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Volumn 90, Issue 12, 2006, Pages 4295-4304

Energetics and dynamics of constrained actin filament bundling

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN;

EID: 33744830290     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.076968     Document Type: Article
Times cited : (16)

References (54)
  • 2
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina, T. M., and G. G. Borisy. 1999. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145:1009-1026.
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 3
    • 0035949715 scopus 로고    scopus 로고
    • Self-organization of a propulsive actin network as an evolutionary process
    • Maly, I. V., and G. G. Borisy. 2001. Self-organization of a propulsive actin network as an evolutionary process. Proc. Natl. Acad. Sci. USA. 98:11324-11329.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11324-11329
    • Maly, I.V.1    Borisy, G.G.2
  • 4
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D., and G. G. Borisy. 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
  • 5
    • 0037452054 scopus 로고    scopus 로고
    • The cytoskeleton, cellular motility and the reductionist agenda
    • Pollard, T. D. 2003. The cytoskeleton, cellular motility and the reductionist agenda. Nature. 422:741-745.
    • (2003) Nature , vol.422 , pp. 741-745
    • Pollard, T.D.1
  • 6
    • 0034496280 scopus 로고    scopus 로고
    • Association of cortactin with dynamic actin in lamellipodia and on endosomal vesicles
    • Kaksonen, M., H. B. Peng, and H. Rauvala. 2000. Association of cortactin with dynamic actin in lamellipodia and on endosomal vesicles. J. Cell Sci. 113:4421-4426.
    • (2000) J. Cell Sci. , vol.113 , pp. 4421-4426
    • Kaksonen, M.1    Peng, H.B.2    Rauvala, H.3
  • 8
    • 0141545013 scopus 로고    scopus 로고
    • Long continuous actin bundles in Drosophila bristles are constructed by overlapping short filaments
    • Guild, G. M., P. S. Connelly, L. Ruggiero, K. A. Vranich, and L. G. Tilney. 2003. Long continuous actin bundles in Drosophila bristles are constructed by overlapping short filaments. J. Cell Biol. 162:1069-1077.
    • (2003) J. Cell Biol. , vol.162 , pp. 1069-1077
    • Guild, G.M.1    Connelly, P.S.2    Ruggiero, L.3    Vranich, K.A.4    Tilney, L.G.5
  • 9
    • 0026437563 scopus 로고
    • Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity
    • Lewis, A. K., and P. C. Bridgman. 1992. Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity. J. Cell Biol. 119:1219-1243.
    • (1992) J. Cell Biol. , vol.119 , pp. 1219-1243
    • Lewis, A.K.1    Bridgman, P.C.2
  • 11
    • 23244441861 scopus 로고    scopus 로고
    • The physics of filopodial protrusion
    • Mogilner, A., and B. Rubinstein. 2005. The physics of filopodial protrusion. Biophys. J. 89:782-795.
    • (2005) Biophys. J. , vol.89 , pp. 782-795
    • Mogilner, A.1    Rubinstein, B.2
  • 14
    • 0035140487 scopus 로고    scopus 로고
    • Role of the actin bundling protein fascin in growth cone morphogenesis: Localization in filopodia and lamellipodia
    • Cohan, C. S., E. A. Welnhofer, L. Zhao, F. Matsumura, and S. Yamashiro. 2001. Role of the actin bundling protein fascin in growth cone morphogenesis: localization in filopodia and lamellipodia. Cell Motil. Cytoskeleton. 48:109-120.
    • (2001) Cell Motil. Cytoskeleton , vol.48 , pp. 109-120
    • Cohan, C.S.1    Welnhofer, E.A.2    Zhao, L.3    Matsumura, F.4    Yamashiro, S.5
  • 15
    • 4644346321 scopus 로고    scopus 로고
    • Fascin protrusions in cell interactions
    • Adams, J. C. 2004. Fascin protrusions in cell interactions. Trends Cardiovasc. Med. 14:221-226.
    • (2004) Trends Cardiovasc. Med. , vol.14 , pp. 221-226
    • Adams, J.C.1
  • 16
    • 0028106038 scopus 로고
    • cDNA cloning and expression of the human homolog of the sea urchin fascin and Drosophila singed genes, which encode an actin-bundling protein
    • Duh, F., F. Latif, Y. Weng, L. Geil, W. Modi, T. Stackhouse, F. Matsumura, D. Duan, W. Linehan, M. Lerman, and J. Gnarra. 1994. cDNA cloning and expression of the human homolog of the sea urchin fascin and Drosophila singed genes, which encode an actin-bundling protein. DNA Cell Biol. 13:821-827.
    • (1994) DNA Cell Biol. , vol.13 , pp. 821-827
    • Duh, F.1    Latif, F.2    Weng, Y.3    Geil, L.4    Modi, W.5    Stackhouse, T.6    Matsumura, F.7    Duan, D.8    Linehan, W.9    Lerman, M.10    Gnarra, J.11
  • 17
    • 0018068395 scopus 로고
    • Separation and interaction of the major components of sea urchin actin gel
    • Bryan, J., and R. E. Kane. 1978. Separation and interaction of the major components of sea urchin actin gel. J. Mol. Biol. 125:207-224.
    • (1978) J. Mol. Biol. , vol.125 , pp. 207-224
    • Bryan, J.1    Kane, R.E.2
  • 18
    • 0028269631 scopus 로고
    • Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension
    • Cant, K., B. A. Knowles, M. S. Mooseker, and L. Cooley. 1994. Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. J. Cell Biol. 125:369-380.
    • (1994) J. Cell Biol. , vol.125 , pp. 369-380
    • Cant, K.1    Knowles, B.A.2    Mooseker, M.S.3    Cooley, L.4
  • 19
    • 0028902746 scopus 로고
    • Cloning and expression of a murine fascin homolog from mouse brain
    • Edwards, R. A., H. Herrera-Sosa, J. Otto, and J. Bryan. 1995. Cloning and expression of a murine fascin homolog from mouse brain. J. Biol. Chem. 270:10764-10770.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10764-10770
    • Edwards, R.A.1    Herrera-Sosa, H.2    Otto, J.3    Bryan, J.4
  • 20
    • 0018483411 scopus 로고
    • Formation of filopodia in coelomocytes: Localization of fascin, a 58,000 Dalton actin crosslinking protein
    • Otto, J. J., R. E. Kane, and J. Bryan. 1979. Formation of filopodia in coelomocytes: localization of fascin, a 58,000 Dalton actin crosslinking protein. Cell. 17:285-293.
    • (1979) Cell , vol.17 , pp. 285-293
    • Otto, J.J.1    Kane, R.E.2    Bryan, J.3
  • 21
    • 0028799146 scopus 로고
    • Fascins, a family of actin bundling proteins
    • Edwards, R. A., and J. Bryan. 1995. Fascins, a family of actin bundling proteins. Cell Motil. Cytoskeleton. 32:1-9.
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 1-9
    • Edwards, R.A.1    Bryan, J.2
  • 22
    • 15844362435 scopus 로고    scopus 로고
    • Phosphorylation of human fascin inhibits its action binding and bundling activities
    • Yamakita, Y., S. Ono, F. Matsumura, and S. Yamashiro. 1996. Phosphorylation of human fascin inhibits its action binding and bundling activities. J. Biol. Chem. 271:12632-12638.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12632-12638
    • Yamakita, Y.1    Ono, S.2    Matsumura, F.3    Yamashiro, S.4
  • 23
    • 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
  • 24
    • 0030814006 scopus 로고    scopus 로고
    • Actin filament cables in Drosophila nurse cells are composed of modules that slide passively past one another during dumping
    • Guild, G. M., P. S. Connelly, M. K. Shaw, and L. G. Tilney. 1997. Actin filament cables in Drosophila nurse cells are composed of modules that slide passively past one another during dumping. J. Cell Biol. 138:783-797.
    • (1997) J. Cell Biol. , vol.138 , pp. 783-797
    • Guild, G.M.1    Connelly, P.S.2    Shaw, M.K.3    Tilney, L.G.4
  • 25
    • 0026472782 scopus 로고
    • Assembly of the intestinal brush border cytoskeleton
    • Heintzelman, M. B., and M. S. Mooseker. 1992. Assembly of the intestinal brush border cytoskeleton. Curr. Top. Dev. Biol. 26:93-122.
    • (1992) Curr. Top. Dev. Biol. , vol.26 , pp. 93-122
    • Heintzelman, M.B.1    Mooseker, M.S.2
  • 26
    • 0024152090 scopus 로고
    • Hair cells: Transduction, tuning, and transmission in the inner ear
    • Roberts, W. M., J. Howard, and A. J. Hudspeth. 1988. Hair cells: transduction, tuning, and transmission in the inner ear. Annu. Rev. Cell Biol. 4:63-92.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 63-92
    • Roberts, W.M.1    Howard, J.2    Hudspeth, A.J.3
  • 29
    • 0033627645 scopus 로고    scopus 로고
    • Models for spatial polymerization dynamics of rod-like polymers
    • Edelstein-Keshet, L., and G. B. Ermentrout. 2000. Models for spatial polymerization dynamics of rod-like polymers. J. Math. Biol. 40:64-96.
    • (2000) J. Math. Biol. , vol.40 , pp. 64-96
    • Edelstein-Keshet, L.1    Ermentrout, G.B.2
  • 30
    • 10044240503 scopus 로고    scopus 로고
    • Kinetics of filament bundling with attractive interactions
    • Yu, X., and A. E. Carlsson. 2004. Kinetics of filament bundling with attractive interactions. Biophys. J. 87:3679-3689.
    • (2004) Biophys. J. , vol.87 , pp. 3679-3689
    • Yu, X.1    Carlsson, A.E.2
  • 31
    • 37649028306 scopus 로고    scopus 로고
    • Collapse of a semiflexible polymer in poor solvent
    • Montesi, A., M. Pasquali, and F. C. MacKintosh. 2004. Collapse of a semiflexible polymer in poor solvent. Phys. Rev. E. 69:021916.
    • (2004) Phys. Rev. E , vol.69 , pp. 021916
    • Montesi, A.1    Pasquali, M.2    MacKintosh, F.C.3
  • 32
    • 22944472087 scopus 로고    scopus 로고
    • Brownian dynamics algorithm for bead-rod semiflexible chain with anisotropic friction
    • Montesi, A., D. C. Morse, and M. Pasquali. 2005. Brownian dynamics algorithm for bead-rod semiflexible chain with anisotropic friction. J. Chem. Phys. 122:084903.
    • (2005) J. Chem. Phys. , vol.122 , pp. 084903
    • Montesi, A.1    Morse, D.C.2    Pasquali, M.3
  • 34
    • 0037433090 scopus 로고    scopus 로고
    • Viscoelasticity of suspensions of long, rigid rods
    • Dhont, J. K., and W. J. Briels. 2003. Viscoelasticity of suspensions of long, rigid rods. Colloids Surf. A. 213:131-156.
    • (2003) Colloids Surf. A , vol.213 , pp. 131-156
    • Dhont, J.K.1    Briels, W.J.2
  • 35
    • 0037439719 scopus 로고    scopus 로고
    • Inhomogeneous suspensions of rigid rods in flow
    • Dhont, J. K., and W. J. Briels. 2003. Inhomogeneous suspensions of rigid rods in flow. J. Chem. Phys. 118:1466-1478.
    • (2003) J. Chem. Phys. , vol.118 , pp. 1466-1478
    • Dhont, J.K.1    Briels, W.J.2
  • 36
    • 22544482060 scopus 로고    scopus 로고
    • Brownian dynamics simulations of the self-and collective rotational diffusion coefficients of rigid long thin rods
    • Tao, Y.-G., W. K. den Otter, J. T. Padding, J. K. G. Dhont, and W. J. Briels. 2005. Brownian dynamics simulations of the self-and collective rotational diffusion coefficients of rigid long thin rods. J. Chem. Phys. 122:244903.
    • (2005) J. Chem. Phys. , vol.122 , pp. 244903
    • Tao, Y.-G.1    Den Otter, W.K.2    Padding, J.T.3    Dhont, J.K.G.4    Briels, W.J.5
  • 37
    • 0037636333 scopus 로고    scopus 로고
    • Simulation of F-actin filaments of several microns
    • Ming, D., Y. Kong, Y. Wu, and J. Ma. 2003. Simulation of F-actin filaments of several microns. Biophys. J. 85:27-35.
    • (2003) Biophys. J. , vol.85 , pp. 27-35
    • Ming, D.1    Kong, Y.2    Wu, Y.3    Ma, J.4
  • 39
    • 0034804332 scopus 로고    scopus 로고
    • Growth of branched actin networks against obstacles
    • Carlsson, A. E. 2001. Growth of branched actin networks against obstacles. Biophys. J. 81:1907-1923.
    • (2001) Biophys. J. , vol.81 , pp. 1907-1923
    • Carlsson, A.E.1
  • 40
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • Gittes, F., B. Mickey, J. Nettleton, and J. Howard. 1993. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 120:923-934.
    • (1993) J. Cell Biol. , vol.120 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 41
    • 0031207977 scopus 로고    scopus 로고
    • Elastohydrodynamic study of actin filaments using fluorescence microscopy
    • Riveline, D., C. H. Wiggins, R. E. Goldstein, and A. Ott. 1997. Elastohydrodynamic study of actin filaments using fluorescence microscopy. Phys. Rev. E. 56:R1330-R1333.
    • (1997) Phys. Rev. E , vol.56
    • Riveline, D.1    Wiggins, C.H.2    Goldstein, R.E.3    Ott, A.4
  • 42
    • 0001660186 scopus 로고
    • Measurement of the persistence length of polymerized actin using fluorescence microscopy
    • Ott, A., M. Magnasco, A. Simon, and A. Libchaber. 1993. Measurement of the persistence length of polymerized actin using fluorescence microscopy. Phys. Rev. E. 48:R1642-R1645.
    • (1993) Phys. Rev. E , vol.48
    • Ott, A.1    Magnasco, M.2    Simon, A.3    Libchaber, A.4
  • 43
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert, H., P. Venier, A. Maggs, A. Fattoum, R. Kassab, D. Pantaloni, and M. Carlier. 1995. Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J. Biol. Chem. 270:11437-11444.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.3    Fattoum, A.4    Kassab, R.5    Pantaloni, D.6    Carlier, M.7
  • 44
    • 0021204075 scopus 로고
    • Detection and characterization of actin monomers, oligomers, and filaments in solution by measurement of fluorescence photobleaching recovery
    • Lanni, F., and B. R. Ware. 1984. Detection and characterization of actin monomers, oligomers, and filaments in solution by measurement of fluorescence photobleaching recovery. Biophys. J. 46:97-110.
    • (1984) Biophys. J. , vol.46 , pp. 97-110
    • Lanni, F.1    Ware, B.R.2
  • 45
    • 0032819362 scopus 로고    scopus 로고
    • The actin-based nanomachine at the leading edge of migrating cells
    • Abraham, V. C., V. Krishnamurthi, D. L. Taylor, and F. Lanni. 1999. The actin-based nanomachine at the leading edge of migrating cells. Biophys. J. 77:1721-1732.
    • (1999) Biophys. J. , vol.77 , pp. 1721-1732
    • Abraham, V.C.1    Krishnamurthi, V.2    Taylor, D.L.3    Lanni, F.4
  • 47
    • 0345413328 scopus 로고    scopus 로고
    • Multiscale study of counterion-induced attraction and bundle formation of F-actin using an Ising-like mean-field model
    • Yu, X., and A. E. Carlsson. 2003. Multiscale study of counterion-induced attraction and bundle formation of F-actin using an Ising-like mean-field model. Biophys. J. 85:3532-3543.
    • (2003) Biophys. J. , vol.85 , pp. 3532-3543
    • Yu, X.1    Carlsson, A.E.2
  • 48
    • 0027162413 scopus 로고
    • Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels
    • Wachsstock, D., W. Schwarz, and T. Pollard. 1993. Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels. Biophys. J. 65:205-214.
    • (1993) Biophys. J. , vol.65 , pp. 205-214
    • Wachsstock, D.1    Schwarz, W.2    Pollard, T.3
  • 49
    • 0028265522 scopus 로고
    • Crosslinker dynamics determine the mechanical properties of actin gels
    • Wachsstock, D., W. Schwarz, and T. Pollard. 1994. Crosslinker dynamics determine the mechanical properties of actin gels. Biophys. J. 66:801-809.
    • (1994) Biophys. J. , vol.66 , pp. 801-809
    • Wachsstock, D.1    Schwarz, W.2    Pollard, T.3
  • 50
    • 0021259403 scopus 로고
    • Acanthamoeba castellanii capping protein: Properties, mechanism of action, immunologic cross-reactivity, and localization
    • Cooper, J. A., J. D. Blum, and T. D. Pollard. 1984. Acanthamoeba castellanii capping protein: properties, mechanism of action, immunologic cross-reactivity, and localization. J. Cell Biol. 99:217-225.
    • (1984) J. Cell Biol. , vol.99 , pp. 217-225
    • Cooper, J.A.1    Blum, J.D.2    Pollard, T.D.3
  • 51
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphosphoinositides
    • Schafer, D. A., P. B. Jennings, and J. A. Cooper. 1996. Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides. J. Cell Biol. 135:169-179.
    • (1996) J. Cell Biol. , vol.135 , pp. 169-179
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 52
    • 1142310674 scopus 로고    scopus 로고
    • End versus side branching by Arp2/3 complex
    • Carlsson, A. E., M. A. Wear, and J. A. Cooper. 2004. End versus side branching by Arp2/3 complex. Biophys. J. 86:1074-1081.
    • (2004) Biophys. J. , vol.86 , pp. 1074-1081
    • Carlsson, A.E.1    Wear, M.A.2    Cooper, J.A.3
  • 53
    • 0035094485 scopus 로고    scopus 로고
    • The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments
    • Amann, K. J., and T. D. Pollard. 2001. The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments. Nat. Cell Biol. 3:306-310.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 306-310
    • Amann, K.J.1    Pollard, T.D.2
  • 54
    • 23244458300 scopus 로고    scopus 로고
    • The effect of branching on the critical concentration and average filament length of actin
    • Carlsson, A. E. 2005. The effect of branching on the critical concentration and average filament length of actin. Biophys. J. 89:130-140.
    • (2005) Biophys. J. , vol.89 , pp. 130-140
    • Carlsson, A.E.1


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