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Volumn 1853, Issue 11, 2015, Pages 3006-3014

Reconstituting the actin cytoskeleton at or near surfaces in vitro

Author keywords

Actin cortex; Actin polymerization; Actin based motility; Biomimetic systems; Contractility; Lamellipodium

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX; LIPOSOME; MYOSIN; PLASTIC; BACTERIAL PROTEIN; MEMBRANE PROTEIN;

EID: 84944155623     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.07.021     Document Type: Review
Times cited : (16)

References (114)
  • 1
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard T.D. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 1986, 103:2747-2754.
    • (1986) J. Cell Biol. , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 3
    • 84938330770 scopus 로고    scopus 로고
    • Model systems for studying cell adhesion and biomimetic actin networks
    • Brüggemann D., Frohnmayer J.P., Spatz J.P. Model systems for studying cell adhesion and biomimetic actin networks. Beilstein J. Nanotechnol. 2014, 5:1193-1202.
    • (2014) Beilstein J. Nanotechnol. , vol.5 , pp. 1193-1202
    • Brüggemann, D.1    Frohnmayer, J.P.2    Spatz, J.P.3
  • 4
    • 84867192170 scopus 로고    scopus 로고
    • Minimal systems to study membrane-cytoskeleton interactions
    • Vogel S.K., Schwille P. Minimal systems to study membrane-cytoskeleton interactions. Curr. Opin. Biotechnol. 2012, 23:758-765.
    • (2012) Curr. Opin. Biotechnol. , vol.23 , pp. 758-765
    • Vogel, S.K.1    Schwille, P.2
  • 5
    • 84873720325 scopus 로고    scopus 로고
    • In vitro studies of actin filament and network dynamics
    • Mullins R.D., Hansen S.D. In vitro studies of actin filament and network dynamics. Curr. Opin. Cell Biol. 2013, 25:6-13.
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 6-13
    • Mullins, R.D.1    Hansen, S.D.2
  • 6
    • 69249235852 scopus 로고    scopus 로고
    • Biology under construction: in vitro reconstitution of cellular function
    • Liu A.P., Fletcher D.A. Biology under construction: in vitro reconstitution of cellular function. Nat. Rev. Mol. Cell Biol. 2009, 10:644-650.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 644-650
    • Liu, A.P.1    Fletcher, D.A.2
  • 7
    • 69249215233 scopus 로고    scopus 로고
    • Biomimetic membrane systems to study cellular organization
    • Loose M., Schwille P. Biomimetic membrane systems to study cellular organization. J. Struct. Biol. 2009, 168:143-151.
    • (2009) J. Struct. Biol. , vol.168 , pp. 143-151
    • Loose, M.1    Schwille, P.2
  • 8
    • 0027316090 scopus 로고
    • The wily ways of a parasite: induction of actin assembly by Listeria
    • Tilney L.G., Tilney M.S. The wily ways of a parasite: induction of actin assembly by Listeria. Trends Microbiol. 1993, 1:25-31.
    • (1993) Trends Microbiol. , vol.1 , pp. 25-31
    • Tilney, L.G.1    Tilney, M.S.2
  • 9
    • 0028918040 scopus 로고
    • Actin-based bacterial motility
    • Cossart P. Actin-based bacterial motility. Curr. Opin. Cell Biol. 1995, 7:94-101.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 94-101
    • Cossart, P.1
  • 10
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot J.A., Mitchison T.J. Actin microfilament dynamics in locomoting cells. Nature 1991, 352:126-131.
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 11
    • 0026547790 scopus 로고
    • The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization
    • Theriot J.A., Mitchison T.J., Tilney L.G., Portnoy D.A. The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature 1992, 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
  • 12
    • 0027194759 scopus 로고
    • Cellular motions and thermal fluctuations: the Brownian ratchet
    • Peskin C.S., Odell G.M., Oster G.F. Cellular motions and thermal fluctuations: the Brownian ratchet. Biophys. J. 1993, 65:316-324.
    • (1993) Biophys. J. , vol.65 , pp. 316-324
    • Peskin, C.S.1    Odell, G.M.2    Oster, G.F.3
  • 13
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • Mogilner A., Oster G. Cell motility driven by actin polymerization. Biophys. J. 1996, 71:3030-3045.
    • (1996) Biophys. J. , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 14
    • 0033055077 scopus 로고    scopus 로고
    • A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii
    • Gouin E., Gantelet H., Egile C., Lasa I., Ohayon H., Villiers V., Gounon P., Sansonetti P.J., Cossart P. A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii. J. Cell Sci. 1999, 112:1697-1708.
    • (1999) J. Cell Sci. , vol.112 , pp. 1697-1708
    • Gouin, E.1    Gantelet, H.2    Egile, C.3    Lasa, I.4    Ohayon, H.5    Villiers, V.6    Gounon, P.7    Sansonetti, P.J.8    Cossart, P.9
  • 15
    • 0029294733 scopus 로고
    • The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins
    • Pistor S., Chakraborty T., Walter U., Wehland J. The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins. Curr. Biol. 1995, 5:517-525.
    • (1995) Curr. Biol. , vol.5 , pp. 517-525
    • Pistor, S.1    Chakraborty, T.2    Walter, U.3    Wehland, J.4
  • 16
    • 0030908903 scopus 로고    scopus 로고
    • The isolated comet tail pseudopodium of Listeria monocytogenes: a tail of two actin filament populations, long and axial and short and random
    • Sechi A., Wehland J., Small J.V. The isolated comet tail pseudopodium of Listeria monocytogenes: a tail of two actin filament populations, long and axial and short and random. J. Cell Biol. 1997, 137:155-167.
    • (1997) J. Cell Biol. , vol.137 , pp. 155-167
    • Sechi, A.1    Wehland, J.2    Small, J.V.3
  • 17
    • 0034617996 scopus 로고    scopus 로고
    • Three regions within ActA promote Arp2/3 complex-mediated actin nucleation and Listeria monocytogenes motility
    • Skoble J., Portnoy D.A., Welch M.D. Three regions within ActA promote Arp2/3 complex-mediated actin nucleation and Listeria monocytogenes motility. J. Cell Biol. 2000, 150:527-537.
    • (2000) J. Cell Biol. , vol.150 , pp. 527-537
    • Skoble, J.1    Portnoy, D.A.2    Welch, M.D.3
  • 18
    • 0035494440 scopus 로고    scopus 로고
    • Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility
    • Skoble J., Auerbuch V., Goley E.D., Welch M.D., Portnoy D.A. Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility. J. Cell Biol. 2001, 155:89-100.
    • (2001) J. Cell Biol. , vol.155 , pp. 89-100
    • Skoble, J.1    Auerbuch, V.2    Goley, E.D.3    Welch, M.D.4    Portnoy, D.A.5
  • 19
    • 0036323119 scopus 로고    scopus 로고
    • Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/Vasodilator-stimulated Phosphoprotein (VASP) function during cell migration
    • Loureiro J.J., Rubinson D.A., Bear J.E., Baltus G.A., Kwiatkowski A.V., Gertler F.B. Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/Vasodilator-stimulated Phosphoprotein (VASP) function during cell migration. Mol. Biol. Cell 2002, 13:2533-2546.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2533-2546
    • Loureiro, J.J.1    Rubinson, D.A.2    Bear, J.E.3    Baltus, G.A.4    Kwiatkowski, A.V.5    Gertler, F.B.6
  • 20
    • 0036320467 scopus 로고    scopus 로고
    • Contribution of Ena/VASP proteins to intracellular motility of Listeria requires phosphorylation and proline-rich core but not F-actin binding or multimerization
    • Geese M., Loureiro J.J., Bear J.E., Wehland J., Gertler F.B., Sechi A.S. Contribution of Ena/VASP proteins to intracellular motility of Listeria requires phosphorylation and proline-rich core but not F-actin binding or multimerization. Mol. Biol. Cell 2002, 13:2383-2396.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2383-2396
    • Geese, M.1    Loureiro, J.J.2    Bear, J.E.3    Wehland, J.4    Gertler, F.B.5    Sechi, A.S.6
  • 21
    • 0035193153 scopus 로고    scopus 로고
    • Effects of intermediate filaments on actin-based motility of Listeria monocytogenes
    • Giardini P.A., Theriot J.A. Effects of intermediate filaments on actin-based motility of Listeria monocytogenes. Biophys. J. 2001, 81:3193-3203.
    • (2001) Biophys. J. , vol.81 , pp. 3193-3203
    • Giardini, P.A.1    Theriot, J.A.2
  • 23
    • 0028173688 scopus 로고
    • Involvement of profilin in the actin-based motility of L. monocytogenes in cells and cell-free extracts
    • Theriot J.A., Rosenblatt J., Portnoy D.A., Goldschimdt-Clermont P.J., Mitchison T.J. Involvement of profilin in the actin-based motility of L. monocytogenes in cells and cell-free extracts. Cell 1994, 76:505-517.
    • (1994) Cell , vol.76 , pp. 505-517
    • Theriot, J.A.1    Rosenblatt, J.2    Portnoy, D.A.3    Goldschimdt-Clermont, P.J.4    Mitchison, T.J.5
  • 25
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins R.D., Heuser J.A., Pollard T.D. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. 1998, 95:6181-6186.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 26
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch M.D., Rosenblatt J., Skoble J., Portnoy D.A., Mitchison T.J. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 1998, 281:105-108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 28
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel T.P., Boujemaa R., Pantaloni D., Carlier M.F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 1999, 401:613-616.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 29
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/Cofilin
    • Andrianantoandro E., Pollard T.D. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/Cofilin. Mol. Cell 2006, 24:13-23.
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 30
    • 84919647021 scopus 로고    scopus 로고
    • Aip1 destabilizes cofilin-saturated actin filaments by severing and accelerating monomer dissociation from ends
    • Nadkarni A.V., Brieher W.M. Aip1 destabilizes cofilin-saturated actin filaments by severing and accelerating monomer dissociation from ends. Curr. Biol. 2014, 24:2749-2757.
    • (2014) Curr. Biol. , vol.24 , pp. 2749-2757
    • Nadkarni, A.V.1    Brieher, W.M.2
  • 31
    • 84921652672 scopus 로고    scopus 로고
    • Aip1 promotes actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring
    • Chen Q., Courtemanche N., Pollard T.D. Aip1 promotes actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring. J. Biol. Chem. 2015, 290:2289-2300.
    • (2015) J. Biol. Chem. , vol.290 , pp. 2289-2300
    • Chen, Q.1    Courtemanche, N.2    Pollard, T.D.3
  • 36
    • 84873096363 scopus 로고    scopus 로고
    • Actin filament elongation in Arp2/3-derived networks is controlled by three distinct mechanisms
    • Michelot A., Grassart A., Okreglak V., Costanzo M., Boone C., Drubin D.G. Actin filament elongation in Arp2/3-derived networks is controlled by three distinct mechanisms. Dev. Cell 2013, 24:182-195.
    • (2013) Dev. Cell , vol.24 , pp. 182-195
    • Michelot, A.1    Grassart, A.2    Okreglak, V.3    Costanzo, M.4    Boone, C.5    Drubin, D.G.6
  • 39
    • 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., Borisy G.C. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 1999, 145:1009-1026.
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.C.2
  • 41
    • 3142699814 scopus 로고    scopus 로고
    • The effect of diffusion, depolymerization and nucleation promoting factors on actin gel growth
    • Plastino J., Lelidis I., Prost J., Sykes C. The effect of diffusion, depolymerization and nucleation promoting factors on actin gel growth. Eur. Biophys. J. 2004, 33:310-320.
    • (2004) Eur. Biophys. J. , vol.33 , pp. 310-320
    • Plastino, J.1    Lelidis, I.2    Prost, J.3    Sykes, C.4
  • 45
    • 0033587188 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex
    • Yarar D., To W., Abo A., Welch M.D. The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 1999, 9:555-558.
    • (1999) Curr. Biol. , vol.9 , pp. 555-558
    • Yarar, D.1    To, W.2    Abo, A.3    Welch, M.D.4
  • 47
    • 0035887313 scopus 로고    scopus 로고
    • A WASP-VASP complex regulates actin polymerization at the plasma membrane
    • Castellano F., Le Clainche C., Patin D., Carlier M.-F., Chavrier P. A WASP-VASP complex regulates actin polymerization at the plasma membrane. EMBO J. 2001, 20:5603-5614.
    • (2001) EMBO J. , vol.20 , pp. 5603-5614
    • Castellano, F.1    Le Clainche, C.2    Patin, D.3    Carlier, M.-F.4    Chavrier, P.5
  • 49
    • 4644298002 scopus 로고    scopus 로고
    • Actin filaments align into hollow comets for rapid VASP-mediated propulsion
    • Plastino J., Olivier S., Sykes C. Actin filaments align into hollow comets for rapid VASP-mediated propulsion. Curr. Biol. 2004, 14:1766-1771.
    • (2004) Curr. Biol. , vol.14 , pp. 1766-1771
    • Plastino, J.1    Olivier, S.2    Sykes, C.3
  • 50
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero S., Le Clainche C., Didry D., Egile C., Pantaloni D., Carlier M.-F. Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 2004, 119:419-429.
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    Le Clainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.-F.6
  • 53
    • 33748579946 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography
    • Morone N., Fujiwara T., Murase K., Kasai R.S., Ike H., Yuasa S., Usukura J., Kusumi A. Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography. J. Cell Biol. 2006, 174:851-862.
    • (2006) J. Cell Biol. , vol.174 , pp. 851-862
    • Morone, N.1    Fujiwara, T.2    Murase, K.3    Kasai, R.S.4    Ike, H.5    Yuasa, S.6    Usukura, J.7    Kusumi, A.8
  • 55
    • 84895542705 scopus 로고    scopus 로고
    • Homeostatic actin cytoskeleton networks are regulated by assembly factor competition for monomers
    • Burke T.A., Christensen J.R., Barone E., Suarez C., Sirotkin V., Kovar D.R. Homeostatic actin cytoskeleton networks are regulated by assembly factor competition for monomers. Curr. Biol. 2014, 24:579-585.
    • (2014) Curr. Biol. , vol.24 , pp. 579-585
    • Burke, T.A.1    Christensen, J.R.2    Barone, E.3    Suarez, C.4    Sirotkin, V.5    Kovar, D.R.6
  • 57
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-Wasp and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R., Ma L., Miki H., Lopez M., Kirchausen H., Takenawa T., Kirschner M. The interaction between N-Wasp and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 1999, 97:221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchausen, H.5    Takenawa, T.6    Kirschner, M.7
  • 58
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky L.M., Insall R.H. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 1998, 8:1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 59
    • 0032403083 scopus 로고    scopus 로고
    • WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac
    • Miki H., Suetsugu S., Takenawa T. WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 1998, 17:6932-6941.
    • (1998) EMBO J. , vol.17 , pp. 6932-6941
    • Miki, H.1    Suetsugu, S.2    Takenawa, T.3
  • 61
    • 0142026447 scopus 로고    scopus 로고
    • Regulation of actin dynamics by WASP family proteins
    • Miki H., Takenawa T. Regulation of actin dynamics by WASP family proteins. J. Biochem. 2003, 134:309-313.
    • (2003) J. Biochem. , vol.134 , pp. 309-313
    • Miki, H.1    Takenawa, T.2
  • 62
    • 1942469424 scopus 로고    scopus 로고
    • Forces generated during actin-based propulsion: a direct measurement by micromanipulation
    • Marcy Y., Prost J., Carlier M.-F., Sykes C. Forces generated during actin-based propulsion: a direct measurement by micromanipulation. Proc. Natl. Acad. Sci. U. S. A. 2004, 5992-5997.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , pp. 5992-5997
    • Marcy, Y.1    Prost, J.2    Carlier, M.-F.3    Sykes, C.4
  • 64
    • 0035846598 scopus 로고    scopus 로고
    • Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
    • Zalevsky J., Lempert L., Kranitz H., Mullins R.D. Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities. Curr. Biol. 2001, 11:1903-1913.
    • (2001) Curr. Biol. , vol.11 , pp. 1903-1913
    • Zalevsky, J.1    Lempert, L.2    Kranitz, H.3    Mullins, R.D.4
  • 67
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: cellular control of actin assembly
    • Campellone K.G., Welch M.D. A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 2010, 11:237-251.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 70
    • 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 R.D. Capping protein increases the rate of actin-based motility by promoting filament nucleation by the Arp2/3 complex. Cell 2008, 133:841-851.
    • (2008) Cell , vol.133 , pp. 841-851
    • Akin, O.1    Mullins, R.D.2
  • 74
    • 0038652046 scopus 로고    scopus 로고
    • Compression forces generated by actin comet tails on lipid vesicles
    • Giardini P.A., Fletcher D.A., Theriot J.A. Compression forces generated by actin comet tails on lipid vesicles. Proc. Natl. Acad. Sci. 2003, 100:6493-6498.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 6493-6498
    • Giardini, P.A.1    Fletcher, D.A.2    Theriot, J.A.3
  • 75
    • 42749108949 scopus 로고    scopus 로고
    • Soft Listeria: actin-based propulsion of liquid drops
    • (061906/061901-061906/061904)
    • Boukellal H., Campas O., Joanny J.-F., Prost J., Sykes C. Soft Listeria: actin-based propulsion of liquid drops. Phys. Rev. E 2004, 69. (061906/061901-061906/061904).
    • (2004) Phys. Rev. E , vol.69
    • Boukellal, H.1    Campas, O.2    Joanny, J.-F.3    Prost, J.4    Sykes, C.5
  • 76
    • 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 K.H.D., Gaucher J.-F., Carlier M.-F., Romet-Lemonne G. 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, 94:4890-4905.
    • (2008) Biophys. J. , vol.94 , pp. 4890-4905
    • Delatour, V.1    Helfer, E.2    Didry, D.3    Lê, K.H.D.4    Gaucher, J.-F.5    Carlier, M.-F.6    Romet-Lemonne, G.7
  • 77
    • 33846820108 scopus 로고    scopus 로고
    • VASP governs actin dynamics by modulating filament anchoring
    • Trichet L., Campas O., Sykes C., Plastino J. VASP governs actin dynamics by modulating filament anchoring. Biophys. J. 2007, 92:1081-1089.
    • (2007) Biophys. J. , vol.92 , pp. 1081-1089
    • Trichet, L.1    Campas, O.2    Sykes, C.3    Plastino, J.4
  • 78
    • 84155163062 scopus 로고    scopus 로고
    • Cortactin releases the brakes in actin-based motility by enhancing WASP-VCA detachment from Arp2/3 branches
    • Siton O., Ideses Y., Albeck S., Unger T., Bershadsky A.D., Gov N.S., Bernheim-Groswasser A. Cortactin releases the brakes in actin-based motility by enhancing WASP-VCA detachment from Arp2/3 branches. Curr. Biol. 2011, 21:2092-2097.
    • (2011) Curr. Biol. , vol.21 , pp. 2092-2097
    • Siton, O.1    Ideses, Y.2    Albeck, S.3    Unger, T.4    Bershadsky, A.D.5    Gov, N.S.6    Bernheim-Groswasser, A.7
  • 79
    • 33847420373 scopus 로고    scopus 로고
    • Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains
    • Co C., Wong D.T., Gierke S., Change V., Taunton J. Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains. Cell 2007, 128:901-913.
    • (2007) Cell , vol.128 , pp. 901-913
    • Co, C.1    Wong, D.T.2    Gierke, S.3    Change, V.4    Taunton, J.5
  • 80
    • 35649021883 scopus 로고    scopus 로고
    • Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP
    • Ferron F., Rebowski G., Lee S.H., Dominguez R. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 2007, 26:4597-4606.
    • (2007) EMBO J. , vol.26 , pp. 4597-4606
    • Ferron, F.1    Rebowski, G.2    Lee, S.H.3    Dominguez, R.4
  • 81
    • 33845368663 scopus 로고    scopus 로고
    • Actin polymerization serves as a membrane domain switch in model lipid bilayers
    • Liu A.P., Fletcher D.A. Actin polymerization serves as a membrane domain switch in model lipid bilayers. Biophys. J. 2006, 91:4064-4070.
    • (2006) Biophys. J. , vol.91 , pp. 4064-4070
    • Liu, A.P.1    Fletcher, D.A.2
  • 83
    • 77956537388 scopus 로고    scopus 로고
    • Self-assembly of filopodia-like structures on supported lipid bilayers
    • Lee K., Gallop J.L., Rambani K., Kirschner M.W. Self-assembly of filopodia-like structures on supported lipid bilayers. Science 2010, 329:1341-1345.
    • (2010) Science , vol.329 , pp. 1341-1345
    • Lee, K.1    Gallop, J.L.2    Rambani, K.3    Kirschner, M.W.4
  • 85
    • 0037495920 scopus 로고    scopus 로고
    • On the organization of self-assembled actin networks in giant vesicles
    • Limozin L., Bärmann M., Sackmann E. On the organization of self-assembled actin networks in giant vesicles. Eur. Phys. J. E 2003, 10:319-330.
    • (2003) Eur. Phys. J. E , vol.10 , pp. 319-330
    • Limozin, L.1    Bärmann, M.2    Sackmann, E.3
  • 86
    • 18744363662 scopus 로고    scopus 로고
    • Polymorphism of cross-linked actin networks in giant vesicles
    • Limozin L., Sackmann E. Polymorphism of cross-linked actin networks in giant vesicles. Phys. Rev. Lett. 2002, 89:168103.
    • (2002) Phys. Rev. Lett. , vol.89 , pp. 168103
    • Limozin, L.1    Sackmann, E.2
  • 87
    • 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. U. S. A. 1992, 89:11547-11551.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11547-11551
    • Miyata, H.1    Hotani, H.2
  • 89
    • 80051487510 scopus 로고    scopus 로고
    • Encapsulation of active cytoskeletal protein networks in cell-sized liposomes
    • Tsai F.-C., Stuhrmann B., Koenderink G. Encapsulation of active cytoskeletal protein networks in cell-sized liposomes. Langmuir 2011, 27:10061-10071.
    • (2011) Langmuir , vol.27 , pp. 10061-10071
    • Tsai, F.-C.1    Stuhrmann, B.2    Koenderink, G.3
  • 91
    • 33748264168 scopus 로고    scopus 로고
    • Actin-binding proteins sensitively mediate F-actin bundle stiffness
    • Claessens M.M.A.E., Bathe M., Frey E., Bausch A.R. Actin-binding proteins sensitively mediate F-actin bundle stiffness. Nat. Mater. 2006, 5:748-753.
    • (2006) Nat. Mater. , vol.5 , pp. 748-753
    • Claessens, M.M.A.E.1    Bathe, M.2    Frey, E.3    Bausch, A.R.4
  • 92
    • 84896370127 scopus 로고    scopus 로고
    • Alignment of nematic and bundled semiflexible polymers in cell-sized confinement
    • Alvarado J., Mulder B.M., Koenderink G.H. Alignment of nematic and bundled semiflexible polymers in cell-sized confinement. Soft Matter 2014, 10:2354-2364.
    • (2014) Soft Matter , vol.10 , pp. 2354-2364
    • Alvarado, J.1    Mulder, B.M.2    Koenderink, G.H.3
  • 93
    • 84887525898 scopus 로고    scopus 로고
    • The biology of boundary conditions: cellular reconstitution in one, two, and three dimensions
    • Vahey M.D., Fletcher D.A. The biology of boundary conditions: cellular reconstitution in one, two, and three dimensions. Curr. Opin. Cell Biol. 2014, 26:60-68.
    • (2014) Curr. Opin. Cell Biol. , vol.26 , pp. 60-68
    • Vahey, M.D.1    Fletcher, D.A.2
  • 94
    • 59449108327 scopus 로고    scopus 로고
    • Reconstitution and anchoring of cytoskeleton inside giant unilamellar vesicles
    • Merkle D., Kahya N., Schwille P. Reconstitution and anchoring of cytoskeleton inside giant unilamellar vesicles. ChemBioChem 2008, 9:2673-2681.
    • (2008) ChemBioChem , vol.9 , pp. 2673-2681
    • Merkle, D.1    Kahya, N.2    Schwille, P.3
  • 96
    • 84899636675 scopus 로고    scopus 로고
    • Mimicking the mechanical properties of the cell cortex by the self-assembly of an actin cortex in vesicles
    • Luo T., Srivastava V., Ren Y., Robinson D.N. Mimicking the mechanical properties of the cell cortex by the self-assembly of an actin cortex in vesicles. Appl. Phys. Lett. 2014, 104:153701.
    • (2014) Appl. Phys. Lett. , vol.104 , pp. 153701
    • Luo, T.1    Srivastava, V.2    Ren, Y.3    Robinson, D.N.4
  • 98
    • 84899888780 scopus 로고    scopus 로고
    • Symmetry breaking in reconstituted actin cortices
    • Shah E.A., Keren K. Symmetry breaking in reconstituted actin cortices. eLife 2014, 3:e01433.
    • (2014) eLife , vol.3 , pp. e01433
    • Shah, E.A.1    Keren, K.2
  • 99
    • 84921777202 scopus 로고    scopus 로고
    • Dynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins
    • Suetsugu S., Kurisu S., Takenawa T. Dynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins. Physiol. Rev. 2014, 94:1219-1248.
    • (2014) Physiol. Rev. , vol.94 , pp. 1219-1248
    • Suetsugu, S.1    Kurisu, S.2    Takenawa, T.3
  • 103
    • 84902653316 scopus 로고    scopus 로고
    • Actomyosin sliding is attenuated in contractile biomimetic cortices
    • Murrell M., Gardel M.L. Actomyosin sliding is attenuated in contractile biomimetic cortices. Mol. Biol. Cell 2014, 25:1845-1853.
    • (2014) Mol. Biol. Cell , vol.25 , pp. 1845-1853
    • Murrell, M.1    Gardel, M.L.2
  • 109
    • 84858246364 scopus 로고    scopus 로고
    • ADF/Cofilin regulates actomyosin assembly through competitive inhibition of Myosin II binding to F-actin
    • Wiggan O., Shaw A.E., DeLuca J.G., Bamburg J.R. ADF/Cofilin regulates actomyosin assembly through competitive inhibition of Myosin II binding to F-actin. Dev. Cell 2012, 22:530-543.
    • (2012) Dev. Cell , vol.22 , pp. 530-543
    • Wiggan, O.1    Shaw, A.E.2    DeLuca, J.G.3    Bamburg, J.R.4
  • 110
    • 84862124625 scopus 로고    scopus 로고
    • Actin depolymerization drives actomyosin ring contraction during budding yeast cytokinesis
    • Mendes Pinto I., Rubinstein B., Kucharavy A., Unruh J.R., Li R. Actin depolymerization drives actomyosin ring contraction during budding yeast cytokinesis. Dev. Cell 2012, 22:1247-1260.
    • (2012) Dev. Cell , vol.22 , pp. 1247-1260
    • Mendes Pinto, I.1    Rubinstein, B.2    Kucharavy, A.3    Unruh, J.R.4    Li, R.5
  • 111
    • 36549035377 scopus 로고    scopus 로고
    • A cytoskeletal demolition worker: myosin II acts as an actin depolymerization agent
    • Haviv L., Gillo D., Backouche F., Bernheim-Groswasser A. A cytoskeletal demolition worker: myosin II acts as an actin depolymerization agent. J. Mol. Biol. 2008, 375:325-330.
    • (2008) J. Mol. Biol. , vol.375 , pp. 325-330
    • Haviv, L.1    Gillo, D.2    Backouche, F.3    Bernheim-Groswasser, A.4
  • 112
    • 84871395592 scopus 로고    scopus 로고
    • F-actin buckling coordinates contractility and severing in a biomimetic actomyosin cortex
    • Murrell M.P., Gardel M.L. F-actin buckling coordinates contractility and severing in a biomimetic actomyosin cortex. Proc. Natl. Acad. Sci. 2012, 109:20820-20825.
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 20820-20825
    • Murrell, M.P.1    Gardel, M.L.2
  • 113
    • 84875910049 scopus 로고    scopus 로고
    • Myosin motors fragment and compact membrane-bound actin filaments
    • Vogel S.K., Petrasek Z., Heinemann F., Schwille P. Myosin motors fragment and compact membrane-bound actin filaments. eLife 2013, 2:e00116.
    • (2013) eLife , vol.2 , pp. e00116
    • Vogel, S.K.1    Petrasek, Z.2    Heinemann, F.3    Schwille, P.4
  • 114
    • 0026515440 scopus 로고
    • L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • Kocks C., Gouin E., Tabouret M., Berche P., Ohayon H., Cossart P. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 1992, 68:521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, E.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6


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