메뉴 건너뛰기




Volumn 4, Issue 6, 2014, Pages

A phenomenological density-scaling approach to lamellipodial actin dynamics

Author keywords

actin dynamics; actin network; Lamellipodium; Photoactivation

Indexed keywords


EID: 84908190345     PISSN: 20428898     EISSN: 20428901     Source Type: Journal    
DOI: 10.1098/rsfs.2014.0006     Document Type: Article
Times cited : (16)

References (42)
  • 1
    • 0027194759 scopus 로고
    • Cellular motions and thermal fluctuations: The Brownian ratchet
    • Peskin, C, Odell, G, Oster, G. 1993 Cellular motions and thermal fluctuations: the Brownian ratchet. Biophys. J. 65, 316–324.(doi:10.1016/S0006-3495(93)81035-X)
    • (1993) Biophys. J , vol.65 , pp. 316-324
    • Peskin, C.1    Odell, G.2    Oster, G.3
  • 2
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin  polymerization
    • Mogilner, A, Oster, G. 1996 Cell motility driven by actin  polymerization. Biophys. J. 71, 3030–3045.(doi:10.1016/S0006-3495(96)79496-1)
    • (1996) Biophys. J , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 3
    • 33846672361 scopus 로고    scopus 로고
    • Lamellipodial actin  mechanically links myosin activity with adhesion-site formation
    • Giannone, G et al. 2007 Lamellipodial actin  mechanically links myosin activity with adhesion-site formation. Cell 128, 561–575.(doi:10.1016/j. cell.2006.12.039)
    • (2007) Cell , vol.128 , pp. 561-575
    • Giannone, G.1
  • 4
    • 33748556828 scopus 로고    scopus 로고
    • Direct measurement of the lamellipodial protrusive force in a migrating cell
    • Prass, M, Jacobson, K, Mogilner, A. 2006 Direct measurement of the lamellipodial protrusive force in a migrating cell. J. Cell Biol. 174, 767–772.(doi:10.1083/jcb.200601159)
    • (2006) J. Cell Biol , vol.174 , pp. 767-772
    • Prass, M.1    Jacobson, K.2    Mogilner, A.3
  • 6
    • 1942469424 scopus 로고    scopus 로고
    • Forces generated during actin -based propulsion: A direct measurement by micromanipulation
    • Marcy, Y, Prost, J, Carlier, MF, Sykes, C. 2004 Forces generated during actin -based propulsion: a direct measurement by micromanipulation. Proc. Natl Acad. Sci. USA 101, 5992–5997.(doi:10.1073/pnas. 0307704101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 5992-5997
    • Marcy, Y.1    Prost, J.2    Carlier, M.F.3    Sykes, C.4
  • 7
    • 0024109183 scopus 로고
    • Cytoskeletal dynamics and nerve growth
    • Mitchison, T, Kirschner, M. 1988 Cytoskeletal dynamics and nerve growth. Neuron 1, 761–772.(doi:10.1016/0896-6273(88)90124-9)
    • (1988) Neuron , vol.1 , pp. 761-772
    • Mitchison, T.1    Kirschner, M.2
  • 10
    • 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.(doi:10. 1083/jcb.139.2.397)
    • (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
  • 11
    • 0032568650 scopus 로고    scopus 로고
    • The interactin of Arp2/3 complex with actin : Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Dyche Mullins, R, Heuser, J, Pollard, T. 1998 The interactin of Arp2/3 complex with actin : nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl Acad. Sci. USA 95, 6181–6186.(doi:10.1073/pnas.95.11.6181)
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Dyche Mullins, R.1    Heuser, J.2    Pollard, T.3
  • 12
    • 0022881322 scopus 로고
    • Rate constants for the reactins of ATP- and ADP-actin  with the ends of actin  filaments
    • Pollard, T. 1986 Rate constants for the reactins of ATP- and ADP-actin  with the ends of actin  filaments. J. Cell Biol. 103, 2747–2754.(doi:10. 1083/jcb.103.6.2747)
    • (1986) J. Cell Biol , vol.103 , pp. 2747-2754
    • Pollard, T.1
  • 13
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin  filaments
    • Pollard, T, Borisy, GG. 2003 Cellular motility driven by assembly and disassembly of actin  filaments. Cell 112, 453–465.(doi:10.1016/S0092-8674(03)00120-X)
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.1    Borisy, G.G.2
  • 14
    • 41949088527 scopus 로고    scopus 로고
    • Arp2/3 complex interactins and actin  network turnover in lamellipodia
    • Lai, FP et al. 2008 Arp2/3 complex interactins and actin  network turnover in lamellipodia. EMBO J. 27, 982–992.(doi:10.1038/emboj.2008.34)
    • (2008) EMBO J , vol.27 , pp. 982-992
    • Lai, F.P.1
  • 15
    • 4544309783 scopus 로고    scopus 로고
    • Two distinct actin  networks drive the protrusion of migrating cells
    • Ponti, A. 2004 Two distinct actin  networks drive the protrusion of migrating cells. Science 305, 1782–1786.(doi:10.1126/science.1100533)
    • (2004) Science , vol.305 , pp. 1782-1786
    • Ponti, A.1
  • 16
    • 33845700946 scopus 로고    scopus 로고
    • actin  turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin  network: Evidence of frequent filament severing
    • Miyoshi, T, Tsuji, T, Higashida, C. 2006 actin  turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin  network: evidence of frequent filament severing. J. Cell Biol. 175, 947–955.(doi:10.1083/jcb.200604176)
    • (2006) J. Cell Biol , vol.175 , pp. 947-955
    • Miyoshi, T.1    Tsuji, T.2    Higashida, C.3
  • 17
    • 62849104599 scopus 로고    scopus 로고
    • An order of magnitude faster AIP1-associated actin  disruption than nucleation by the Arp2/3 complex in lamellipodia
    • Tsuji, T, Miyoshi, T, Higashida, C, Narumiya, S, Watanabe, N. 2009 An order of magnitude faster AIP1-associated actin  disruption than nucleation by the Arp2/3 complex in lamellipodia. PLoS ONE 4, e4921.(doi:10.1371/journal.pone.0004921)
    • (2009) PLoS ONE , pp. 4
    • Tsuji, T.1    Miyoshi, T.2    Higashida, C.3    Narumiya, S.4    Watanabe, N.5
  • 18
    • 84876314947 scopus 로고    scopus 로고
    • Can filament treadmilling alone account for the F-actin  turnover in lamellipodia?
    • Miyoshi, T, Watanabe, N. 2013 Can filament treadmilling alone account for the F-actin  turnover in lamellipodia? Cytoskeleton 70, 179–190.(doi:10. 1002/cm.21098)
    • (2013) Cytoskeleton , vol.70 , pp. 179-190
    • Miyoshi, T.1    Watanabe, N.2
  • 19
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: cellular control of actin  assembly
    • Campellone, KG, Welch, MD. 2010 A nucleator arms race: cellular control of actin  assembly. Nat. Rev. Mol. Cell Biol. 11, 237–251.(doi:10.1038/ nrm2867)
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 20
    • 0030843484 scopus 로고    scopus 로고
    • actin  depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin -based motility
    • Carlier, MF, Laurent, V, Santolini, J, Melki, R, Didry, D, Xia, G-X, Hong, Y, Chua, N-H, Pantaloni, D. 1997 actin  depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin -based motility. J. Cell Biol. 136, 1307–1323.(doi:10. 1083/jcb.136.6.1307)
    • (1997) J. Cell Biol , vol.136 , pp. 1307-1323
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.-X.6    Hong, Y.7    Chua, N.-H.8    Pantaloni, D.9
  • 21
    • 12844269159 scopus 로고    scopus 로고
    • actin -depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin  depolymerization in mammalian nonmuscle cells
    • Hotulainen, P. 2004 actin -depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin  depolymerization in mammalian nonmuscle cells. Mol. Biol. Cell 16, 649–664.(doi:10.1091/ mbc.E04-07-0555)
    • (2004) Mol. Biol. Cell , vol.16 , pp. 649-664
    • Hotulainen, P.1
  • 22
    • 48249121534 scopus 로고    scopus 로고
    • actin  disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers
    • Kueh, HY, Charras, GT, Mitchison, TJ, Brieher, WM. 2008 actin  disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers. J. Cell Biol. 182, 341–353.(doi:10.1083/ jcb.200801027)
    • (2008) J. Cell Biol , vol.182 , pp. 341-353
    • Kueh, H.Y.1    Charras, G.T.2    Mitchison, T.J.3    Brieher, W.M.4
  • 23
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin  polymerization and defines the direction of cell motility
    • Ghosh, M, Song, X, Mouneimne, G, Sidani, M, Lawrence, DS, Condeelis, J. 2004 Cofilin promotes actin  polymerization and defines the direction of cell motility. Science, 304, 743–746.(doi:10.1126/ science.1094561)
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.6
  • 24
    • 0025785552 scopus 로고
    • Control of actin  polymerization in live and permeabilized fibroblasts
    • Symons, MH, Mitchison, TJ. 1991 Control of actin  polymerization in live and permeabilized fibroblasts. J. Cell Biol. 114, 503–513.(doi:10.1083/jcb. 114.3.503)
    • (1991) J. Cell Biol , vol.114 , pp. 503-513
    • Symons, M.H.1    Mitchison, T.J.2
  • 25
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
    • Wang, YL. 1985 Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J. Cell Biol. 101, 597–602.(doi:10. 1083/jcb.101.2.597)
    • (1985) J. Cell Biol , vol.101 , pp. 597-602
    • Wang, Y.L.1
  • 26
    • 0025740949 scopus 로고
    • actin  microfilament dynamics in locomoting cells
    • Theriot, JA, Mitchison, TJ. 1991 actin  microfilament dynamics in locomoting cells. Nature 352, 126–131.(doi:10.1038/352126a0)
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 27
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin  filament turnover in lamellipodia
    • Watanabe, N, Mitchison, TJ. 2002 Single-molecule speckle analysis of actin  filament turnover in lamellipodia. Science 295, 1083–1086.(doi:10. 1126/science.1067470)
    • (2002) Science , vol.295 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 28
    • 84872032983 scopus 로고    scopus 로고
    • A comparison of computational models for eukaryotic cell shape and motility
    • Holmes, WR, Edelstein-Keshet, L. 2012 A comparison of computational models for eukaryotic cell shape and motility. PLoS Comput. Biol. 8, e1002793.(doi:10.1371/journal.pcbi.1002793)
    • (2012) PLoS Comput. Biol , pp. 8
    • Holmes, W.R.1    Edelstein-Keshet, L.2
  • 29
    • 35448981763 scopus 로고    scopus 로고
    • Mathematical modeling of cell migration
    • Carlsson, AE, Sept, D. 2008 Mathematical modeling of cell migration. Methods Cell Biol. 84, 911–937.(doi:10.1016/S0091-679X(07) 84029-5)
    • (2008) Methods Cell Biol , vol.84 , pp. 911-937
    • Carlsson, A.E.1    Sept, D.2
  • 30
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson, GH. 2002 A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297, 1873–1877.(doi:10.1126/science. 1074952)
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1
  • 32
    • 77952555125 scopus 로고    scopus 로고
    • Inside view of cell locomotion through single-molecule: Fast F-/G-actin  cycle and G-actin  regulation of polymer restoration
    • Watanabe, N. 2010 Inside view of cell locomotion through single-molecule: fast F-/G-actin  cycle and G-actin  regulation of polymer restoration. Proc. Jpn Acad. B Phys. Biol. Sci. 86, 62–83.(doi:10.2183/ pjab.86.62)
    • (2010) Proc. Jpn Acad. B Phys. Biol. Sci , vol.86 , pp. 62-83
    • Watanabe, N.1
  • 33
    • 0028861944 scopus 로고
    • Interpreting photoactivated fluorescence microscopy measurements of steady-state actin  dynamics
    • Tardy, Y, McGrath, JL, Hartwig, JH, Dewey, CF. 1995 Interpreting photoactivated fluorescence microscopy measurements of steady-state actin  dynamics. Biophys. J. 69, 1674–1682.(doi:10.1016/S0006-3495(95)80085-8)
    • (1995) Biophys. J , vol.69 , pp. 1674-1682
    • Tardy, Y.1    McGrath, J.L.2    Hartwig, J.H.3    Dewey, C.F.4
  • 34
    • 18544399146 scopus 로고    scopus 로고
    • Measuring chemotaxis and chemokinesis: The under-agarose cell migration assay
    • Heit, B, Kubes, P. 2003 Measuring chemotaxis and chemokinesis: the under-agarose cell migration assay. Sci. Signal. 2003, p l5.(doi:10.1126/stke.2003. 170.pl5)
    • (2003) Sci. Signal , pp. l5
    • Heit, B.1    Kubes, P.2
  • 35
    • 0036708436 scopus 로고    scopus 로고
    • Regulation of actin  dynamics in rapidly moving cells: A quantitative analysis
    • Mogilner, A, Edelstein-Keshet, L. 2002 Regulation of actin  dynamics in rapidly moving cells: a quantitative analysis. Biophys. J. 83, 1237–1258.(doi:10.1016/S0006-3495(02)73897-6)
    • (2002) Biophys. J , vol.83 , pp. 1237-1258
    • Mogilner, A.1    Edelstein-Keshet, L.2
  • 36
    • 33747167610 scopus 로고    scopus 로고
    • actin  filament branching and protrusion velocity in a simple 1D model of a motile cell
    • Dawes, AT, Bard Ermentrout, G, Cytrynbaum, E, Edelstein-Keshet, L. 2006 actin  filament branching and protrusion velocity in a simple 1D model of a motile cell. J. Theor. Biol. 242, 265–279.(doi:10. 1016/j.jtbi.2006.02.017)
    • (2006) J. Theor. Biol , vol.242 , pp. 265-279
    • Dawes, A.T.1    Bard Ermentrout, G.2    Cytrynbaum, E.3    Edelstein-Keshet, L.4
  • 37
    • 69249212192 scopus 로고    scopus 로고
    • Characterization of two classes of small molecule inhibitors of Arp2/3 complex
    • Nolen, B, Tomasevic, N, Russell, A, Pierce, D. 2009 Characterization of two classes of small molecule inhibitors of Arp2/3 complex. Nature 460, 1031–1035.(doi:10.1038/nature 08231)
    • (2009) Nature , vol.460 , pp. 1031-1035
    • Nolen, B.1    Tomasevic, N.2    Russell, A.3    Pierce, D.4
  • 38
    • 13944273671 scopus 로고    scopus 로고
    • Cell migration without a lamellipodium: Translation of actin  dynamics into cell movement mediated by tropomyosin
    • Gupton, SL et al. 2005 Cell migration without a lamellipodium: translation of actin  dynamics into cell movement mediated by tropomyosin. J. Cell Biol. 168, 619–631.(doi:10.1083/jcb.200406063)
    • (2005) J. Cell Biol , vol.168 , pp. 619-631
    • Gupton, S.L.1
  • 39
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin -filament nucleation, capping, and disassembly
    • Iwasa, J, Mullins, R. 2007 Spatial and temporal relationships between actin -filament nucleation, capping, and disassembly. Curr. Biol. 17, 395–406.(doi:10.1016/j.cub.2007.02.012)
    • (2007) Curr. Biol , vol.17 , pp. 395-406
    • Iwasa, J.1    Mullins, R.2
  • 40
    • 84874980720 scopus 로고    scopus 로고
    • Arp2/3 complex ATP hydrolysis promotes lamellipodial actin  network disassembly but is dispensable for assembly
    • Ingerman, E, Hsiao, JY, Mullins, R. 2013 Arp2/3 complex ATP hydrolysis promotes lamellipodial actin  network disassembly but is dispensable for assembly. J. Cell Biol. 200, 619–633.(doi:10.1083/ jcb.201211069)
    • (2013) J. Cell Biol , vol.200 , pp. 619-633
    • Ingerman, E.1    Hsiao, J.Y.2    Mullins, R.3
  • 41
    • 80054710650 scopus 로고    scopus 로고
    • LIM kinase has a dual role in regulating lamellipodium extension by decelerating the rate of actin  retrograde flow and the rate of actin  polymerization
    • Ohashi, K, Fujiwara, S, Watanabe, T, Kondo, H, Kiuchi, T, Sato, M, Mizuno, K. 2011 LIM kinase has a dual role in regulating lamellipodium extension by decelerating the rate of actin  retrograde flow and the rate of actin  polymerization. J. Biol. Chem. 286, 36340–36351.(doi:10.1074/jbc.M111.259135)
    • (2011) J. Biol. Chem , vol.286 , pp. 36340-36351
    • Ohashi, K.1    Fujiwara, S.2    Watanabe, T.3    Kondo, H.4    Kiuchi, T.5    Sato, M.6    Mizuno, K.7
  • 42
    • 34248227301 scopus 로고    scopus 로고
    • Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin  monomers
    • Kiuchi, T, Ohashi, K, Kurita, S, Mizuno, K. 2007 Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin  monomers. J. Cell Biol. 177, 465–476.(doi:10.1083/jcb.200610005)
    • (2007) J. Cell Biol , vol.177 , pp. 465-476
    • Kiuchi, T.1    Ohashi, K.2    Kurita, S.3    Mizuno, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.