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Volumn 68, Issue 5, 2011, Pages 259-265

Self-regulative organization of the cytoskeleton

Author keywords

Actin; Emergent behavior; Microtubules; Self assembly; Self organization

Indexed keywords

ACTIN;

EID: 79955992225     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.20509     Document Type: Short Survey
Times cited : (11)

References (52)
  • 1
    • 41149156427 scopus 로고    scopus 로고
    • Tracking the ends: a dynamic protein network controls the fate of microtubule tips
    • Akhmanova A, Steinmetz, MO. 2008. Tracking the ends: a dynamic protein network controls the fate of microtubule tips. Nat Rev Mol Cell Biol 9: 309-322.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 309-322
    • Akhmanova, A.1    Steinmetz, M.O.2
  • 2
    • 27744590494 scopus 로고    scopus 로고
    • Morphology of the lamellipodium and organization of actin filaments at the leading edge of crawling cells
    • Atilgan E, Wirtz D, Sun SX. 2005. Morphology of the lamellipodium and organization of actin filaments at the leading edge of crawling cells. Biophys J 89: 3589-3602.
    • (2005) Biophys J , vol.89 , pp. 3589-3602
    • Atilgan, E.1    Wirtz, D.2    Sun, S.X.3
  • 3
    • 78649373184 scopus 로고    scopus 로고
    • Roles of ADF/cofilin in actin polymerization and beyond. F1000
    • Bamburg JR, Bernstein BW. 2010. Roles of ADF/cofilin in actin polymerization and beyond. F1000 Biol Rep 2: 62.
    • (2010) Biol Rep , vol.2 , pp. 62
    • Bamburg, J.R.1    Bernstein, B.W.2
  • 5
    • 77950859278 scopus 로고    scopus 로고
    • ADF/Cofilin: a functional node in cell biology
    • Bernstein BW, Bamburg JR. 2010. ADF/Cofilin: a functional node in cell biology. Trends Cell Biol 20: 187-195.
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 6
    • 33750365532 scopus 로고    scopus 로고
    • Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1
    • Brieher WM, Kueh HY, Ballif BA, Mitchison TJ. 2006. Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1. J Cell Biol 175: 315-324.
    • (2006) J Cell Biol , vol.175 , pp. 315-324
    • Brieher, W.M.1    Kueh, H.Y.2    Ballif, B.A.3    Mitchison, T.J.4
  • 7
    • 77952896939 scopus 로고    scopus 로고
    • Control of actin filament treadmilling in cell motility
    • Bugyi B, Carlier M. 2010. Control of actin filament treadmilling in cell motility. Annu Rev Biophys 39: 449-470.
    • (2010) Annu Rev Biophys , vol.39 , pp. 449-470
    • Bugyi, B.1    Carlier, M.2
  • 9
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/Cofilin) enhances the rate of filament turnover: implication in actin-based motility
    • Carlier M, Laurent V, Santolini J, Melki R, Didry D, Xia GX, Hong Y, Chua NH, 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.
    • (1997) J Cell Biol , vol.136 , pp. 1307-1323
    • Carlier, M.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
  • 10
    • 0033607682 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier M, Ressad F, Pantaloni D. 1999. Control of actin dynamics in cell motility. J Biol Chem 274: 33827-33830.
    • (1999) J Biol Chem , vol.274 , pp. 33827-33830
    • Carlier, M.1    Ressad, F.2    Pantaloni, D.3
  • 11
    • 51049117096 scopus 로고    scopus 로고
    • Model of reduction of actin polymerization forces by ATP hydrolysis
    • Carlsson AE. 2008. Model of reduction of actin polymerization forces by ATP hydrolysis. Phys Biol 5: 36002.
    • (2008) Phys Biol , vol.5 , pp. 36002
    • Carlsson, A.E.1
  • 12
    • 58149230940 scopus 로고    scopus 로고
    • Traction dynamics of filopodia on compliant substrates
    • Chan CE, Odde DJ. 2008. Traction dynamics of filopodia on compliant substrates. Science 322: 1687-1691.
    • (2008) Science , vol.322 , pp. 1687-1691
    • Chan, C.E.1    Odde, D.J.2
  • 13
    • 77957834345 scopus 로고    scopus 로고
    • Differential regulation of unconventional fission yeast myosins via the actin track
    • Clayton JE, Sammons MR, Stark BC, Hodges AR, Lord M. 2010. Differential regulation of unconventional fission yeast myosins via the actin track. Curr Biol 20: 1423-1431.
    • (2010) Curr Biol , vol.20 , pp. 1423-1431
    • Clayton, J.E.1    Sammons, M.R.2    Stark, B.C.3    Hodges, A.R.4    Lord, M.5
  • 14
    • 12544252575 scopus 로고    scopus 로고
    • Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions
    • De La Cruz EM. 2005. Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions. J Mol Biol 346: 557-564.
    • (2005) J Mol Biol , vol.346 , pp. 557-564
    • De La Cruz, E.M.1
  • 15
    • 77952196594 scopus 로고    scopus 로고
    • The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament
    • De La Cruz EM, Sept D. 2010. The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament. Biophys J 98: 1893-1901.
    • (2010) Biophys J , vol.98 , pp. 1893-1901
    • De La Cruz, E.M.1    Sept, D.2
  • 16
    • 33846942073 scopus 로고    scopus 로고
    • Emergence: The Hole at the Wheel's Hub
    • Clayton P, Davies P, editors. Oxford, UK: Oxford University Press. Chapter 5;
    • Deacon TW. 2006. Emergence: The Hole at the Wheel's Hub. In: Clayton P, Davies P, editors. The Re-emergence of Emergence. Oxford, UK: Oxford University Press. Chapter 5; pp 111-150. [http://www.worldcat.org/oclc/65425759].
    • (2006) The Re-emergence of Emergence , pp. 111-150
    • Deacon, T.W.1
  • 18
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis RJ. 2001. Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 26: 597-604.
    • (2001) Trends Biochem Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 19
    • 33847773123 scopus 로고    scopus 로고
    • Direct measurement of force generation by actin filament polymerization using an optical trap
    • Footer MJ, Kerssemakers JWJ, Theriot JA, Dogterom M. 2007. Direct measurement of force generation by actin filament polymerization using an optical trap. Proc Natl Acad Sci USA 104: 2181-2186.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2181-2186
    • Footer, M.J.1    Kerssemakers, J.W.J.2    Theriot, J.A.3    Dogterom, M.4
  • 20
    • 42249107315 scopus 로고    scopus 로고
    • Effects of solution crowding on Actin polymerization reveal the energetic basis for nucleotide-dependent filament stability
    • Frederick KB, Sept D, de La Cruz EM. 2008. Effects of solution crowding on Actin polymerization reveal the energetic basis for nucleotide-dependent filament stability. J Mol Biol 378: 540-550.
    • (2008) J Mol Biol , vol.378 , pp. 540-550
    • Frederick, K.B.1    Sept, D.2    de La Cruz, E.M.3
  • 21
    • 65549103882 scopus 로고    scopus 로고
    • Coronin switches roles in actin disassembly depending on the nucleotide state of actin
    • Gandhi M, Achard V, Blanchoin L, Goode BL. 2009. Coronin switches roles in actin disassembly depending on the nucleotide state of actin. Mol Cell 34: 364-374.
    • (2009) Mol Cell , vol.34 , pp. 364-374
    • Gandhi, M.1    Achard, V.2    Blanchoin, L.3    Goode, B.L.4
  • 22
    • 20444398071 scopus 로고    scopus 로고
    • Tropomyosin isoforms: divining rods for actin cytoskeleton function
    • Gunning PW, Schevzov G, Kee AJ, Hardeman EC. 2005. Tropomyosin isoforms: divining rods for actin cytoskeleton function. Trends Cell Biol 15: 333-341.
    • (2005) Trends Cell Biol , vol.15 , pp. 333-341
    • Gunning, P.W.1    Schevzov, G.2    Kee, A.J.3    Hardeman, E.C.4
  • 23
    • 39149121834 scopus 로고    scopus 로고
    • Tubulin modifications and their cellular functions
    • Hammond JW, Cai D, Verhey KJ. 2008. Tubulin modifications and their cellular functions. Curr Opin Cell Biol 20: 71-76.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 71-76
    • Hammond, J.W.1    Cai, D.2    Verhey, K.J.3
  • 24
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman SJ, Ridley AJ. 2008. Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat Rev Mol Cell Biol 9: 690-701.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 25
    • 4544297320 scopus 로고    scopus 로고
    • Crowding-induced organization in cells: spontaneous alignment and sorting of filaments with physiological control points
    • Herzfeld J. 2004. Crowding-induced organization in cells: spontaneous alignment and sorting of filaments with physiological control points. J Mol Recognit 17: 376-381.
    • (2004) J Mol Recognit , vol.17 , pp. 376-381
    • Herzfeld, J.1
  • 26
    • 67650309799 scopus 로고    scopus 로고
    • Mechanical signaling in networks of motor and cytoskeletal proteins
    • Howard J. 2009. Mechanical signaling in networks of motor and cytoskeletal proteins. Annu Rev Biophys 38: 217-234.
    • (2009) Annu Rev Biophys , vol.38 , pp. 217-234
    • Howard, J.1
  • 27
    • 58749099628 scopus 로고    scopus 로고
    • Growing actin networks form lamellipodium and lamellum by self-assembly
    • Huber F, Käs J, Stuhrmann B. 2008. Growing actin networks form lamellipodium and lamellum by self-assembly. Biophys J 95: 5508-5523.
    • (2008) Biophys J , vol.95 , pp. 5508-5523
    • Huber, F.1    Käs, J.2    Stuhrmann, B.3
  • 29
    • 0037477845 scopus 로고    scopus 로고
    • Dynamic instability of microtubules is regulated by force
    • Janson M, de Dood M, Dogter M. 2003. Dynamic instability of microtubules is regulated by force. JCB 161: 1029-1034.
    • (2003) JCB , vol.161 , pp. 1029-1034
    • Janson, M.1    de Dood, M.2    Dogter, M.3
  • 30
    • 33644609311 scopus 로고    scopus 로고
    • Self-organization versus Watchmaker: Molecular motors and protein translocation
    • Kurakin A. 2006. Self-organization versus Watchmaker: Molecular motors and protein translocation. Biosystems 84: 15-23.
    • (2006) Biosystems , vol.84 , pp. 15-23
    • Kurakin, A.1
  • 31
    • 44449097488 scopus 로고    scopus 로고
    • On the Rho'd: The regulation of membrane protrusions by Rho-GTPases
    • Ladwein M, Rottner K. 2008. On the Rho'd: The regulation of membrane protrusions by Rho-GTPases. FEBS Lett 582: 2066-2074.
    • (2008) FEBS Lett , vol.582 , pp. 2066-2074
    • Ladwein, M.1    Rottner, K.2
  • 32
    • 35248826540 scopus 로고    scopus 로고
    • Cross-linker unbinding and self-similarity in bundled cytoskeletal networks
    • Lieleg O, Bausch AR. 2007. Cross-linker unbinding and self-similarity in bundled cytoskeletal networks. Phys Rev Lett 99: 158105.
    • (2007) Phys Rev Lett , vol.99 , pp. 158105
    • Lieleg, O.1    Bausch, A.R.2
  • 34
    • 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. 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.4
  • 35
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough A, Pope B, Chiu W, Weeds A. 1997. Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function. J Cell Biol 138: 771-781.
    • (1997) J Cell Biol , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 36
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T, Kirschner M. 1984. Dynamic instability of microtubule growth. Nature 312: 237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 37
    • 42449124179 scopus 로고    scopus 로고
    • Tug-of-war as a cooperative mechanism for bidirectional cargo transport by molecular motors
    • Müller MJI, Klumpp S, Lipowsky R. 2008. Tug-of-war as a cooperative mechanism for bidirectional cargo transport by molecular motors. Proc Natl Acad Sci 105: 4609-4614.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 4609-4614
    • Müller, M.J.I.1    Klumpp, S.2    Lipowsky, R.3
  • 38
    • 0033884332 scopus 로고    scopus 로고
    • Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties
    • Nishizaka T, Seo R, Tadakuma H, Kinosita K, Ishiwata S. 2000. Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties. Biophys J 79: 962-974.
    • (2000) Biophys J , vol.79 , pp. 962-974
    • Nishizaka, T.1    Seo, R.2    Tadakuma, H.3    Kinosita, K.4    Ishiwata, S.5
  • 39
    • 2942557125 scopus 로고    scopus 로고
    • Dynamic microtubules lead the way for spindle positioning
    • Pearson CG, Bloom K. 2004. Dynamic microtubules lead the way for spindle positioning. Nat Rev Mol Cell Biol 5: 481-492.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 481-492
    • Pearson, C.G.1    Bloom, K.2
  • 40
    • 0027194759 scopus 로고
    • Cellular motions and thermal fluctuations: The Brownian Ratchet
    • Peskin CS, Odell GM, Oster GF. 1993. Cellular motions and thermal fluctuations: The Brownian Ratchet Biophys J 65: 316-324.
    • (1993) Biophys J , vol.65 , pp. 316-324
    • Peskin, C.S.1    Odell, G.M.2    Oster, G.F.3
  • 42
    • 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
  • 45
    • 78651368473 scopus 로고    scopus 로고
    • Structural reorganization of parallel actin bundles by crosslinking proteins: Incommensurate states of twist
    • Shin H, Grason GM. 2010. Structural reorganization of parallel actin bundles by crosslinking proteins: Incommensurate states of twist. Phys Rev E 82: 51919.
    • (2010) Phys Rev E , vol.82 , pp. 51919
    • Shin, H.1    Grason, G.M.2
  • 46
    • 77957850795 scopus 로고    scopus 로고
    • Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast
    • Skau CT, Kovar DR. 2010. Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast. Curr Biol 20: 1415-1422.
    • (2010) Curr Biol , vol.20 , pp. 1415-1422
    • Skau, C.T.1    Kovar, D.R.2
  • 47
    • 79251549180 scopus 로고    scopus 로고
    • Robust organizational principles of protrusive biopolymer networks in migrating living cells
    • Stuhrmann B, Huber F, Käs J. 2011. Robust organizational principles of protrusive biopolymer networks in migrating living cells. PLoS ONE 6: e14471.
    • (2011) PLoS ONE , vol.6
    • Stuhrmann, B.1    Huber, F.2    Käs, J.3
  • 48
    • 77953046399 scopus 로고    scopus 로고
    • Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts
    • Sudo H, Baas, PW. 2010. Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts. J Neurosci 30: 7215-7226.
    • (2010) J Neurosci , vol.30 , pp. 7215-7226
    • Sudo, H.1    Baas, P.W.2
  • 49
    • 0342903325 scopus 로고    scopus 로고
    • Physical properties determining self-organization of motors and microtubules
    • Surrey T, Nedelec F, Leibler S, Karsenti E. 2001. Physical properties determining self-organization of motors and microtubules. Science 292: 1167-1171.
    • (2001) Science , vol.292 , pp. 1167-1171
    • Surrey, T.1    Nedelec, F.2    Leibler, S.3    Karsenti, E.4
  • 50
    • 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
  • 52
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • Veigel C, Schmitz S, Wang F, Sellers JR. 2005. Load-dependent kinetics of myosin-V can explain its high processivity. Nat Cell Biol 7: 861-869.
    • (2005) Nat Cell Biol , vol.7 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4


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