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Volumn 105, Issue 9, 2013, Pages 1946-1955

Modeling the synergy of cofilin and Arp2/3 in lamellipodial protrusive activity

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; ACTIN RELATED PROTEIN 2-3 COMPLEX; TROPOMYOSIN;

EID: 84887383958     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.09.013     Document Type: Article
Times cited : (24)

References (59)
  • 1
    • 0344299281 scopus 로고    scopus 로고
    • Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation
    • M. Bailly, and F. Macaluso J.S. Condeelis Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation J. Cell Biol. 145 1999 331 345
    • (1999) J. Cell Biol. , vol.145 , pp. 331-345
    • Bailly, M.1    Macaluso, F.2    Condeelis, J.S.3
  • 2
    • 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
    • R.D. Mullins, J.A. Heuser, and T.D. Pollard 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. USA 95 1998 6181 6186
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 4
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • T.D. Pollard, and G.G. Borisy Cellular motility driven by assembly and disassembly of actin filaments Cell 112 2003 453 465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 5
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • I. Ichetovkin, W. Grant, and J. Condeelis Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex Curr. Biol. 12 2002 79 84
    • (2002) Curr. Biol. , vol.12 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 6
    • 37249000008 scopus 로고    scopus 로고
    • EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells
    • J. van Rheenen, and X. Song J.S. Condeelis EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells J. Cell Biol. 179 2007 1247 1259
    • (2007) J. Cell Biol. , vol.179 , pp. 1247-1259
    • Van Rheenen, J.1    Song, X.2    Condeelis, J.S.3
  • 7
    • 34249281332 scopus 로고    scopus 로고
    • The cofilin pathway in breast cancer invasion and metastasis
    • W. Wang, R. Eddy, and J. Condeelis The cofilin pathway in breast cancer invasion and metastasis Nat. Rev. Cancer 7 2007 429 440
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 429-440
    • Wang, W.1    Eddy, R.2    Condeelis, J.3
  • 8
    • 0036708436 scopus 로고    scopus 로고
    • Regulation of actin dynamics in rapidly moving cells: A quantitative analysis
    • A. Mogilner, and L. Edelstein-Keshet Regulation of actin dynamics in rapidly moving cells: a quantitative analysis Biophys. J. 83 2002 1237 1258
    • (2002) Biophys. J. , vol.83 , pp. 1237-1258
    • Mogilner, A.1    Edelstein-Keshet, L.2
  • 9
    • 50349095873 scopus 로고    scopus 로고
    • Quantitative analysis of G-actin transport in motile cells
    • I.L. Novak, B.M. Slepchenko, and A. Mogilner Quantitative analysis of G-actin transport in motile cells Biophys. J. 95 2008 1627 1638
    • (2008) Biophys. J. , vol.95 , pp. 1627-1638
    • Novak, I.L.1    Slepchenko, B.M.2    Mogilner, A.3
  • 10
    • 67650391440 scopus 로고    scopus 로고
    • An open model of actin dendritic nucleation
    • J.A. Ditlev, and N.M. Vacanti L.M. Loew An open model of actin dendritic nucleation Biophys. J. 96 2009 3529 3542
    • (2009) Biophys. J. , vol.96 , pp. 3529-3542
    • Ditlev, J.A.1    Vacanti, N.M.2    Loew, L.M.3
  • 11
    • 4444339659 scopus 로고    scopus 로고
    • Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension
    • V. DesMarais, and F. Macaluso M. Bailly Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension J. Cell Sci. 117 2004 3499 3510
    • (2004) J. Cell Sci. , vol.117 , pp. 3499-3510
    • Desmarais, V.1    Macaluso, F.2    Bailly, M.3
  • 12
    • 33751229634 scopus 로고    scopus 로고
    • Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex
    • R.E. Mahaffy, and T.D. Pollard Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex Biophys. J. 91 2006 3519 3528
    • (2006) Biophys. J. , vol.91 , pp. 3519-3528
    • Mahaffy, R.E.1    Pollard, T.D.2
  • 13
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments
    • L. Blanchoin, and T.D. Pollard Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments J. Biol. Chem. 274 1999 15538 15546
    • (1999) J. Biol. Chem. , vol.274 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 14
    • 0034687235 scopus 로고    scopus 로고
    • Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks
    • L. Blanchoin, T.D. Pollard, and R.D. Mullins Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks Curr. Biol. 10 2000 1273 1282
    • (2000) Curr. Biol. , vol.10 , pp. 1273-1282
    • Blanchoin, L.1    Pollard, T.D.2    Mullins, R.D.3
  • 15
    • 0037080339 scopus 로고    scopus 로고
    • Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin
    • L. Blanchoin, and T.D. Pollard Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin Biochemistry 41 2002 597 602
    • (2002) Biochemistry , vol.41 , pp. 597-602
    • Blanchoin, L.1    Pollard, T.D.2
  • 16
    • 0022876860 scopus 로고
    • Direct evidence for ADP-Pi-F-actin as the major intermediate in ATP-actin polymerization. Rate of dissociation of Pi from actin filaments
    • M.F. Carlier, and D. Pantaloni Direct evidence for ADP-Pi-F-actin as the major intermediate in ATP-actin polymerization. Rate of dissociation of Pi from actin filaments Biochemistry 25 1986 7789 7792
    • (1986) Biochemistry , vol.25 , pp. 7789-7792
    • Carlier, M.F.1    Pantaloni, D.2
  • 17
    • 0029661920 scopus 로고    scopus 로고
    • Continuous monitoring of Pi release after nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay
    • R. Melki, S. Fievez, and M.-F. Carlier Continuous monitoring of Pi release after nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay Biochemistry 35 1996 12038 12045
    • (1996) Biochemistry , vol.35 , pp. 12038-12045
    • Melki, R.1    Fievez, S.2    Carlier, M.-F.3
  • 18
    • 84856295948 scopus 로고    scopus 로고
    • Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin
    • A. Jégou, and T. Niedermayer G. Romet-Lemonne Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin PLoS Biol. 9 2011 e1001161
    • (2011) PLoS Biol. , vol.9 , pp. 1001161
    • Jégou, A.1    Niedermayer, T.2    Romet-Lemonne, G.3
  • 19
    • 41549124089 scopus 로고    scopus 로고
    • WASP family members and formin proteins coordinate regulation of cell protrusions in carcinoma cells
    • C. Sarmiento, and W. Wang J. Condeelis WASP family members and formin proteins coordinate regulation of cell protrusions in carcinoma cells J. Cell Biol. 180 2008 1245 1260
    • (2008) J. Cell Biol. , vol.180 , pp. 1245-1260
    • Sarmiento, C.1    Wang, W.2    Condeelis, J.3
  • 20
    • 41949088527 scopus 로고    scopus 로고
    • Arp2/3 complex interactions and actin network turnover in lamellipodia
    • F.P. Lai, and M. Szczodrak K. Rottner Arp2/3 complex interactions and actin network turnover in lamellipodia EMBO J. 27 2008 982 992
    • (2008) EMBO J. , vol.27 , pp. 982-992
    • Lai, F.P.1    Szczodrak, M.2    Rottner, K.3
  • 22
    • 0036900955 scopus 로고    scopus 로고
    • ADF/cofilin and actin dynamics in disease
    • J.R. Bamburg, and O.P. Wiggan ADF/cofilin and actin dynamics in disease Trends Cell Biol. 12 2002 598 605
    • (2002) Trends Cell Biol. , vol.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 24
    • 4444296491 scopus 로고    scopus 로고
    • Phospholipase C and cofilin are required for carcinoma cell directionality in response to EGF stimulation
    • G. Mouneimne, and L. Soon J. Condeelis Phospholipase C and cofilin are required for carcinoma cell directionality in response to EGF stimulation J. Cell Biol. 166 2004 697 708
    • (2004) J. Cell Biol. , vol.166 , pp. 697-708
    • Mouneimne, G.1    Soon, L.2    Condeelis, J.3
  • 25
    • 1642391823 scopus 로고    scopus 로고
    • Formin-induced nucleation of actin filaments
    • S.H. Zigmond Formin-induced nucleation of actin filaments Curr. Opin. Cell Biol. 16 2004 99 105
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 99-105
    • Zigmond, S.H.1
  • 26
    • 33745608331 scopus 로고    scopus 로고
    • Polarization and movement of keratocytes: A multiscale modeling approach
    • A.F. Marée, and A. Jilkine L. Edelstein-Keshet Polarization and movement of keratocytes: a multiscale modeling approach Bull. Math. Biol. 68 2006 1169 1211
    • (2006) Bull. Math. Biol. , vol.68 , pp. 1169-1211
    • Marée, A.F.1    Jilkine, A.2    Edelstein-Keshet, L.3
  • 27
    • 34548475260 scopus 로고    scopus 로고
    • Emergence of large-scale cell morphology and movement from local actin filament growth dynamics
    • C.I. Lacayo, and Z. Pincus J.A. Theriot Emergence of large-scale cell morphology and movement from local actin filament growth dynamics PLoS Biol. 5 2007 e233
    • (2007) PLoS Biol. , vol.5 , pp. 233
    • Lacayo, C.I.1    Pincus, Z.2    Theriot, J.A.3
  • 28
    • 79959729826 scopus 로고    scopus 로고
    • A temporal model of cofilin regulation and the early peak of actin barbed ends in invasive tumor cells
    • N. Tania, and E. Prosk L. Edelstein-Keshet A temporal model of cofilin regulation and the early peak of actin barbed ends in invasive tumor cells Biophys. J. 100 2011 1883 1892
    • (2011) Biophys. J. , vol.100 , pp. 1883-1892
    • Tania, N.1    Prosk, E.2    Edelstein-Keshet, L.3
  • 29
    • 77952196594 scopus 로고    scopus 로고
    • The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament
    • E.M. De La Cruz, and D. Sept The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament Biophys. J. 98 2010 1893 1901
    • (2010) Biophys. J. , vol.98 , pp. 1893-1901
    • De La Cruz, E.M.1    Sept, D.2
  • 30
    • 33747167610 scopus 로고    scopus 로고
    • Actin filament branching and protrusion velocity in a simple 1D model of a motile cell
    • A.T. Dawes, and G. Bard Ermentrout L. Edelstein-Keshet Actin filament branching and protrusion velocity in a simple 1D model of a motile cell J. Theor. Biol. 242 2006 265 279
    • (2006) J. Theor. Biol. , vol.242 , pp. 265-279
    • Dawes, A.T.1    Bard Ermentrout, G.2    Edelstein-Keshet, L.3
  • 31
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • A. Mogilner, and G. Oster Cell motility driven by actin polymerization Biophys. J. 71 1996 3030 3045
    • (1996) Biophys. J. , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 32
    • 84883405308 scopus 로고    scopus 로고
    • Spatial regulation of RhoC activity defines protrusion formation in migrating cells
    • J.J. Bravo-Cordero, and V.P. Sharma L. Hodgson Spatial regulation of RhoC activity defines protrusion formation in migrating cells J. Cell Sci. 126 2013 3356 3369
    • (2013) J. Cell Sci. , vol.126 , pp. 3356-3369
    • Bravo-Cordero, J.J.1    Sharma, V.P.2    Hodgson, L.3
  • 33
    • 65249141705 scopus 로고    scopus 로고
    • A common cofilin activity cycle in invasive tumor cells and inflammatory cells
    • J. van Rheenen, J. Condeelis, and M. Glogauer A common cofilin activity cycle in invasive tumor cells and inflammatory cells J. Cell Sci. 122 2009 305 311
    • (2009) J. Cell Sci. , vol.122 , pp. 305-311
    • Van Rheenen, J.1    Condeelis, J.2    Glogauer, M.3
  • 34
    • 2642579936 scopus 로고    scopus 로고
    • Signaling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein) family proteins and the Arp2/3 complex
    • T.H. Millard, S.J. Sharp, and L.M. Machesky Signaling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein) family proteins and the Arp2/3 complex Biochem. J. 380 2004 1 17
    • (2004) Biochem. J. , vol.380 , pp. 1-17
    • Millard, T.H.1    Sharp, S.J.2    Machesky, L.M.3
  • 35
    • 34948908535 scopus 로고    scopus 로고
    • Cdc42 is required for EGF-stimulated protrusion and motility in MTLn3 carcinoma cells
    • M. El-Sibai, and P. Nalbant J.M. Backer Cdc42 is required for EGF-stimulated protrusion and motility in MTLn3 carcinoma cells J. Cell Sci. 120 2007 3465 3474
    • (2007) J. Cell Sci. , vol.120 , pp. 3465-3474
    • El-Sibai, M.1    Nalbant, P.2    Backer, J.M.3
  • 36
    • 0036912348 scopus 로고    scopus 로고
    • Spatial regulation of actin dynamics: A tropomyosin-free, actin-rich compartment at the leading edge
    • V. DesMarais, and I. Ichetovkin S.E. Hitchcock-DeGregori Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge J. Cell Sci. 115 2002 4649 4660
    • (2002) J. Cell Sci. , vol.115 , pp. 4649-4660
    • Desmarais, V.1    Ichetovkin, I.2    Hitchcock-Degregori, S.E.3
  • 37
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • S. Ono, and K. Ono Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics J. Cell Biol. 156 2002 1065 1076
    • (2002) J. Cell Biol. , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 38
    • 80051977000 scopus 로고    scopus 로고
    • Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASP-VCA on Arp2/3 complex
    • S.C. Ti, and C.T. Jurgenson T.D. Pollard Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASP-VCA on Arp2/3 complex Proc. Natl. Acad. Sci. USA 108 2011 E463 E471
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108
    • Ti, S.C.1    Jurgenson, C.T.2    Pollard, T.D.3
  • 39
    • 33646167587 scopus 로고    scopus 로고
    • Stimulation of actin polymerization by filament severing
    • A.E. Carlsson Stimulation of actin polymerization by filament severing Biophys. J. 90 2006 413 422
    • (2006) Biophys. J. , vol.90 , pp. 413-422
    • Carlsson, A.E.1
  • 40
    • 64049091643 scopus 로고    scopus 로고
    • Cofilin dissociates Arp2/3 complex and branches from actin filaments
    • C. Chan, C.C. Beltzner, and T.D. Pollard Cofilin dissociates Arp2/3 complex and branches from actin filaments Curr. Biol. 19 2009 537 545
    • (2009) Curr. Biol. , vol.19 , pp. 537-545
    • Chan, C.1    Beltzner, C.C.2    Pollard, T.D.3
  • 41
    • 79251549180 scopus 로고    scopus 로고
    • Robust organizational principles of protrusive biopolymer networks in migrating living cells
    • B. Stuhrmann, F. Huber, and J. Käs Robust organizational principles of protrusive biopolymer networks in migrating living cells PLoS ONE 6 2011 e14471
    • (2011) PLoS ONE , vol.6 , pp. 14471
    • Stuhrmann, B.1    Huber, F.2    Käs, J.3
  • 42
    • 0035928737 scopus 로고    scopus 로고
    • Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin
    • L. Blanchoin, T.D. Pollard, and S.E. Hitchcock-DeGregori Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin Curr. Biol. 11 2001 1300 1304
    • (2001) Curr. Biol. , vol.11 , pp. 1300-1304
    • Blanchoin, L.1    Pollard, T.D.2    Hitchcock-Degregori, S.E.3
  • 43
    • 0037031320 scopus 로고    scopus 로고
    • Actin dynamics: Tropomyosin provides stability
    • J.A. Cooper Actin dynamics: tropomyosin provides stability Curr. Biol. 12 2002 R523 R525
    • (2002) Curr. Biol. , vol.12
    • Cooper, J.A.1
  • 44
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • M.-F. Carlier, and V. Laurent D. Pantaloni Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility J. Cell Biol. 136 1997 1307 1322
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.-F.1    Laurent, V.2    Pantaloni, D.3
  • 45
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • J.R. Bamburg Proteins of the ADF/cofilin family: essential regulators of actin dynamics Annu. Rev. Cell Dev. Biol. 15 1999 185 230
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 47
    • 21844458415 scopus 로고    scopus 로고
    • Multiscale two-dimensional modeling of a motile simple-shaped cell
    • B. Rubinstein, K. Jacobson, and A. Mogilner Multiscale two-dimensional modeling of a motile simple-shaped cell Multiscale Model Simul 3 2005 413 439
    • (2005) Multiscale Model Simul , vol.3 , pp. 413-439
    • Rubinstein, B.1    Jacobson, K.2    Mogilner, A.3
  • 48
    • 84871395592 scopus 로고    scopus 로고
    • F-actin buckling coordinates contractility and severing in a biomimetic actomyosin cortex
    • M.P. Murrell, and M.L. Gardel F-actin buckling coordinates contractility and severing in a biomimetic actomyosin cortex Proc. Natl. Acad. Sci. USA 109 2012 20820 20825
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 20820-20825
    • Murrell, M.P.1    Gardel, M.L.2
  • 49
    • 44049093878 scopus 로고    scopus 로고
    • Stochastic severing of actin filaments by actin depolymerizing factor/cofilin controls the emergence of a steady dynamical regime
    • J. Roland, and J. Berro J.-L. Martiel Stochastic severing of actin filaments by actin depolymerizing factor/cofilin controls the emergence of a steady dynamical regime Biophys. J. 94 2008 2082 2094
    • (2008) Biophys. J. , vol.94 , pp. 2082-2094
    • Roland, J.1    Berro, J.2    Martiel, J.-L.3
  • 50
    • 80052476842 scopus 로고    scopus 로고
    • Cofilin-linked changes in actin filament flexibility promote severing
    • B.R. McCullough, and E.E. Grintsevich E.M. De La Cruz Cofilin-linked changes in actin filament flexibility promote severing Biophys. J. 101 2011 151 159
    • (2011) Biophys. J. , vol.101 , pp. 151-159
    • McCullough, B.R.1    Grintsevich, E.E.2    De La Cruz, E.M.3
  • 51
    • 79957453658 scopus 로고    scopus 로고
    • Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries
    • C. Suarez, and J. Roland L. Blanchoin Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries Curr. Biol. 21 2011 862 868
    • (2011) Curr. Biol. , vol.21 , pp. 862-868
    • Suarez, C.1    Roland, J.2    Blanchoin, L.3
  • 52
    • 0032558437 scopus 로고    scopus 로고
    • Kinetic studies on the effect of yeast cofilin on yeast actin polymerization
    • J. Du, and C. Frieden Kinetic studies on the effect of yeast cofilin on yeast actin polymerization Biochemistry 37 1998 13276 13284
    • (1998) Biochemistry , vol.37 , pp. 13276-13284
    • Du, J.1    Frieden, C.2
  • 53
    • 48249121534 scopus 로고    scopus 로고
    • Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers
    • H.Y. Kueh, and G.T. Charras W.M. Brieher Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers J. Cell Biol. 182 2008 341 353
    • (2008) J. Cell Biol. , vol.182 , pp. 341-353
    • Kueh, H.Y.1    Charras, G.T.2    Brieher, W.M.3
  • 54
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • E. Andrianantoandro, and T.D. Pollard Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin Mol. Cell 24 2006 13 23
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 55
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • T.M. Svitkina, and G.G. Borisy Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia J. Cell Biol. 145 1999 1009 1026
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 56
    • 0034695421 scopus 로고    scopus 로고
    • Polymerization and structure of nucleotide-free actin filaments
    • E.M. De La Cruz, and A. Mandinova T.D. Pollard Polymerization and structure of nucleotide-free actin filaments J. Mol. Biol. 295 2000 517 526
    • (2000) J. Mol. Biol. , vol.295 , pp. 517-526
    • De La Cruz, E.M.1    Mandinova, A.2    Pollard, T.D.3
  • 57
    • 0021749110 scopus 로고
    • Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • E. Nishida, S. Maekawa, and H. Sakai Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin Biochemistry 23 1984 5307 5313
    • (1984) Biochemistry , vol.23 , pp. 5307-5313
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 58
    • 0032819362 scopus 로고    scopus 로고
    • The actin-based nanomachine at the leading edge of migrating cells
    • V.C. Abraham, and V. Krishnamurthi F. Lanni The actin-based nanomachine at the leading edge of migrating cells Biophys. J. 77 1999 1721 1732
    • (1999) Biophys. J. , vol.77 , pp. 1721-1732
    • Abraham, V.C.1    Krishnamurthi, V.2    Lanni, F.3
  • 59
    • 0023782867 scopus 로고
    • Rate of binding of tropomyosin to actin filaments
    • A. Wegner, and K. Ruhnau Rate of binding of tropomyosin to actin filaments Biochemistry 27 1988 6994 7000
    • (1988) Biochemistry , vol.27 , pp. 6994-7000
    • Wegner, A.1    Ruhnau, K.2


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