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Volumn 7, Issue 7, 2011, Pages

The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation

Author keywords

[No Author keywords available]

Indexed keywords

COARSE-GRAINED MODELING; ORDINARY DIFFERENTIAL EQUATIONS; SIGNALING; STOCHASTIC MODELS; STOCHASTIC SYSTEMS;

EID: 79960948489     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002088     Document Type: Article
Times cited : (53)

References (49)
  • 1
    • 44349179335 scopus 로고    scopus 로고
    • Filopodia: molecular architecture and cellular functions
    • Mattila PK, Lappalainen P, (2008) Filopodia: molecular architecture and cellular functions. Nat Rev Mol Cell Biol 9: 446-454.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 446-454
    • Mattila, P.K.1    Lappalainen, P.2
  • 2
    • 23244441861 scopus 로고    scopus 로고
    • The physics of filopodial protrusion
    • Mogilner A, Rubinstein B, (2005) The physics of filopodial protrusion. Biophys J 89: 782-795.
    • (2005) Biophys J , vol.89 , pp. 782-795
    • Mogilner, A.1    Rubinstein, B.2
  • 3
    • 1842453175 scopus 로고    scopus 로고
    • Critical role of Ena/VASP proteins for filopodia formation in neurons and in function downstream of netrin-1
    • Lebrand C, Dent EW, Strasser GA, Lanier LM, Krause M, et al. (2004) Critical role of Ena/VASP proteins for filopodia formation in neurons and in function downstream of netrin-1. Neuron 42: 37-49.
    • (2004) Neuron , vol.42 , pp. 37-49
    • Lebrand, C.1    Dent, E.W.2    Strasser, G.A.3    Lanier, L.M.4    Krause, M.5
  • 4
    • 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. EMBO J 27: 2943-2954.
    • (2008) EMBO J , vol.27 , pp. 2943-2954
    • Breitsprecher, D.1    Kiesewetter, A.K.2    Linkner, J.3    Urbanke, C.4    Resch, G.P.5
  • 5
    • 44349090393 scopus 로고    scopus 로고
    • Ena/VASP proteins capture actin filament barbed ends
    • Pasic L, Kotova T, Schafer DA, (2008) Ena/VASP proteins capture actin filament barbed ends. J Biol Chem 283: 9814-9819.
    • (2008) J Biol Chem , vol.283 , pp. 9814-9819
    • Pasic, L.1    Kotova, T.2    Schafer, D.A.3
  • 7
    • 78049521359 scopus 로고    scopus 로고
    • VASP is a processive actin polymerase that requires monomeric actin for barbed end association
    • Hansen SD, Mullins RD, (2010) VASP is a processive actin polymerase that requires monomeric actin for barbed end association. J Cell Biol 191: 571-584.
    • (2010) J Cell Biol , vol.191 , pp. 571-584
    • Hansen, S.D.1    Mullins, R.D.2
  • 9
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end
    • Mejillano MR, Kojima S, 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.2    Applewhite, D.A.3    Gertler, F.B.4    Svitkina, T.M.5
  • 10
    • 10344251483 scopus 로고    scopus 로고
    • Eps8 controls actin-based motility by capping the barbed ends of actin filaments
    • Disanza A, Carlier MF, Stradal TE, Didry D, Frittoli E, et al. (2004) Eps8 controls actin-based motility by capping the barbed ends of actin filaments. Nat Cell Biol 6: 1180-1188.
    • (2004) Nat Cell Biol , vol.6 , pp. 1180-1188
    • Disanza, A.1    Carlier, M.F.2    Stradal, T.E.3    Didry, D.4    Frittoli, E.5
  • 11
    • 0033197996 scopus 로고    scopus 로고
    • The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses
    • Abbott MA, Wells DG, Fallon JR, (1999) The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses. J Neurosci 19: 7300-7308.
    • (1999) J Neurosci , vol.19 , pp. 7300-7308
    • Abbott, M.A.1    Wells, D.G.2    Fallon, J.R.3
  • 12
    • 33751543109 scopus 로고    scopus 로고
    • Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex
    • Disanza A, Mantoani S, Hertzog M, Gerboth S, Frittoli E, et al. (2006) Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex. Nat Cell Biol 8: 1337-1347.
    • (2006) Nat Cell Biol , vol.8 , pp. 1337-1347
    • Disanza, A.1    Mantoani, S.2    Hertzog, M.3    Gerboth, S.4    Frittoli, E.5
  • 13
    • 0032891376 scopus 로고    scopus 로고
    • Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1
    • Oda K, Shiratsuchi T, Nishimori H, Inazawa J, Yoshikawa H, et al. (1999) Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1. Cytogenet Cell Genet 84: 75-82.
    • (1999) Cytogenet Cell Genet , vol.84 , pp. 75-82
    • Oda, K.1    Shiratsuchi, T.2    Nishimori, H.3    Inazawa, J.4    Yoshikawa, H.5
  • 14
    • 0033113093 scopus 로고    scopus 로고
    • Cloning and characterization of cDNA for DRPLA interacting protein
    • Okamumoho Y, Yamada M, (1999) [Cloning and characterization of cDNA for DRPLA interacting protein]. Nippon Rinsho 57: 856-861.
    • (1999) Nippon Rinsho , vol.57 , pp. 856-861
    • Okamumoho, Y.1    Yamada, M.2
  • 15
    • 39149109271 scopus 로고    scopus 로고
    • IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions
    • Scita G, Confalonieri S, Lappalainen P, Suetsugu S, (2008) IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions. Trends Cell Biol 18: 52-60.
    • (2008) Trends Cell Biol , vol.18 , pp. 52-60
    • Scita, G.1    Confalonieri, S.2    Lappalainen, P.3    Suetsugu, S.4
  • 16
    • 67649935286 scopus 로고    scopus 로고
    • Eps8 regulates axonal filopodia in hippocampal neurons in response to brain-derived neurotrophic factor (BDNF)
    • Menna E, Disanza A, Cagnoli C, Schenk U, Gelsomino G, et al. (2009) Eps8 regulates axonal filopodia in hippocampal neurons in response to brain-derived neurotrophic factor (BDNF). PLoS Biol 7: e1000138.
    • (2009) PLoS Biol , vol.7
    • Menna, E.1    Disanza, A.2    Cagnoli, C.3    Schenk, U.4    Gelsomino, G.5
  • 18
    • 43849086657 scopus 로고    scopus 로고
    • The stochastic dynamics of filopodial growth
    • Lan Y, Papoian GA, (2008) The stochastic dynamics of filopodial growth. Biophys J 94: 3839-3852.
    • (2008) Biophys J , vol.94 , pp. 3839-3852
    • Lan, Y.1    Papoian, G.A.2
  • 19
    • 51049111874 scopus 로고    scopus 로고
    • Performance of a population of independent filaments in lamellipodial protrusion
    • Schaus TE, Borisy GG, (2008) Performance of a population of independent filaments in lamellipodial protrusion. Biophys J 95: 1393-1411.
    • (2008) Biophys J , vol.95 , pp. 1393-1411
    • Schaus, T.E.1    Borisy, G.G.2
  • 20
    • 33646164411 scopus 로고    scopus 로고
    • Mechanics and dynamics of actin-driven thin membrane protrusions
    • Atilgan E, Wirtz D, Sun SX, (2006) Mechanics and dynamics of actin-driven thin membrane protrusions. Biophys J 90: 65-76.
    • (2006) Biophys J , vol.90 , pp. 65-76
    • Atilgan, E.1    Wirtz, D.2    Sun, S.X.3
  • 21
    • 67650899090 scopus 로고    scopus 로고
    • Molecular noise of capping protein binding induces macroscopic instability in filopodial dynamics
    • Zhuravlev PI, Papoian GA, (2009) Molecular noise of capping protein binding induces macroscopic instability in filopodial dynamics. Proc Natl Acad Sci U S A 106: 11570-11575.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 11570-11575
    • Zhuravlev, P.I.1    Papoian, G.A.2
  • 22
    • 77951642746 scopus 로고    scopus 로고
    • Mechano-chemical feedbacks regulate actin mesh growth in lamellipodial protrusions
    • Hu L, Papoian GA, (2010) Mechano-chemical feedbacks regulate actin mesh growth in lamellipodial protrusions. Biophys J 98: 1375-1384.
    • (2010) Biophys J , vol.98 , pp. 1375-1384
    • Hu, L.1    Papoian, G.A.2
  • 23
    • 77951647952 scopus 로고    scopus 로고
    • Design of active transport must be highly intricate: a possible role of myosin and Ena/VASP for G-actin transport in filopodia
    • Zhuravlev PI, Der BS, Papoian GA, (2010) Design of active transport must be highly intricate: a possible role of myosin and Ena/VASP for G-actin transport in filopodia. Biophys J 98: 1439-1448.
    • (2010) Biophys J , vol.98 , pp. 1439-1448
    • Zhuravlev, P.I.1    Der, B.S.2    Papoian, G.A.3
  • 24
    • 0033895234 scopus 로고    scopus 로고
    • Molecular mechanisms controlling actin filament dynamics in nonmuscle cells
    • Pollard TD, Blanchoin L, Mullins RD, (2000) Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu Rev Biophys Biomol Struct 29: 545-576.
    • (2000) Annu Rev Biophys Biomol Struct , vol.29 , pp. 545-576
    • Pollard, T.D.1    Blanchoin, L.2    Mullins, R.D.3
  • 25
    • 0032475981 scopus 로고    scopus 로고
    • Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover
    • Didry D, Carlier MF, Pantaloni D, (1998) Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J Biol Chem 273: 25602-25611.
    • (1998) J Biol Chem , vol.273 , pp. 25602-25611
    • Didry, D.1    Carlier, M.F.2    Pantaloni, D.3
  • 26
    • 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.
    • (2002) Biophys J , vol.83 , pp. 1237-1258
    • Mogilner, A.1    Edelstein-Keshet, L.2
  • 27
    • 50349095873 scopus 로고    scopus 로고
    • Quantitative analysis of G-actin transport in motile cells
    • Novak IL, Slepchenko BM, Mogilner A, (2008) Quantitative analysis of G-actin transport in motile cells. Biophys J 95: 1627-1638.
    • (2008) Biophys J , vol.95 , pp. 1627-1638
    • Novak, I.L.1    Slepchenko, B.M.2    Mogilner, A.3
  • 28
    • 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
  • 29
    • 0032819362 scopus 로고    scopus 로고
    • The actin-based nanomachine at the leading edge of migrating cells
    • Abraham VC, Krishnamurthi V, Taylor DL, Lanni F, (1999) The actin-based nanomachine at the leading edge of migrating cells. Biophys J 77: 1721-1732.
    • (1999) Biophys J , vol.77 , pp. 1721-1732
    • Abraham, V.C.1    Krishnamurthi, V.2    Taylor, D.L.3    Lanni, F.4
  • 30
    • 33846781374 scopus 로고    scopus 로고
    • Phosphoinositides and Rho proteins spatially regulate actin polymerization to initiate and maintain directed movement in a one-dimensional model of a motile cell
    • Dawes AT, Edelstein-Keshet L, (2007) Phosphoinositides and Rho proteins spatially regulate actin polymerization to initiate and maintain directed movement in a one-dimensional model of a motile cell. Biophys J 92: 744-768.
    • (2007) Biophys J , vol.92 , pp. 744-768
    • Dawes, A.T.1    Edelstein-Keshet, L.2
  • 31
    • 0028882496 scopus 로고
    • Actin filament barbed-end capping activity in neutrophil lysates: the role of capping protein-beta 2
    • DiNubile MJ, Cassimeris L, Joyce M, Zigmond SH, (1995) Actin filament barbed-end capping activity in neutrophil lysates: the role of capping protein-beta 2. Mol Biol Cell 6: 1659-1671.
    • (1995) Mol Biol Cell , vol.6 , pp. 1659-1671
    • DiNubile, M.J.1    Cassimeris, L.2    Joyce, M.3    Zigmond, S.H.4
  • 32
    • 68949183227 scopus 로고    scopus 로고
    • Ena/VASP: towards resolving a pointed controversy at the barbed end
    • Bear JE, Gertler FB, (2009) Ena/VASP: towards resolving a pointed controversy at the barbed end. J Cell Sci 122: 1947-1953.
    • (2009) J Cell Sci , vol.122 , pp. 1947-1953
    • Bear, J.E.1    Gertler, F.B.2
  • 33
    • 34347395435 scopus 로고    scopus 로고
    • Ena/VASP proteins have an anti-capping independent function in filopodia formation
    • Applewhite DA, Barzik M, Kojima S, Svitkina TM, Gertler FB, et al. (2007) Ena/VASP proteins have an anti-capping independent function in filopodia formation. Mol Biol Cell 18: 2579-2591.
    • (2007) Mol Biol Cell , vol.18 , pp. 2579-2591
    • Applewhite, D.A.1    Barzik, M.2    Kojima, S.3    Svitkina, T.M.4    Gertler, F.B.5
  • 35
    • 42049089943 scopus 로고    scopus 로고
    • Relaxing the actin cytoskeleton for adhesion and movement with Ena/VASP
    • Trichet L, Sykes C, Plastino J, (2008) Relaxing the actin cytoskeleton for adhesion and movement with Ena/VASP. J Cell Biol 181: 19-25.
    • (2008) J Cell Biol , vol.181 , pp. 19-25
    • Trichet, L.1    Sykes, C.2    Plastino, J.3
  • 36
    • 0035975963 scopus 로고    scopus 로고
    • Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex
    • Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, et al. (2001) Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex. Curr Biol 11: 1645-1655.
    • (2001) Curr Biol , vol.11 , pp. 1645-1655
    • Krugmann, S.1    Jordens, I.2    Gevaert, K.3    Driessens, M.4    Vandekerckhove, J.5
  • 37
    • 2442458996 scopus 로고    scopus 로고
    • A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein
    • Yamagishi A, Masuda M, Ohki T, Onishi H, Mochizuki N, (2004) A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. J Biol Chem 279: 14929-14936.
    • (2004) J Biol Chem , vol.279 , pp. 14929-14936
    • Yamagishi, A.1    Masuda, M.2    Ohki, T.3    Onishi, H.4    Mochizuki, N.5
  • 38
    • 66249118393 scopus 로고    scopus 로고
    • Coordination of membrane and actin cytoskeleton dynamics during filopodia protrusion
    • Yang C, Hoelzle M, Disanza A, Scita G, Svitkina T, (2009) Coordination of membrane and actin cytoskeleton dynamics during filopodia protrusion. PLoS One 4: e5678.
    • (2009) PLoS One , vol.4
    • Yang, C.1    Hoelzle, M.2    Disanza, A.3    Scita, G.4    Svitkina, T.5
  • 39
    • 33244462037 scopus 로고    scopus 로고
    • Dynamics of membranes driven by actin polymerization
    • Gov NS, Gopinathan A, (2006) Dynamics of membranes driven by actin polymerization. Biophys J 90: 454-469.
    • (2006) Biophys J , vol.90 , pp. 454-469
    • Gov, N.S.1    Gopinathan, A.2
  • 40
    • 52649105443 scopus 로고    scopus 로고
    • Actin bundling: initiation mechanisms and kinetics
    • Kraikivski P, Slepchenko BM, Novak IL, (2008) Actin bundling: initiation mechanisms and kinetics. Phys Rev Lett 101: 128102.
    • (2008) Phys Rev Lett , vol.101 , pp. 128102
    • Kraikivski, P.1    Slepchenko, B.M.2    Novak, I.L.3
  • 41
    • 36849073141 scopus 로고    scopus 로고
    • Phase transitions of the coupled membrane-cytoskeleton modify cellular shape
    • Veksler A, Gov NS, (2007) Phase transitions of the coupled membrane-cytoskeleton modify cellular shape. Biophys J 93: 3798-3810.
    • (2007) Biophys J , vol.93 , pp. 3798-3810
    • Veksler, A.1    Gov, N.S.2
  • 42
    • 0035662567 scopus 로고    scopus 로고
    • Distribution, cellular localization, and postnatal development of VASP and Mena expression in mouse tissues
    • Gambaryan S, Hauser W, Kobsar A, Glazova M, Walter U, (2001) Distribution, cellular localization, and postnatal development of VASP and Mena expression in mouse tissues. Histochem Cell Biol 116: 535-543.
    • (2001) Histochem Cell Biol , vol.116 , pp. 535-543
    • Gambaryan, S.1    Hauser, W.2    Kobsar, A.3    Glazova, M.4    Walter, U.5
  • 43
    • 0037007130 scopus 로고    scopus 로고
    • Ena/VASP proteins regulate cortical neuronal positioning
    • Goh KL, Cai L, Cepko CL, Gertler FB, (2002) Ena/VASP proteins regulate cortical neuronal positioning. Curr Biol 12: 565-569.
    • (2002) Curr Biol , vol.12 , pp. 565-569
    • Goh, K.L.1    Cai, L.2    Cepko, C.L.3    Gertler, F.B.4
  • 45
    • 0033594081 scopus 로고    scopus 로고
    • Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes
    • Laurent V, Loisel TP, Harbeck B, Wehman A, Grobe L, et al. (1999) Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. J Cell Biol 144: 1245-1258.
    • (1999) J Cell Biol , vol.144 , pp. 1245-1258
    • Laurent, V.1    Loisel, T.P.2    Harbeck, B.3    Wehman, A.4    Grobe, L.5
  • 47
    • 0034705317 scopus 로고    scopus 로고
    • Negative regulation of fibroblast motility by Ena/VASP proteins
    • Bear JE, Loureiro JJ, Libova I, Fassler R, Wehland J, et al. (2000) Negative regulation of fibroblast motility by Ena/VASP proteins. Cell 101: 717-728.
    • (2000) Cell , vol.101 , pp. 717-728
    • Bear, J.E.1    Loureiro, J.J.2    Libova, I.3    Fassler, R.4    Wehland, J.5
  • 48
    • 2342483041 scopus 로고    scopus 로고
    • Abi1 is essential for the formation and activation of a WAVE2 signalling complex
    • Innocenti M, Zucconi A, Disanza A, Frittoli E, Areces LB, et al. (2004) Abi1 is essential for the formation and activation of a WAVE2 signalling complex. Nat Cell Biol 6: 319-327.
    • (2004) Nat Cell Biol , vol.6 , pp. 319-327
    • Innocenti, M.1    Zucconi, A.2    Disanza, A.3    Frittoli, E.4    Areces, L.B.5
  • 49
    • 32544443964 scopus 로고    scopus 로고
    • Systems Biology Toolbox for MATLAB: a computational platform for research in systems biology
    • Schmidt H, Jirstrand M, (2006) Systems Biology Toolbox for MATLAB: a computational platform for research in systems biology. Bioinformatics 22: 514-515.
    • (2006) Bioinformatics , vol.22 , pp. 514-515
    • Schmidt, H.1    Jirstrand, M.2


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