메뉴 건너뛰기




Volumn 7, Issue 2, 2012, Pages

Actin filament attachments for sustained motility in vitro are maintained by filament bundling

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; CAPPING PROTEIN; CELL PROTEIN; PROFILIN; UNCLASSIFIED DRUG; ACTIN CAPPING PROTEIN; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 84863180524     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0031385     Document Type: Article
Times cited : (11)

References (103)
  • 1
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin- agarose
    • Machesky LM, Atkinson SJ, Ampe C, Vandekerckhove J, Pollard TD, (1994) Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin- agarose. J Cell Biol 127: 107-115.
    • (1994) J Cell Biol , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 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 TM, Borisy GG, (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
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins
    • Higgs HN, Pollard TD, (2001) Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annual review of biochemistry 70: 649-676.
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 4
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG, (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
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel TP, Boujemaa R, Pantaloni D, Carlier M-F, (1999) Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401: 613-616.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.-F.4
  • 6
    • 0026547790 scopus 로고
    • The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization
    • Theriot JA, Mitchison TJ, Tilney LG, Portnoy DA, (1992) The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature 357: 257-260.
    • (1992) Nature , vol.357 , pp. 257-260
    • Theriot, J.A.1    Mitchison, T.J.2    Tilney, L.G.3    Portnoy, D.A.4
  • 8
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes
    • Tilney LG, Portnoy DA, (1989) Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol 109: 1597-1608.
    • (1989) J Cell Biol , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 9
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile C, Loisel TP, Laurent V, Li R, Pantaloni D, et al. (1999) Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J Cell Biol 146: 1319-1332.
    • (1999) J Cell Biol , vol.146 , pp. 1319-1332
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5
  • 13
    • 0028173688 scopus 로고
    • Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts
    • Theriot JA, Rosenblatt J, Portnoy DA, Goldschmidt-Clermont PJ, Mitchison TJ, (1994) Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts. Cell 76: 505-517.
    • (1994) Cell , vol.76 , pp. 505-517
    • Theriot, J.A.1    Rosenblatt, J.2    Portnoy, D.A.3    Goldschmidt-Clermont, P.J.4    Mitchison, T.J.5
  • 14
    • 0026577663 scopus 로고
    • A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin
    • Domann E, Wehland J, Rohde M, Pistor S, Hartl M, et al. (1992) A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. The EMBO journal 11: 1981-1990.
    • (1992) The EMBO Journal , vol.11 , pp. 1981-1990
    • Domann, E.1    Wehland, J.2    Rohde, M.3    Pistor, S.4    Hartl, M.5
  • 15
    • 77957267234 scopus 로고    scopus 로고
    • Cytoskeletal Mechanisms for Breaking Symmetry
    • Mullins RD, (2010) Cytoskeletal Mechanisms for Breaking Symmetry. Cold Spring Harb Perspect Biol 2: a003392.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Mullins, R.D.1
  • 16
    • 70349766884 scopus 로고    scopus 로고
    • In silico reconstitution of actin-based symmetry breaking and motility
    • Dayel MJ, Akin O, Landeryou M, Risca V, Mogilner A, et al. (2009) In silico reconstitution of actin-based symmetry breaking and motility. PLoS biology 7: e1000201.
    • (2009) PLoS Biology , vol.7
    • Dayel, M.J.1    Akin, O.2    Landeryou, M.3    Risca, V.4    Mogilner, A.5
  • 17
    • 67650679132 scopus 로고    scopus 로고
    • A Multi-Scale Mechanistic Model for Actin-Propelled Bacteria
    • Dickinson RB, (2008) A Multi-Scale Mechanistic Model for Actin-Propelled Bacteria. Cellular and Molecular Bioengineering 1: 110-121.
    • (2008) Cellular and Molecular Bioengineering , vol.1 , pp. 110-121
    • Dickinson, R.B.1
  • 20
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch MD, Iwamatsu A, Mitchison TJ, (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
  • 21
    • 0037415575 scopus 로고    scopus 로고
    • A biomimetic motility assay provides insight into the mechanism of actin-based motility
    • Wiesner S, Helfer E, Didry D, Ducouret G, Lafuma F, et al. (2003) A biomimetic motility assay provides insight into the mechanism of actin-based motility. J Cell Biol 160: 387-398.
    • (2003) J Cell Biol , vol.160 , pp. 387-398
    • Wiesner, S.1    Helfer, E.2    Didry, D.3    Ducouret, G.4    Lafuma, F.5
  • 22
    • 53049085712 scopus 로고    scopus 로고
    • Close packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization
    • Footer MJ, Lyo JK, Theriot JA, (2008) Close packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization. The Journal of biological chemistry 283: 23852-23862.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 23852-23862
    • Footer, M.J.1    Lyo, J.K.2    Theriot, J.A.3
  • 26
    • 33847420373 scopus 로고    scopus 로고
    • Mechanism of Actin Network Attachment to Moving Membranes: Barbed End Capture by N-WASP WH2 Domains
    • Co C, Wong DT, Gierke S, Chang V, Taunton J, (2007) Mechanism of Actin Network Attachment to Moving Membranes: Barbed End Capture by N-WASP WH2 Domains. Cell 128: 901-913.
    • (2007) Cell , vol.128 , pp. 901-913
    • Co, C.1    Wong, D.T.2    Gierke, S.3    Chang, V.4    Taunton, J.5
  • 27
    • 45849083156 scopus 로고    scopus 로고
    • Arp2/3 controls the motile behavior of N-WASP-functionalized GUVs and modulates N-WASP surface distribution by mediating transient links with actin filaments
    • Delatour V, Helfer E, Didry D, Lê KHD, Gaucher J-F, et al. (2008) Arp2/3 controls the motile behavior of N-WASP-functionalized GUVs and modulates N-WASP surface distribution by mediating transient links with actin filaments. Biophys J.
    • (2008) Biophys J
    • Delatour, V.1    Helfer, E.2    Didry, D.3    Lê, K.H.D.4    Gaucher, J.-F.5
  • 28
    • 17244373549 scopus 로고    scopus 로고
    • Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement
    • Giganti A, Plastino J, Janji B, van Troys M, Lentz D, et al. (2005) Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement. Journal of cell science 118: 1255-1265.
    • (2005) Journal of Cell Science , vol.118 , pp. 1255-1265
    • Giganti, A.1    Plastino, J.2    Janji, B.3    van Troys, M.4    Lentz, D.5
  • 29
    • 0141504153 scopus 로고    scopus 로고
    • Polymer motors: pushing out the front and pulling up the back
    • Mogilner A, Oster G, (2003) Polymer motors: pushing out the front and pulling up the back. Curr Biol 13: R721-733.
    • (2003) Curr Biol , vol.13
    • Mogilner, A.1    Oster, G.2
  • 30
    • 0037339268 scopus 로고    scopus 로고
    • Force Generation by Actin Polymerization II: The Elastic Ratchet and Tethered Filaments
    • Mogilner A, Oster G, (2003) Force Generation by Actin Polymerization II: The Elastic Ratchet and Tethered Filaments. Biophys J 84: 1591-1605.
    • (2003) Biophys J , vol.84 , pp. 1591-1605
    • Mogilner, A.1    Oster, G.2
  • 32
    • 14044270698 scopus 로고    scopus 로고
    • In silico reconstitution of Listeria propulsion exhibits nano-saltation
    • Alberts JB, Odell GM, (2004) In silico reconstitution of Listeria propulsion exhibits nano-saltation. PLoS biology 2: e412.
    • (2004) PLoS Biology , vol.2
    • Alberts, J.B.1    Odell, G.M.2
  • 33
  • 34
    • 77957267062 scopus 로고    scopus 로고
    • Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation
    • Rebowski G, Namgoong S, Boczkowska M, Leavis PC, Navaza J, et al. (2010) Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation. Journal of molecular biology 403: 11-23.
    • (2010) Journal of Molecular Biology , vol.403 , pp. 11-23
    • Rebowski, G.1    Namgoong, S.2    Boczkowska, M.3    Leavis, P.C.4    Navaza, J.5
  • 35
    • 35348969696 scopus 로고    scopus 로고
    • The beta-Thymosin/WH2 Fold: Multifunctionality and Structure
    • Dominguez R, (2007) The beta-Thymosin/WH2 Fold: Multifunctionality and Structure. Annals of the New York Academy of Sciences 1112: 86-94.
    • (2007) Annals of the New York Academy of Sciences , vol.1112 , pp. 86-94
    • Dominguez, R.1
  • 37
    • 0036154207 scopus 로고    scopus 로고
    • Clamped-filament elongation model for actin-based motors
    • Dickinson RB, Purich DL, (2002) Clamped-filament elongation model for actin-based motors. Biophysical Journal 82: 605-617.
    • (2002) Biophysical Journal , vol.82 , pp. 605-617
    • Dickinson, R.B.1    Purich, D.L.2
  • 38
    • 10344258168 scopus 로고    scopus 로고
    • Force Generation by Cytoskeletal Filament End-Tracking Proteins
    • Dickinson RB, Caro L, Purich D, (2004) Force Generation by Cytoskeletal Filament End-Tracking Proteins. Biophysical Journal 87: 2838-2854.
    • (2004) Biophysical Journal , vol.87 , pp. 2838-2854
    • Dickinson, R.B.1    Caro, L.2    Purich, D.3
  • 39
    • 56549108193 scopus 로고    scopus 로고
    • Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation
    • Breitsprecher D, Kiesewetter AK, Linkner J, Urbanke C, Resch GP, et al. (2008) Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation. The EMBO journal 27: 2943-2954.
    • (2008) The EMBO Journal , vol.27 , pp. 2943-2954
    • Breitsprecher, D.1    Kiesewetter, A.K.2    Linkner, J.3    Urbanke, C.4    Resch, G.P.5
  • 40
    • 6944220067 scopus 로고    scopus 로고
    • Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces
    • Kovar DR, Pollard TD, (2004) Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc Natl Acad Sci U S A 101: 14725-14730.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 14725-14730
    • Kovar, D.R.1    Pollard, T.D.2
  • 43
    • 80051977000 scopus 로고    scopus 로고
    • Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex
    • Ti S-C, Jurgenson CT, Nolen BJ, Pollard TD, (2011) Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proc Natl Acad Sci USA 108: E463-471.
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Ti, S.-C.1    Jurgenson, C.T.2    Nolen, B.J.3    Pollard, T.D.4
  • 45
    • 0034698675 scopus 로고    scopus 로고
    • Stimulation of fascin spikes by thrombospondin-1 is mediated by the GTPases Rac and Cdc42
    • Adams JC, Schwartz MA, (2000) Stimulation of fascin spikes by thrombospondin-1 is mediated by the GTPases Rac and Cdc42. J Cell Biol 150: 807-822.
    • (2000) J Cell Biol , vol.150 , pp. 807-822
    • Adams, J.C.1    Schwartz, M.A.2
  • 47
    • 2142654946 scopus 로고    scopus 로고
    • Fascin-mediated propulsion of Listeria monocytogenes independent of frequent nucleation by the Arp2/3 complex
    • Brieher WM, Coughlin M, Mitchison TJ, (2004) Fascin-mediated propulsion of Listeria monocytogenes independent of frequent nucleation by the Arp2/3 complex. J Cell Biol 165: 233-242.
    • (2004) J Cell Biol , vol.165 , pp. 233-242
    • Brieher, W.M.1    Coughlin, M.2    Mitchison, T.J.3
  • 48
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • Amann KJ, Pollard TD, (2001) Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proc Natl Acad Sci U S A 98: 15009-15013.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 49
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • Kuhn JR, Pollard TD, (2005) Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophysical Journal 88: 1387-1402.
    • (2005) Biophysical Journal , vol.88 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 50
    • 43949143882 scopus 로고    scopus 로고
    • Capping Protein Increases the Rate of Actin-Based Motility by Promoting Filament Nucleation by the Arp2/3 Complex
    • Akin O, Mullins RD, (2008) Capping Protein Increases the Rate of Actin-Based Motility by Promoting Filament Nucleation by the Arp2/3 Complex. Cell 133: 841-851.
    • (2008) Cell , vol.133 , pp. 841-851
    • Akin, O.1    Mullins, R.D.2
  • 51
    • 77649187115 scopus 로고    scopus 로고
    • A primer-based mechanism underlies branched actin filament network formation and motility
    • Achard V, Martiel J-L, Michelot A, Guérin C, Reymann A-C, et al. (2010) A primer-based mechanism underlies branched actin filament network formation and motility. Curr Biol 20: 423-428.
    • (2010) Curr Biol , vol.20 , pp. 423-428
    • Achard, V.1    Martiel, J.-L.2    Michelot, A.3    Guérin, C.4    Reymann, A.-C.5
  • 53
    • 0345146913 scopus 로고    scopus 로고
    • Formation of filopodia-like bundles in vitro from a dendritic network
    • Vignjevic D, Yarar D, Welch MD, Peloquin J, Svitkina TM, et al. (2003) Formation of filopodia-like bundles in vitro from a dendritic network. J Cell Biol 160: 951-962.
    • (2003) J Cell Biol , vol.160 , pp. 951-962
    • Vignjevic, D.1    Yarar, D.2    Welch, M.D.3    Peloquin, J.4    Svitkina, T.M.5
  • 55
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end
    • Mejillano MR, Kojima S-i, Applewhite DA, Gertler FB, Svitkina TM, et al. (2004) Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell 118: 363-373.
    • (2004) Cell , vol.118 , pp. 363-373
    • Mejillano, M.R.1    Kojima, S.-i.2    Applewhite, D.A.3    Gertler, F.B.4    Svitkina, T.M.5
  • 56
    • 33947726569 scopus 로고    scopus 로고
    • Crowded surfaces change annealing dynamics of actin filaments
    • Popp D, Yamamoto A, Maeda Y, (2007) Crowded surfaces change annealing dynamics of actin filaments. Journal of molecular biology 368: 365-374.
    • (2007) Journal of Molecular Biology , vol.368 , pp. 365-374
    • Popp, D.1    Yamamoto, A.2    Maeda, Y.3
  • 58
    • 0030012323 scopus 로고    scopus 로고
    • The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation
    • Tang JX, Janmey PA, (1996) The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation. The Journal of biological chemistry 271: 8556-8563.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 8556-8563
    • Tang, J.X.1    Janmey, P.A.2
  • 59
    • 0030845631 scopus 로고    scopus 로고
    • Opposite effects of electrostatics and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes
    • Tang JX, Ito T, Tao T, Traub P, Janmey PA, (1997) Opposite effects of electrostatics and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes. Biochemistry 36: 12600-12607.
    • (1997) Biochemistry , vol.36 , pp. 12600-12607
    • Tang, J.X.1    Ito, T.2    Tao, T.3    Traub, P.4    Janmey, P.A.5
  • 60
    • 50549084090 scopus 로고    scopus 로고
    • Rheological Characterization of the Bundling Transition in F-Actin Solutions Induced by Methylcellulose
    • Köhler S, Lieleg O, Bausch AR, (2008) Rheological Characterization of the Bundling Transition in F-Actin Solutions Induced by Methylcellulose. PloS one 3: e2736.
    • (2008) PloS One , vol.3
    • Köhler, S.1    Lieleg, O.2    Bausch, A.R.3
  • 62
    • 0029970291 scopus 로고    scopus 로고
    • Polymorphism of F-actin assembly. 1. A quantitative phase diagram of F-actin
    • Suzuki A, Yamazaki M, Ito T, (1996) Polymorphism of F-actin assembly. 1. A quantitative phase diagram of F-actin. Biochemistry 35: 5238-5244.
    • (1996) Biochemistry , vol.35 , pp. 5238-5244
    • Suzuki, A.1    Yamazaki, M.2    Ito, T.3
  • 64
    • 1642317185 scopus 로고    scopus 로고
    • Some precautions in using chelators to buffer metals in biological solutions
    • Patton C, Thompson S, Epel D, (2004) Some precautions in using chelators to buffer metals in biological solutions. Cell calcium 35: 427-431.
    • (2004) Cell Calcium , vol.35 , pp. 427-431
    • Patton, C.1    Thompson, S.2    Epel, D.3
  • 65
    • 0003637031 scopus 로고
    • A practical guide to the study of calcium in living cells
    • Nuccitelli R, (1994) A practical guide to the study of calcium in living cells.
    • (1994)
    • Nuccitelli, R.1
  • 68
    • 0020401107 scopus 로고
    • Cytoplasmic pH and free Mg2+ in lymphocytes
    • Rink TJ, Tsien RY, Pozzan T, (1982) Cytoplasmic pH and free Mg2+ in lymphocytes. J Cell Biol 95: 189-196.
    • (1982) J Cell Biol , vol.95 , pp. 189-196
    • Rink, T.J.1    Tsien, R.Y.2    Pozzan, T.3
  • 69
    • 0020825184 scopus 로고
    • Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament
    • Bonder EM, Fishkind DJ, Mooseker MS, (1983) Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell 34: 491-501.
    • (1983) Cell , vol.34 , pp. 491-501
    • Bonder, E.M.1    Fishkind, D.J.2    Mooseker, M.S.3
  • 70
    • 33748264168 scopus 로고    scopus 로고
    • Actin-binding proteins sensitively mediate F-actin bundle stiffness
    • Claessens MMAE, Bathe M, Frey E, Bausch AR, (2006) Actin-binding proteins sensitively mediate F-actin bundle stiffness. Nature Materials 5: 748-753.
    • (2006) Nature Materials , vol.5 , pp. 748-753
    • Claessens, M.M.A.E.1    Bathe, M.2    Frey, E.3    Bausch, A.R.4
  • 73
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation
    • Svitkina TM, Verkhovsky AB, McQuade KM, Borisy GG, (1997) Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J Cell Biol 139: 397-415.
    • (1997) J Cell Biol , vol.139 , pp. 397-415
    • Svitkina, T.M.1    Verkhovsky, A.B.2    McQuade, K.M.3    Borisy, G.G.4
  • 75
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero S, Clainche CL, Didry D, Egile C, Pantaloni D, et al. (2004) Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119: 419-429.
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    Clainche, C.L.2    Didry, D.3    Egile, C.4    Pantaloni, D.5
  • 77
    • 77953637330 scopus 로고    scopus 로고
    • Physical mechanisms of signal integration by WASP family proteins
    • Padrick SB, Rosen MK, (2010) Physical mechanisms of signal integration by WASP family proteins. Annual review of biochemistry 79: 707-735.
    • (2010) Annual Review of Biochemistry , vol.79 , pp. 707-735
    • Padrick, S.B.1    Rosen, M.K.2
  • 78
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides
    • Schafer DA, Jennings PB, Cooper JA, (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
  • 79
    • 0015402533 scopus 로고
    • Roles of magnesium and calcium ions in cell-to-substrate adhesion
    • Takeichi M, Okada TS, (1972) Roles of magnesium and calcium ions in cell-to-substrate adhesion. Experimental cell research 74: 51-60.
    • (1972) Experimental Cell Research , vol.74 , pp. 51-60
    • Takeichi, M.1    Okada, T.S.2
  • 80
    • 35548939067 scopus 로고    scopus 로고
    • Structural basis for ligand recognition by integrins
    • Takagi J, (2007) Structural basis for ligand recognition by integrins. Current opinion in cell biology 19: 557-564.
    • (2007) Current Opinion in Cell Biology , vol.19 , pp. 557-564
    • Takagi, J.1
  • 81
    • 0034636864 scopus 로고    scopus 로고
    • Micromolar Ca2+ concentrations are essential for Mg2+-dependent binding of collagen by the integrin alpha 2beta 1 in human platelets
    • Onley DJ, Knight CG, Tuckwell DS, Barnes MJ, Farndale RW, (2000) Micromolar Ca2+ concentrations are essential for Mg2+-dependent binding of collagen by the integrin alpha 2beta 1 in human platelets. The Journal of biological chemistry 275: 24560-24564.
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 24560-24564
    • Onley, D.J.1    Knight, C.G.2    Tuckwell, D.S.3    Barnes, M.J.4    Farndale, R.W.5
  • 83
    • 0028970566 scopus 로고
    • Regulation of integrin alpha 5 beta 1-fibronectin interactions by divalent cations. Evidence for distinct classes of binding sites for Mn2+, Mg2+, and Ca2+
    • Mould AP, Akiyama SK, Humphries MJ, (1995) Regulation of integrin alpha 5 beta 1-fibronectin interactions by divalent cations. Evidence for distinct classes of binding sites for Mn2+, Mg2+, and Ca2+. The Journal of biological chemistry 270: 26270-26277.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 26270-26277
    • Mould, A.P.1    Akiyama, S.K.2    Humphries, M.J.3
  • 84
    • 0028809343 scopus 로고
    • Shifts in the concentrations of magnesium and calcium in early porcine and rat wound fluids activate the cell migratory response
    • Grzesiak JJ, Pierschbacher MD, (1995) Shifts in the concentrations of magnesium and calcium in early porcine and rat wound fluids activate the cell migratory response. The Journal of clinical investigation 95: 227-233.
    • (1995) The Journal of Clinical Investigation , vol.95 , pp. 227-233
    • Grzesiak, J.J.1    Pierschbacher, M.D.2
  • 86
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly
    • Iwasa JH, Mullins RD, (2007) Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly. Curr Biol 17: 395-406.
    • (2007) Curr Biol , vol.17 , pp. 395-406
    • Iwasa, J.H.1    Mullins, R.D.2
  • 87
    • 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: 1505-1516.
    • (1988) J Cell Biol , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 90
    • 0031771879 scopus 로고    scopus 로고
    • Effects of Insulin and Insulin-like Growth Factor-1 on Intracellular Magnesium of Platelets* 1,* 2
    • Takaya J, Higashino H, Miyazaki R, Kobayashi Y, (1998) Effects of Insulin and Insulin-like Growth Factor-1 on Intracellular Magnesium of Platelets* 1,* 2. Experimental and Molecular Pathology 65: 104-109.
    • (1998) Experimental and Molecular Pathology , vol.65 , pp. 104-109
    • Takaya, J.1    Higashino, H.2    Miyazaki, R.3    Kobayashi, Y.4
  • 92
    • 33846584112 scopus 로고    scopus 로고
    • The logic of the Membrane, Magnesium, Mitosis (MMM) model for the regulation of animal cell proliferation
    • Rubin H, (2007) The logic of the Membrane, Magnesium, Mitosis (MMM) model for the regulation of animal cell proliferation. Archives of biochemistry and biophysics 458: 16-23.
    • (2007) Archives of Biochemistry and Biophysics , vol.458 , pp. 16-23
    • Rubin, H.1
  • 94
    • 0035670941 scopus 로고    scopus 로고
    • Mg(++)-induced endothelial cell migration: substratum selectivity and receptor-involvement
    • Lapidos KA, Woodhouse EC, Kohn EC, Masiero L, (2001) Mg(++)-induced endothelial cell migration: substratum selectivity and receptor-involvement. Angiogenesis 4: 21-28.
    • (2001) Angiogenesis , vol.4 , pp. 21-28
    • Lapidos, K.A.1    Woodhouse, E.C.2    Kohn, E.C.3    Masiero, L.4
  • 96
    • 69849083758 scopus 로고    scopus 로고
    • Basic fibroblast growth factor increases intracellular magnesium concentration through the specific signaling pathways
    • Hong B, Park S, Kim H, Ma T, Kim H, et al. (2009) Basic fibroblast growth factor increases intracellular magnesium concentration through the specific signaling pathways. Molecules and Cells 28: 13-17.
    • (2009) Molecules and Cells , vol.28 , pp. 13-17
    • Hong, B.1    Park, S.2    Kim, H.3    Ma, T.4    Kim, H.5
  • 97
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S, (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. The Journal of biological chemistry 246: 4866-4871.
    • (1971) The Journal of Biological Chemistry , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 98
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • Pollard TD, Cooper JA, (1984) Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry (Mosc) 23: 6631-6641.
    • (1984) Biochemistry (Mosc) , vol.23 , pp. 6631-6641
    • Pollard, T.D.1    Cooper, J.A.2
  • 99
    • 0033576288 scopus 로고    scopus 로고
    • Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization
    • Higgs HN, Blanchoin L, Pollard TD, (1999) Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization. Biochemistry 38: 15212-15222.
    • (1999) Biochemistry , vol.38 , pp. 15212-15222
    • Higgs, H.N.1    Blanchoin, L.2    Pollard, T.D.3
  • 100
    • 0035886026 scopus 로고    scopus 로고
    • Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin
    • Palmgren S, Ojala PJ, Wear MA, Cooper JA, Lappalainen P, (2001) Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin. J Cell Biol 155: 251-260.
    • (2001) J Cell Biol , vol.155 , pp. 251-260
    • Palmgren, S.1    Ojala, P.J.2    Wear, M.A.3    Cooper, J.A.4    Lappalainen, P.5
  • 101
    • 0024470502 scopus 로고
    • Characterization of renatured profilin purified by urea elution from poly-L-proline agarose columns
    • Kaiser DA, Goldschmidt-Clermont PJ, Levine BA, Pollard TD, (1989) Characterization of renatured profilin purified by urea elution from poly-L-proline agarose columns. Cell Motil Cytoskeleton 14: 251-262.
    • (1989) Cell Motil Cytoskeleton , vol.14 , pp. 251-262
    • Kaiser, D.A.1    Goldschmidt-Clermont, P.J.2    Levine, B.A.3    Pollard, T.D.4
  • 102
  • 103
    • 34948838501 scopus 로고    scopus 로고
    • Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins
    • Kuhn JR, Pollard TD, (2007) Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. The Journal of biological chemistry 282: 28014-28024.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 28014-28024
    • Kuhn, J.R.1    Pollard, T.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.