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Volumn 287, Issue 2, 1999, Pages 293-300

Morphogenesis of liposomes encapsulating actin depends on the type of actin-crosslinking

Author keywords

Actin; Actin crosslinking protein; Dark field microscopy; Giant liposome; Membrane morphogenesis

Indexed keywords

ACTIN; ALPHA ACTININ; FILAMIN; G ACTIN; LIPOSOME;

EID: 0033605879     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2592     Document Type: Article
Times cited : (72)

References (46)
  • 1
    • 0017114442 scopus 로고
    • A quantitative description of the extension and retraction of surface protrusions in spreading 3T3 mouse fibroblasts
    • Albrecht-Buehler G., Lancaster R. M. A quantitative description of the extension and retraction of surface protrusions in spreading 3T3 mouse fibroblasts. J. Cell Biol. 71:1976;370-382.
    • (1976) J. Cell Biol. , vol.71 , pp. 370-382
    • Albrecht-Buehler, G.1    Lancaster, R.M.2
  • 2
    • 0029444559 scopus 로고
    • Surrogate cells or Trojan horses. The discovery of liposomes
    • Bangham A. D. Surrogate cells or Trojan horses. The discovery of liposomes. BioEssays. 17:1995;1081-1088.
    • (1995) BioEssays , vol.17 , pp. 1081-1088
    • Bangham, A.D.1
  • 5
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher A. Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol. 7:1991;337-374.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 6
    • 0020290629 scopus 로고
    • Stress fibers in cells in situ: Immunofluorescence visualization with antiactin, antimyosin, and anti-α-actinin
    • Byers H. R., Fujikawa K. Stress fibers in cells in situ: immunofluorescence visualization with antiactin, antimyosin, and anti-α-actinin. J. Cell Biol. 93:1982;804-811.
    • (1982) J. Cell Biol. , vol.93 , pp. 804-811
    • Byers, H.R.1    Fujikawa, K.2
  • 7
    • 0028269631 scopus 로고
    • Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension
    • Cant K., Knowles B. A., Mooseker M. S., Cooley L. Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. J. Cell Biol. 125:1994;369-380.
    • (1994) J. Cell Biol. , vol.125 , pp. 369-380
    • Cant, K.1    Knowles, B.A.2    Mooseker, M.S.3    Cooley, L.4
  • 8
  • 10
    • 0001621246 scopus 로고
    • A new protein factor promoting contraction of actomyosin
    • Ebashi S., Ebashi F., Maruyama K. A new protein factor promoting contraction of actomyosin. Nature. 203:1964;645-646.
    • (1964) Nature , vol.203 , pp. 645-646
    • Ebashi, S.1    Ebashi, F.2    Maruyama, K.3
  • 11
    • 0028799146 scopus 로고
    • Fascins, a family of actin bundling proteins
    • Edwards R. A., Bryan J. Fascins, a family of actin bundling proteins. Cell Motil. Cytoskel. 32:1995;1-9.
    • (1995) Cell Motil. Cytoskel. , vol.32 , pp. 1-9
    • Edwards, R.A.1    Bryan, J.2
  • 12
    • 0028902746 scopus 로고
    • Cloning and expression of a murine fascin homolog from mouse brain
    • Edwards R. A., Herrera-Sosa H., Otto J., Bryan J. Cloning and expression of a murine fascin homolog from mouse brain. J. Biol. Chem. 270:1995;10764-10770.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10764-10770
    • Edwards, R.A.1    Herrera-Sosa, H.2    Otto, J.3    Bryan, J.4
  • 13
    • 0027437479 scopus 로고
    • Actin conformation is drastically altered by direct interaction with membrane lipids: A differential scanning calorimetry study
    • Gicquaud C. Actin conformation is drastically altered by direct interaction with membrane lipids: a differential scanning calorimetry study. Biochemistry. 32:1993;11873-11877.
    • (1993) Biochemistry , vol.32 , pp. 11873-11877
    • Gicquaud, C.1
  • 14
    • 0028178829 scopus 로고
    • α-Actinin from chicken gizzard: At low temperature, the onset of actin-gelling activity correlates with actin bundling
    • Grazi E., Trombetta G., Magri E., Cuneo P., Schwienbacher C. α-Actinin from chicken gizzard: at low temperature, the onset of actin-gelling activity correlates with actin bundling. Biochem. J. 298:1994;129-133.
    • (1994) Biochem. J. , vol.298 , pp. 129-133
    • Grazi, E.1    Trombetta, G.2    Magri, E.3    Cuneo, P.4    Schwienbacher, C.5
  • 15
    • 0030856099 scopus 로고    scopus 로고
    • Interactions between smooth muscle α-actinin and lipid bilayers
    • Han X., Li G., Li G., Lin K. Interactions between smooth muscle α-actinin and lipid bilayers. Biochemistry. 36:1997;10364-10371.
    • (1997) Biochemistry , vol.36 , pp. 10364-10371
    • Han, X.1    Li, G.2    Li, G.3    Lin, K.4
  • 17
    • 0025053513 scopus 로고
    • Purification of human smooth muscle filamin and characterization of structural domains and functional sites
    • Hock R. S., Davis G., Speicher D. W. Purification of human smooth muscle filamin and characterization of structural domains and functional sites. Biochemistry. 29:1990;9441-9451.
    • (1990) Biochemistry , vol.29 , pp. 9441-9451
    • Hock, R.S.1    Davis, G.2    Speicher, D.W.3
  • 18
    • 0021755796 scopus 로고
    • Transformation pathways of liposomes
    • Hotani H. Transformation pathways of liposomes. J. Mol. Biol. 178:1984;113-120.
    • (1984) J. Mol. Biol. , vol.178 , pp. 113-120
    • Hotani, H.1
  • 19
    • 0025204589 scopus 로고
    • Dynamic features of microtubules as visualized by dark-field microscopy
    • Hotani H., Miyamoto H. Dynamic features of microtubules as visualized by dark-field microscopy. Advan. Biophys. 26:1990;135-156.
    • (1990) Advan. Biophys. , vol.26 , pp. 135-156
    • Hotani, H.1    Miyamoto, H.2
  • 20
    • 0025292782 scopus 로고
    • Brownian motion of inert tracer macromolecules in polymerized and spontaneously bundled mixtures of actin and filamin
    • Hou L., Luby-Phelps K., Lanni F. J. Brownian motion of inert tracer macromolecules in polymerized and spontaneously bundled mixtures of actin and filamin. J. Cell Biol. 110:1990;1645-1654.
    • (1990) J. Cell Biol. , vol.110 , pp. 1645-1654
    • Hou, L.1    Luby-Phelps, K.2    Lanni, F.J.3
  • 21
    • 0024278676 scopus 로고
    • Substructure and higher structure of chicken smooth muscle alpha-actinin molecule
    • Imamura M., Endo T., Kuroda M., Tanaka T., Masaki T. Substructure and higher structure of chicken smooth muscle alpha-actinin molecule. J. Biol. Chem. 263:1988;7800-7805.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7800-7805
    • Imamura, M.1    Endo, T.2    Kuroda, M.3    Tanaka, T.4    Masaki, T.5
  • 22
    • 0016537752 scopus 로고
    • Preparation and purification of polymerized actin from sea urchin egg extracts
    • Kane R. E. Preparation and purification of polymerized actin from sea urchin egg extracts. J. Cell Biol. 66:1975;305-315.
    • (1975) J. Cell Biol. , vol.66 , pp. 305-315
    • Kane, R.E.1
  • 24
    • 0025968124 scopus 로고
    • The conformation of membranes
    • Lipowsky R. The conformation of membranes. Nature. 349:1991;475-481.
    • (1991) Nature , vol.349 , pp. 475-481
    • Lipowsky, R.1
  • 25
    • 0014597040 scopus 로고
    • Some properties of chicken α-actinin
    • Masaki T., Takaiti O. Some properties of chicken α-actinin. J. Biochem. 66:1969;637-643.
    • (1969) J. Biochem. , vol.66 , pp. 637-643
    • Masaki, T.1    Takaiti, O.2
  • 26
    • 0025339009 scopus 로고
    • Bundling of actin filaments by α-actinin depends on its molecular length
    • Meyer R. K., Aebi U. Bundling of actin filaments by α-actinin depends on its molecular length. J. Cell Biol. 110:1990;2013-2024.
    • (1990) J. Cell Biol. , vol.110 , pp. 2013-2024
    • Meyer, R.K.1    Aebi, U.2
  • 27
    • 0023216026 scopus 로고
    • Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and α-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking
    • Mimura N., Asano A. Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and α-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking. J. Biol. Chem. 262:1987;4717-4723.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4717-4723
    • Mimura, N.1    Asano, A.2
  • 28
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison T. J., Cramer L. P. Actin-based cell motility and cell locomotion. Cell. 84:1996;371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 29
    • 0024109183 scopus 로고
    • Cytoskeletal dynamics and nerve growth
    • Mitchison T. J., Kirschner M. Cytoskeletal dynamics and nerve growth. Neuron. 1:1988;761-772.
    • (1988) Neuron , vol.1 , pp. 761-772
    • Mitchison, T.J.1    Kirschner, M.2
  • 30
    • 0026482154 scopus 로고
    • Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles
    • Miyata H., Hotani H. Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles. Proc. Natl Acad. Sci. USA. 89:1992;11547-11551.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11547-11551
    • Miyata, H.1    Hotani, H.2
  • 31
    • 0021111574 scopus 로고
    • Flexural rigidity of singlet microtubules estimated from statistical analysis of their contour length and end-to-end distances
    • Mizushima-Sugano J., Maeda T., Miki-Nomura T. Flexural rigidity of singlet microtubules estimated from statistical analysis of their contour length and end-to-end distances. Biochim. Biophys. Acta. 755:1983;257-262.
    • (1983) Biochim. Biophys. Acta , vol.755 , pp. 257-262
    • Mizushima-Sugano, J.1    Maeda, T.2    Miki-Nomura, T.3
  • 35
    • 0019260574 scopus 로고
    • Redistribution of actin and fascin in sea urchin eggs after fertilization
    • Otto J. J., Kane R. E., Bryan J. Redistribution of actin and fascin in sea urchin eggs after fertilization. Cell Motil. 1:1980;31-40.
    • (1980) Cell Motil. , vol.1 , pp. 31-40
    • Otto, J.J.1    Kane, R.E.2    Bryan, J.3
  • 36
    • 0019888236 scopus 로고
    • Purification of a calcium-sensitive actin gelation protein from Acanthamoeba
    • Pollard T. D. Purification of a calcium-sensitive actin gelation protein from Acanthamoeba. J. Biol. Chem. 256:1981;7666-7670.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7666-7670
    • Pollard, T.D.1
  • 37
    • 0011014320 scopus 로고
    • Actin in dividing cells: Contractile ring filaments bind heavy meromyosin
    • Schroeder T. E. Actin in dividing cells: contractile ring filaments bind heavy meromyosin. Proc. Natl Acad. Sci. USA. 70:1973;1688-1692.
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , pp. 1688-1692
    • Schroeder, T.E.1
  • 38
    • 0025793710 scopus 로고
    • Heavy meromyosin induces sliding movements between antiparallel actin filaments
    • Takiguchi K. Heavy meromyosin induces sliding movements between antiparallel actin filaments. J. Biochem. 109:1991;520-527.
    • (1991) J. Biochem. , vol.109 , pp. 520-527
    • Takiguchi, K.1
  • 39
    • 0018654598 scopus 로고
    • Cytoplasmic structure and contractility in amoeboid cells
    • New York: Academic Press. p. 57-144
    • Taylor D. L., Condeelis J. S. Cytoplasmic structure and contractility in amoeboid cells. Int. Rev. Cytol. 1979;Academic Press, New York. p. 57-144.
    • (1979) Int. Rev. Cytol
    • Taylor, D.L.1    Condeelis, J.S.2
  • 40
    • 0027970371 scopus 로고
    • Insertion of filamin into lipid membranes examined by calorimetry, the film balance technique, and lipid photolabeling
    • Tempel M., Goldmann W. H., Dietrich C., Niggli V., Weber T., Sackmann E., Isenberg G. Insertion of filamin into lipid membranes examined by calorimetry, the film balance technique, and lipid photolabeling. Biochemistry. 33:1994;12565-12572.
    • (1994) Biochemistry , vol.33 , pp. 12565-12572
    • Tempel, M.1    Goldmann, W.H.2    Dietrich, C.3    Niggli, V.4    Weber, T.5    Sackmann, E.6    Isenberg, G.7
  • 41
    • 0027162413 scopus 로고
    • Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels
    • Wachsstock D. H., Schwartz W. H., Pollard T. D. Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels. Biophys. J. 65:1993;205-214.
    • (1993) Biophys. J. , vol.65 , pp. 205-214
    • Wachsstock, D.H.1    Schwartz, W.H.2    Pollard, T.D.3
  • 42
    • 0028265522 scopus 로고
    • Cross-linker dynamics determine the mechanical properties of actin gels
    • Wachsstock D. H., Schwartz W. H., Pollard T. D. Cross-linker dynamics determine the mechanical properties of actin gels. Biophys. J. 66:1994;801-809.
    • (1994) Biophys. J. , vol.66 , pp. 801-809
    • Wachsstock, D.H.1    Schwartz, W.H.2    Pollard, T.D.3
  • 43
    • 0032540368 scopus 로고    scopus 로고
    • Dynamic cross-linking by α-actinin determines the mechanical properties of actin filament networks
    • Xu J., Wirtz D., Pollard T. D. Dynamic cross-linking by α-actinin determines the mechanical properties of actin filament networks. J. Biol. Chem. 273:1998;9570-9576.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9570-9576
    • Xu, J.1    Wirtz, D.2    Pollard, T.D.3
  • 44
    • 15844362435 scopus 로고    scopus 로고
    • Phosphorylation of human fascin inhibits its actin binding and bundling activities
    • Yamakita Y., Ono S., Matsumura F., Yamashiro S. Phosphorylation of human fascin inhibits its actin binding and bundling activities. J. Biol. Chem. 271:1996;12632-12638.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12632-12638
    • Yamakita, Y.1    Ono, S.2    Matsumura, F.3    Yamashiro, S.4
  • 45
    • 0021827569 scopus 로고
    • Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells
    • Yamashiro-Matsumura S., Matsumura F. Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells. J. Biol. Chem. 260:1985;5087-5097.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5087-5097
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 46
    • 0031694209 scopus 로고    scopus 로고
    • Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells
    • Yamashiro S., Yamakita Y., Ono S., Matsumura F. Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells. Mol. Biol. Cell. 9:1998;993-1006.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 993-1006
    • Yamashiro, S.1    Yamakita, Y.2    Ono, S.3    Matsumura, F.4


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