
    • 0025988319 scopus 로고
    • Stimulation of human polymorphonuclear leukocyte phosphatidylinositol-4-phosphate kinase by concanavalin A and formyl-methionylleucyl-phenylalanine is calcium-independent. Correlation with maintenance of actin assembly
    • Pike MC, Costello K, Southwick FS. 1991. Stimulation of human polymorphonuclear leukocyte phosphatidylinositol-4-phosphate kinase by concanavalin A and formyl-methionylleucyl-phenylalanine is calcium-independent. Correlation with maintenance of actin assembly. J. Immunol. 147: 2270-75
    • (1991) J. Immunol. , vol.147 , pp. 2270-2275
    • Pike, M.C.1    Costello, K.2    Southwick, F.S.3
  • 111
    • 0026079365 scopus 로고
    • Mbh 1: A novel gelsolin/severin-related protein which binds actin in vitro and exhibits nuclear localization in vivo
    • Prendergast GC, Ziff EB. 1991. Mbh 1: a novel gelsolin/severin-related protein which binds actin in vitro and exhibits nuclear localization in vivo. EMBO J. 10:757-66
    • (1991) EMBO J. , vol.10 , pp. 757-766
    • Prendergast, G.C.1    Ziff, E.B.2
  • 112
    • 0027328221 scopus 로고
    • The Ca(2+)-sensitizing component of smooth muscle thin filaments: Properties of regulatory factors that interact with caldesmon
    • Pritchard K, Marston SB. 1993. The Ca(2+)-sensitizing component of smooth muscle thin filaments: properties of regulatory factors that interact with caldesmon. Biochem. Biophys. Res. Commun. 190:668-73
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 668-673
    • Pritchard, K.1    Marston, S.B.2
  • 113
    • 0022343675 scopus 로고
    • Mass changes in myoinositol trisphosphate in human platelets stimulated by thrombin
    • Rittenhouse S, Sasson J. 1985. Mass changes in myoinositol trisphosphate in human platelets stimulated by thrombin. J. Biol. Chem. 260:8657-60
    • (1985) J. Biol. Chem. , vol.260 , pp. 8657-8660
    • Rittenhouse, S.1    Sasson, J.2
  • 115
    • 0026634115 scopus 로고
    • The interaction of actin with thymosin beta 4
    • Safer D. 1992. The interaction of actin with thymosin beta 4. J. Muscle Res. Cell. Motil. 13:269-71
    • (1992) J. Muscle Res. Cell. Motil. , vol.13 , pp. 269-271
    • Safer, D.1
  • 116
    • 0025922811 scopus 로고
    • The Ca(2+)-dependent actin filament-severing activity of 74-kDa protein (adseverin) resides in its NH2-terminal half
    • Sakurai T, Kurokawa H, Nonomura Y. 1991. The Ca(2+)-dependent actin filament-severing activity of 74-kDa protein (adseverin) resides in its NH2-terminal half. J. Biol. Chem. 266: 4581-85
    • (1991) J. Biol. Chem. , vol.266 , pp. 4581-4585
    • Sakurai, T.1    Kurokawa, H.2    Nonomura, Y.3
  • 117
    • 0022552120 scopus 로고
    • Is a rise in intracellular concentration of free calcium necessary or sufficient for stimulated cytoskeletal-associated actin
    • Sha'afi R, Shefcyk J, Yassin R, Molski T, Naccache P, et al. 1986. Is a rise in intracellular concentration of free calcium necessary or sufficient for stimulated cytoskeletal-associated actin. J. Cell Biol. 102:1459-63
    • (1986) J. Cell Biol. , vol.102 , pp. 1459-1463
    • ShA'Afi, R.1    Shefcyk, J.2    Yassin, R.3    Molski, T.4    Naccache, P.5
  • 118
    • 0025340881 scopus 로고
    • The actin released from profilin-actin complexes insufficient to account for the increase in F-actin in chemoattractant-stimulated polymorphonuclear leukocytes
    • Southwick F, Young C. 1990. The actin released from profilin-actin complexes insufficient to account for the increase in F-actin in chemoattractant-stimulated polymorphonuclear leukocytes. J. Cell Biol. 110:1965-74
    • (1990) J. Cell Biol. , vol.110 , pp. 1965-1974
    • Southwick, F.1    Young, C.2
  • 119
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel T. 1993. On the crawling of animal cells. Science 260:1086-94
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.1
  • 120
    • 0024457508 scopus 로고
    • From signal to pseudopod. How cells control cytoplasmic actin assembly
    • Stossel TP. 1989. From signal to pseudopod. How cells control cytoplasmic actin assembly. J. Biol. Chem. 264:18261-64
    • (1989) J. Biol. Chem. , vol.264 , pp. 18261-18264
    • Stossel, T.P.1
  • 121
    • 0042930607 scopus 로고
    • The cortical cytoplasmic actin gel
    • ed. J Bereiter-Hahn, OR Anderson, WE Reif, Berlin: Springer
    • Stossel TP, Janmey PA, Zaner KS. 1987. The cortical cytoplasmic actin gel. In Cytomechanics, ed. J Bereiter-Hahn, OR Anderson, WE Reif, pp. 131-53. Berlin: Springer
    • (1987) Cytomechanics , pp. 131-153
    • Stossel, T.P.1    Janmey, P.A.2    Zaner, K.S.3
  • 122
    • 0025924751 scopus 로고
    • Ca(2+)-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4. 1
    • Tanaka T, Kadowaki K, Lazarides E, Sobue K. 1991. Ca(2+)-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4. 1. J. Biol. Chem. 266:1134-40
    • (1991) J. Biol. Chem. , vol.266 , pp. 1134-1140
    • Tanaka, T.1    Kadowaki, K.2    Lazarides, E.3    Sobue, K.4
  • 123
    • 0025989194 scopus 로고
    • Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae
    • Vojtek A, Haarer B, Field J, Gerst J, Pollard TD, et al. 1991. Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae. Cell 66:497-505
    • (1991) Cell , vol.66 , pp. 497-505
    • Vojtek, A.1    Haarer, B.2    Field, J.3    Gerst, J.4    Pollard, T.D.5
  • 124
    • 0021701201 scopus 로고
    • Calcium dependence of villin-induced actin depolymerization
    • Walsh T, Weber A, Davis K, Bonder E, Mooseker M. 1984. Calcium dependence of villin-induced actin depolymerization. Biochemistry 23: 6099-102
    • (1984) Biochemistry , vol.23 , pp. 6099-6102
    • Walsh, T.1    Weber, A.2    Davis, K.3    Bonder, E.4    Mooseker, M.5
  • 125
    • 0025734593 scopus 로고
    • Localization of the calmodulin- And the actin-binding sites of caldesmon
    • Wang CL, Wang LW, Xu SA, Lu RC, Saavedra AV, et al. 1991. Localization of the calmodulin- and the actin-binding sites of caldesmon. J. Biol. Chem. 266:9166-72
    • (1991) J. Biol. Chem. , vol.266 , pp. 9166-9172
    • Wang, C.L.1    Wang, L.W.2    Xu, S.A.3    Lu, R.C.4    Saavedra, A.V.5
  • 126
    • 0024318706 scopus 로고
    • Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis
    • Way M, Gooch J, Pope B, Weeds AG. 1989. Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J. Cell Biol. 109:593-605
    • (1989) J. Cell Biol. , vol.109 , pp. 593-605
    • Way, M.1    Gooch, J.2    Pope, B.3    Weeds, A.G.4
  • 128
    • 0027315149 scopus 로고
    • The Ca(2+)-binding domains in non-muscle type alpha-actinin: Biochemical and genetic analysis
    • 125b. Witke W, Hofmann A, Koppel B, Schleicher M, Noegel AA. 1993. The Ca(2+)-binding domains in non-muscle type alpha-actinin: biochemical and genetic analysis. J. Cell Biol. 121:599-606
    • (1993) J. Cell Biol. , vol.121 , pp. 599-606
    • Witke, W.1    Hofmann, A.2    Koppel, B.3    Schleicher, M.4    Noegel, A.A.5
  • 129
    • 0026593102 scopus 로고
    • Redundancy in the microfilament system: Abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins
    • Witke W, Schleicher M, Noegel AA. 1992. Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins. Cell 68:53-62
    • (1992) Cell , vol.68 , pp. 53-62
    • Witke, W.1    Schleicher, M.2    Noegel, A.A.3
  • 132
    • 0026078926 scopus 로고
    • Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis
    • Yamashiro S, Yamakita Y, Hosoya H, Matsumura F. 1991. Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis. Nature 349:169-72
    • (1991) Nature , vol.349 , pp. 169-172
    • Yamashiro, S.1    Yamakita, Y.2    Hosoya, H.3    Matsumura, F.4
  • 133
    • 0027321473 scopus 로고
    • Microtubule-associated protein interactions with actin filaments: Evidence for differential behavior of neuronal MAP-2 and tau in the presence of phosphatidylinositol
    • Yamauchi PS, Purich DL. 1993. Microtubule-associated protein interactions with actin filaments: evidence for differential behavior of neuronal MAP-2 and tau in the presence of phosphatidylinositol. Biochem. Biophys. Res. Commun. 190:710-15
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 710-715
    • Yamauchi, P.S.1    Purich, D.L.2
  • 134
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • Yin HL, Stossel TP. 1979. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature 281:583-86
    • (1979) Nature , vol.281 , pp. 583-586
    • Yin, H.L.1    Stossel, T.P.2
  • 135
    • 0023424175 scopus 로고
    • Gelsolin. A calcium- And polyphosphoinositide-regulated actin-modulating protein
    • Yin HL. 1987. Gelsolin. A calcium- and polyphosphoinositide-regulated actin-modulating protein. BioEssays 7: 176-79
    • (1987) BioEssays , vol.7 , pp. 176-179
    • Yin, H.L.1
  • 136
    • 0023849688 scopus 로고
    • Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments
    • Yin HL, Iida K, Janmey PA. 1988. Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments. J. Cell Biol. 106:805-12
    • (1988) J. Cell Biol. , vol.106 , pp. 805-812
    • Yin, H.L.1    Iida, K.2    Janmey, P.A.3
  • 138
    • 0026044059 scopus 로고
    • A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin
    • Yonezawa N, Homma Y, Yahara I, Sakai H, Nishida E. 1991. A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J. Biol. Chem. 266:17218-21
    • (1991) J. Biol. Chem. , vol.266 , pp. 17218-17221
    • Yonezawa, N.1    Homma, Y.2    Yahara, I.3    Sakai, H.4    Nishida, E.5
  • 139
    • 0025277362 scopus 로고
    • Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides
    • Yonezawa N, Nishida E, Iida K, Yahara I, Sakai H. 1990. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J. Biol. Chem. 265: 8382-86
    • (1990) J. Biol. Chem. , vol.265 , pp. 8382-8386
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5
  • 140
    • 0025651999 scopus 로고
    • GCap39, a calcium ion- And polyphosphoinositide-regulated actin capping protein
    • Yu FX, Johnston PA, Sudhof TC, Yin HL. 1990. gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein. Science 250:1413-15
    • (1990) Science , vol.250 , pp. 1413-1415
    • Yu, F.X.1    Johnston, P.A.2    Sudhof, T.C.3    Yin, H.L.4
  • 141
    • 0026752622 scopus 로고
    • Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin
    • Yu FX, Sun HQ, Janmey PA, Yin HL. 1992. Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J. Biol. Chem. 267:14616-21
    • (1992) J. Biol. Chem. , vol.267 , pp. 14616-14621
    • Yu, F.X.1    Sun, H.Q.2    Janmey, P.A.3    Yin, H.L.4
  • 142
    • 0026774568 scopus 로고
    • Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed platelets
    • Zhang J, Fry MJ, Waterfield MD, Jaken S, Liao L, et al. 1992. Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed platelets. J. Biol. Chem. 267: 4686-92
    • (1992) J. Biol. Chem. , vol.267 , pp. 4686-4692
    • Zhang, J.1    Fry, M.J.2    Waterfield, M.D.3    Jaken, S.4    Liao, L.5
  • 143
    • 0025046583 scopus 로고
    • 65-kilodalton protein phosphorylated by interleukin 2 stimulation bears two putative actin-binding sites and two calcium-binding sites
    • Zu YL, Shigesada K, Nishida E, Kubota I, Kohno M, et al. 1990. 65-kilodalton protein phosphorylated by interleukin 2 stimulation bears two putative actin-binding sites and two calcium-binding sites. Biochemistry 29: 8319-24
    • (1990) Biochemistry , vol.29 , pp. 8319-8324
    • Zu, Y.L.1    Shigesada, K.2    Nishida, E.3    Kubota, I.4    Kohno, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.