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Volumn 109, Issue 8, 2012, Pages 2913-2918

Actin filament curvature biases branching direction

Author keywords

Actin based motility; Autocatalytic branching; Bending fluctuations; Force sensing; Worm like chain

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX;

EID: 84857389419     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1114292109     Document Type: Article
Times cited : (149)

References (54)
  • 1
    • 79954528993 scopus 로고    scopus 로고
    • Mechanotransduction in development
    • Farge E (2011) Mechanotransduction in development. Curr Top Dev Biol 95:243-265.
    • (2011) Curr Top Dev Biol , vol.95 , pp. 243-265
    • Farge, E.1
  • 2
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V, Sheetz M (2006) Local force and geometry sensing regulate cell functions. Nat Rev Mol Cell Biol 7:265-275.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 3
    • 79960637431 scopus 로고    scopus 로고
    • Dynamic molecular processes mediate cellular mechanotransduction
    • Hoffman BD, Grashoff C, Schwartz MA (2011) Dynamic molecular processes mediate cellular mechanotransduction. Nature 475:316-323.
    • (2011) Nature , vol.475 , pp. 316-323
    • Hoffman, B.D.1    Grashoff, C.2    Schwartz, M.A.3
  • 4
    • 35348847063 scopus 로고    scopus 로고
    • Cell mechanics: Integrating cell responses to mechanical stimuli
    • DOI 10.1146/annurev.bioeng.9.060906.151927
    • Janmey PA, McCulloch CA (2007) Cell mechanics: Integrating cell responses to mechanical stimuli. Annu Rev Biomed Eng 9:1-34. (Pubitemid 350252899)
    • (2007) Annual Review of Biomedical Engineering , vol.9 , pp. 1-34
    • Janmey, P.A.1    McCulloch, C.A.2
  • 5
    • 75749107907 scopus 로고    scopus 로고
    • Cell mechanics and the cytoskeleton
    • Fletcher DA, Mullins RD (2010) Cell mechanics and the cytoskeleton. Nature 463:485-492.
    • (2010) Nature , vol.463 , pp. 485-492
    • Fletcher, D.A.1    Mullins, R.D.2
  • 6
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: An actin nucleator comes of age
    • DOI 10.1038/nrm2026, PII NRM2026
    • Goley ED, Welch MD (2006) The Arp2/3 complex: An actin nucleator comes of age. Nat Rev Mol Cell Biol 7:713-726. (Pubitemid 44450456)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.10 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 7
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • DOI 10.1016/S0092-8674(03)00120-X
    • Pollard TD, Borisy GG (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453-465. (Pubitemid 36263079)
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 12
    • 33748556828 scopus 로고    scopus 로고
    • Direct measurement of the lamellipodial protrusive force in a migrating cell
    • DOI 10.1083/jcb.200601159
    • Prass M, Jacobson K, Mogilner A, Radmacher M (2006) Direct measurement of the lamellipodial protrusive force in a migrating cell. J Cell Biol 174:767-772. (Pubitemid 44373726)
    • (2006) Journal of Cell Biology , vol.174 , Issue.6 , pp. 767-772
    • Prass, M.1    Jacobson, K.2    Mogilner, A.3    Radmacher, M.4
  • 13
    • 79951556468 scopus 로고    scopus 로고
    • New mechanisms and functions of actin nucleation
    • Firat-Karalar EN, Welch MD (2011) New mechanisms and functions of actin nucleation. Curr Opin Cell Biol 23:4-13.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 4-13
    • Firat-Karalar, E.N.1    Welch, M.D.2
  • 14
    • 13444301168 scopus 로고    scopus 로고
    • Actin-based motility of intracellular pathogens
    • DOI 10.1016/j.mib.2004.12.013, Host-Microbe Interactions: Bacteria
    • Gouin E, Welch MD, Cossart P (2005) Actin-based motility of intracellular pathogens. Curr Opin Microbiol 8:35-45. (Pubitemid 40203224)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.1 , pp. 35-45
    • Gouin, E.1    Welch, M.D.2    Cossart, P.3
  • 15
    • 33846314328 scopus 로고    scopus 로고
    • Reversible stress softening of actin networks
    • DOI 10.1038/nature05459, PII NATURE05459
    • Chaudhuri O, Parekh SH, Fletcher DA (2007) Reversible stress softening of actin networks. Nature 445:295-298. (Pubitemid 46122813)
    • (2007) Nature , vol.445 , Issue.7125 , pp. 295-298
    • Chaudhuri, O.1    Parekh, S.H.2    Fletcher, D.A.3
  • 17
    • 68249083215 scopus 로고    scopus 로고
    • Computational analysis of viscoelastic properties of crosslinked actin networks
    • Kim T, Hwang W, Lee H, Kamm RD (2009) Computational analysis of viscoelastic properties of crosslinked actin networks. PLoS Comput Biol 5:e1000439.
    • (2009) PLoS Comput Biol , vol.5
    • Kim, T.1    Hwang, W.2    Lee, H.3    Kamm, R.D.4
  • 18
    • 79951958040 scopus 로고    scopus 로고
    • Slow dynamics and internal stress relaxation in bundled cytoskeletal networks
    • Lieleg O, Kayser J, Brambilla G, Cipelletti L, Bausch AR (2011) Slow dynamics and internal stress relaxation in bundled cytoskeletal networks. Nat Mater 10:236-242.
    • (2011) Nat Mater , vol.10 , pp. 236-242
    • Lieleg, O.1    Kayser, J.2    Brambilla, G.3    Cipelletti, L.4    Bausch, A.R.5
  • 19
    • 23244432866 scopus 로고    scopus 로고
    • Large-scale quantitative analysis of sources of variation in the actin polymerization-based movement of Listeria monocytogenes
    • DOI 10.1529/biophysj.104.051219
    • Soo FS, Theriot JA (2005) Large-scale quantitative analysis of sources of variation in the actin polymerization-based movement of Listeria monocytogenes. Biophys J 89:703-723. (Pubitemid 41098320)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 703-723
    • Soo, F.S.1    Theriot, J.A.2
  • 20
    • 0032054640 scopus 로고    scopus 로고
    • F-actin-binding proteins
    • McGough A (1998) F-actin-binding proteins. Curr Opin Struct Biol 8:166-176.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 166-176
    • McGough, A.1
  • 21
    • 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 346:557-64.
    • (2005) J Mol Biol , vol.346 , pp. 557-564
    • De La Cruz, E.M.1
  • 22
    • 0035795407 scopus 로고    scopus 로고
    • Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits
    • DOI 10.1083/jcb.153.1.75
    • Galkin VE, Orlova A, Lukoyanova N, Wriggers W, Egelman EH (2001) Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J Cell Biol 153:75-86. (Pubitemid 34280195)
    • (2001) Journal of Cell Biology , vol.153 , Issue.1 , pp. 75-86
    • Galkin, V.E.1    Orlova, A.2    Lukoyanova, N.3    Wriggersd, W.4    Egelman, E.H.5
  • 23
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin from Acanthamoeba castellanii
    • Maciver SK, Zot HG, Pollard TD (1991) Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J Cell Biol 115:1611-1620. (Pubitemid 21910001)
    • (1991) Journal of Cell Biology , vol.115 , Issue.6 , pp. 1611-1620
    • Maciver, S.K.1    Zot, H.G.2    Pollard, T.D.3
  • 24
    • 34748872096 scopus 로고    scopus 로고
    • Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state
    • DOI 10.1083/jcb.200703092
    • Okreglak V, Drubin DG (2007) Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state. J Cell Biol 178:1251-1264. (Pubitemid 47480230)
    • (2007) Journal of Cell Biology , vol.178 , Issue.7 , pp. 1251-1264
    • Okreglak, V.1    Drubin, D.G.2
  • 25
    • 80052476842 scopus 로고    scopus 로고
    • Cofilin-linked changes in actin filament flexibility promote severing
    • McCullough BR, et al. (2011) Cofilin-linked changes in actin filament flexibility promote severing. Biophys J 101:151-159.
    • (2011) Biophys J , vol.101 , pp. 151-159
    • McCullough, B.R.1
  • 26
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard TD (2007) Regulation of actin filament assembly by Arp2/3 complex and formins. Annu Rev Biophys Biomol Struct 36:451-477.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 28
    • 80051977000 scopus 로고    scopus 로고
    • Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex
    • Ti S, Jurgenson CT, Nolen BJ, Pollard TD (2011) Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proc Natl Acad Sci USA 108:E463-E471.
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Ti, S.1    Jurgenson, C.T.2    Nolen, B.J.3    Pollard, T.D.4
  • 30
    • 6344258806 scopus 로고    scopus 로고
    • Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor
    • DOI 10.1016/j.molcel.2004.09.018, PII S1097276504005532
    • Goley ED, Rodenbusch SE, Martin AC, Welch MD (2004) Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor. Mol Cell 16:269-279. (Pubitemid 39388841)
    • (2004) Molecular Cell , vol.16 , Issue.2 , pp. 269-279
    • Goley, E.D.1    Rodenbusch, S.E.2    Martin, A.C.3    Welch, M.D.4
  • 31
    • 43749107589 scopus 로고    scopus 로고
    • Pathway of actin filament branch formation by Arp2/3 complex
    • Beltzner CC, Pollard TD (2008) Pathway of actin filament branch formation by Arp2/3 complex. J Biol Chem 283:7135-7144.
    • (2008) J Biol Chem , vol.283 , pp. 7135-7144
    • Beltzner, C.C.1    Pollard, T.D.2
  • 32
    • 84855359693 scopus 로고    scopus 로고
    • Three-dimensional reconstructions of Arp2/3 complex with bound nucleation promoting factors
    • 10.1038/emboj.2011.343
    • Xu X, et al. (2011) Three-dimensional reconstructions of Arp2/3 complex with bound nucleation promoting factors. EMBO J 236-247, 10.1038/emboj.2011.343.
    • (2011) EMBO J , pp. 236-247
    • Xu, X.1
  • 33
    • 33751229634 scopus 로고    scopus 로고
    • Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex
    • DOI 10.1529/biophysj.106.080937
    • Mahaffy RE, Pollard TD (2006) Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex. Biophys J 91:3519-3528. (Pubitemid 44788285)
    • (2006) Biophysical Journal , vol.91 , Issue.9 , pp. 3519-3528
    • Mahaffy, R.E.1    Pollard, T.D.2
  • 34
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • Blanchoin L, et al. (2000) Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404:1007-1011.
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1
  • 35
    • 45749109754 scopus 로고    scopus 로고
    • Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex
    • DOI 10.1021/bi702484h
    • Mahaffy RE, Pollard TD (2008) Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry 47:6460-6467. (Pubitemid 351874237)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6460-6467
    • Mahaffy, R.E.1    Pollard, T.D.2
  • 36
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • DOI 10.1016/S0960-9822(01)00629-7, PII S0960982201006297
    • Ichetovkin I, Grant W, Condeelis J (2002) Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr Biol 12:79-84. (Pubitemid 34063358)
    • (2002) Current Biology , vol.12 , Issue.1 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 40
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert H, et al. (1995) Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J Biol Chem 270:11437-11444.
    • (1995) J Biol Chem , vol.270 , pp. 11437-11444
    • Isambert, H.1
  • 41
    • 0019421683 scopus 로고
    • Gated binding of ligands to proteins
    • DOI 10.1038/293316a0
    • McCammon JA, Northrup SH (1981) Gated binding of ligands to proteins. Nature 293:316-317. (Pubitemid 11016269)
    • (1981) Nature , vol.293 , Issue.5830 , pp. 316-317
    • McCammon, J.A.1    Northrup, S.H.2
  • 42
    • 0013160046 scopus 로고    scopus 로고
    • Growth velocities of branched actin networks
    • Carlsson AE (2003) Growth velocities of branched actin networks. Biophys J 84:2907-2918.
    • (2003) Biophys J , vol.84 , pp. 2907-2918
    • Carlsson, A.E.1
  • 44
    • 0036573450 scopus 로고    scopus 로고
    • Large and small deflections of a cantilever beam
    • DOI 10.1088/0143-0807/23/3/317, PII S0143080702356678
    • Belendez T, Neipp C, Belendez A (2002) Large and small deflections of a cantilever beam. Eur J Phys 23:371-379. (Pubitemid 34590121)
    • (2002) European Journal of Physics , vol.23 , Issue.3 , pp. 371-379
    • Belendez, T.1    Neipp, C.2    Belendez, A.3
  • 45
    • 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. (Pubitemid 29407343)
    • (1999) Biophysical Journal , vol.77 , Issue.3 , pp. 1721-1732
    • Abraham, V.C.1    Krishnamurthi, V.2    Lansing, T.D.3    Lanni, F.4
  • 46
    • 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. (Pubitemid 34977700)
    • (2002) Biophysical Journal , vol.83 , Issue.3 , pp. 1237-1258
    • Mogilner, A.1    Edelstein-Keshet, L.2
  • 47
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • DOI 10.1083/jcb.145.5.1009
    • Svitkina TM, Borisy GG (1999) Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia.J Cell Biol 145:1009-1026. (Pubitemid 29270059)
    • (1999) Journal of Cell Biology , vol.145 , Issue.5 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 48
    • 77951977342 scopus 로고    scopus 로고
    • Electron tomography reveals unbranched networks of actin filaments in lamellipodia
    • Urban E, Jacob S, Nemethova M, Resch GP, Small JV (2010) Electron tomography reveals unbranched networks of actin filaments in lamellipodia. Nat Cell Biol 12:429-435.
    • (2010) Nat Cell Biol , vol.12 , pp. 429-435
    • Urban, E.1    Jacob, S.2    Nemethova, M.3    Resch, G.P.4    Small, J.V.5
  • 49
    • 80052477666 scopus 로고    scopus 로고
    • Reply: Visualizing branched actin filaments in lamellipodia by electron tomography
    • Small JV, Winkler C, Vinzenz M, Schmeiser C (2011) Reply: Visualizing branched actin filaments in lamellipodia by electron tomography. Nat Cell Biol 13:1013-1014.
    • (2011) Nat Cell Biol , vol.13 , pp. 1013-1014
    • Small, J.V.1    Winkler, C.2    Vinzenz, M.3    Schmeiser, C.4
  • 50
    • 69249088090 scopus 로고    scopus 로고
    • Structural plasticity in actin and tubulin polymer dynamics
    • Kueh HY, Mitchison TJ (2009) Structural plasticity in actin and tubulin polymer dynamics. Science 325:960-963.
    • (2009) Science , vol.325 , pp. 960-963
    • Kueh, H.Y.1    Mitchison, T.J.2
  • 51
    • 37549005604 scopus 로고    scopus 로고
    • Actin structure and function: What we still do not understand
    • Reisler E, Egelman EH (2007) Actin structure and function: What we still do not understand. J Biol Chem 282:36133-36137.
    • (2007) J Biol Chem , vol.282 , pp. 36133-36137
    • Reisler, E.1    Egelman, E.H.2
  • 52
    • 48049098171 scopus 로고    scopus 로고
    • Cofilin increases the bending flexibility of actin filaments: Implications for severing and cell mechanics
    • McCullough BR, Blanchoin L, Martiel J, Dela Cruz EM(2008) Cofilin increases the bending flexibility of actin filaments: Implications for severing and cell mechanics. J Mol Biol 381:550-558.
    • (2008) J Mol Biol , vol.381 , pp. 550-558
    • McCullough, B.R.1    Blanchoin, L.2    Martiel, J.3    Dela Cruz, E.M.4
  • 53
    • 80054079832 scopus 로고    scopus 로고
    • Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament
    • Hayakawa K, Tatsumi H, Sokabe M (2011) Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament. J Cell Biol 195:721-727.
    • (2011) J Cell Biol , vol.195 , pp. 721-727
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 54
    • 79851502285 scopus 로고    scopus 로고
    • Atomic force microscopy reveals drebrin induced remodeling of F-actin with subnanometer resolution
    • Sharma S, Grintsevich EE, Phillips ML, Reisler E, Gimzewski JK (2011) Atomic force microscopy reveals drebrin induced remodeling of F-actin with subnanometer resolution. Nano Lett 11:825-827.
    • (2011) Nano Lett , vol.11 , pp. 825-827
    • Sharma, S.1    Grintsevich, E.E.2    Phillips, M.L.3    Reisler, E.4    Gimzewski, J.K.5


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