The actin slingshot

Current Opinion in Cell Biology

Volumn 17, Issue 1, 2005, Pages 62-66

  Plastino, Julie ^a   Sykes, Cécile ^a  

^a INSTITUT CURIE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL PROTEIN;

ACTIN FILAMENT; BIOCHEMISTRY; BIOMIMETICS; CELL MEMBRANE; CELL MOTILITY; CELL SHAPE; CELL SURFACE; CYTOLOGY; EXPERIMENTAL MODEL; HUMAN; IN VITRO STUDY; LISTERIA MONOCYTOGENES; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN POLYMERIZATION; REVIEW; THEORETICAL MODEL; THERMAL ANALYSIS;

ACTINS; BIOCHEMISTRY; CELL MEMBRANE; CELL MOVEMENT; LISTERIA MONOCYTOGENES; MICROTUBULES; MODELS, BIOLOGICAL; POLYMERS;

LISTERIA; LISTERIA MONOCYTOGENES;

EID: 12344338318     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.12.001     Document Type: Review

References (49)

1. C.J. Merrifield, S.E. Moss, C. Ballestrem, B.A. Imhof, G. Giese, I. Wunderlich, and W. Almers Endocytic vesicles move at the tips of actin tails in cultured mast cells Nat Cell Biol 1 1999 72 74
2. M. Kaksonen, Y. Sun, and D.G. Drubin A pathway for association of receptors, adaptors, and actin during endocytic internalization Cell 115 2003 475 487
3. A. Ott, M. Magnasco, A. Simon, and A. Libchaber Measurement of the persistence length of polymerized actin using fluorescence microscopy Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics 48 1993 R1642 R1645
4. F. Gittes, B. Mickey, J. Nettleton, and J. Howard Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape J Cell Biol 120 1993 923 934
5. M. Dogterom, and B. Yurke Measurement of the force-velocity relation for growing microtubules Science 278 1997 856 860
6. A. Mogilner, and G. Oster Force generation by actin polymerization II: the elastic ratchet and tethered filaments Biophys J 84 2003 1591 1605
7. U. Euteneuer, and M. Schliwa Persistent, directional motility of cells and cytoplasmic fragments in the absence of microtubules Nature 310 1984 58 61
8. K.S. Uchida, T. Kitanishi-Yumura, and S. Yumura Myosin II contributes to the posterior contraction and the anterior extension during the retraction phase in migrating Dictyostelium cells J Cell Sci 116 2003 51 60
9. A.E. Carlsson Structure of autocatalytically branched actin solutions Phys Rev Lett 92 2004 238102
10. K.J. Amann, and T.D. Pollard Direct real-time observation of actin filament branching mediated by ARP2/3 complex using total internal reflection fluorescence microscopy Proc Natl Acad Sci USA 98 2001 15009 15013
11. T.M. Svitkina, and G.C. 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
12. F. Nakamura, E. Osborn, P.A. Janmey, and T.P. Stossel Comparison of filamin A-induced cross-linking and Arp2/3 complex-mediated branching on the mechanics of actin filaments J Biol Chem 277 2002 9148 9154
13. L.M. Machesky, and R.H. Insall Signaling to actin dynamics J Cell Biol 146 1999 267 272
14. J.V. Small, M. Herzog, and K. Anderson Actin filament organization in the fish keratocyte lamellipodium J Cell Biol 129 1995 1275 1286
15. T.M. Svitkina, E.A. Bulanova, O.Y. Chaga, D.M. Vignjevic, S. Kojima, J.M. Vasiliev, and G.G. Borisy Mechanism of filopodia initiation by reorganization of a dendritic network J Cell Biol 160 2003 409 421 The authors employ a challenging experimental approach consisting of live cell fluorescence imaging of filopodia formation, followed by electron microscopy of these same filopodia. They conclude that filopodia are not de novo structures, but are produced by a reorganization of the existing branched actin network that involves shedding of the Arp2/3 complex and association with fascin and VASP.
16. E.S. Harris, and H.N. Higgs Actin cytoskeleton: formins lead the way Curr Biol 14 2004 520 522
17. S. Samarin, S. Romero, C. Kocks, D. Didry, D. Pantaloni, and M.F. Carlier How VASP enhances actin-based motility J Cell Biol 163 2003 131 142 This is a study of the molecular mechanism by which VASP enhances motility. Using ActA-coated beads in the mixture of purified proteins that reconstitute actin-based motility, the authors show that the presence of VASP facilitates the dissociation of branched Arp2/3 junctions from the bead surface.
18. J. Plastino, S. Olivier, and C. Sykes Actin filaments align into hollow comets for rapid VASP-mediated propulsion Curr Biol 14 2004 1766 1771 The authors show that hollow comets propel beads faster than filament-packed comets. Hollow comets are obtained by increasing the recruitment of VASP to the surface of beads placed in cell extracts. By enhancing the detachment of actin filaments from the surface, the presence of VASP allows the comet to be pulled off at the rear of the bead, thereby decreasing comet-bead friction and enhancing velocity.
19. J.E. Bear, T.M. Svitkina, M. Krause, D.A. Schafer, J.J. Loureiro, G.A. Strasser, I.V. Maly, O.Y. Chaga, J.A. Cooper, and G.G. Borisy Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility Cell 109 2002 509 521
20. A. Ponti, M. Machacek, S.L. Gupton, C.M. Waterman-Storer, and G. Danuser Two distinct actin networks drive the protrusion of migrating cells Science 305 2004 1782 1786
21. J.A. Theriot, T.J. Mitchison, L.G. Tilney, and D.A. Portnoy The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization Nature 357 1992 257 260
22. M.D. Welch, J. Rosenblatt, J. Skoble, D.A. Portnoy, and T.J. Mitchison Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation Science 281 1998 105 108
23. F. Gerbal, V. Laurent, A. Ott, M.-F. Carlier, P. Chaikin, and J. Prost Measurement of the elasticity of the actin tail of Listeria monocytogenes Eur Biophys J 29 2000 134 140
24. Y. Marcy, J. Prost, M.-F. Carlier, and C. Sykes Forces generated during actin-based propulsion: a direct measurement by micromanipulation Proc Natl Acad Sci USA 101 2004 5992 5997 The purified protein actin-based motility assay is used in conjunction with a micromanipulation set-up to quantitatively measure the force velocity relationship of the propulsive force generated by actin polymerization at a surface. The authors obtain the values of the propulsive force, the elastic modulus, the stall force and the pull-out force of the comet.
25. T.P. Loisel, R. Boujemaa, D. Pantaloni, and M.F. Carlier Reconstitution of actin-based motility of Listeria and Shigella using pure proteins Nature 401 1999 613 616
26. P. Cossart Actin-based bacterial motility Curr Opin Cell Biol 7 1995 94 101
27. L.A. Cameron, M.J. Footer, A. Van Oudenaarden, and J.A. Theriot Motility of ActA protein-coated microspheres driven by actin polymerization Proc Natl Acad Sci USA 96 1999 4908 4913
28. A. Bernheim-Groswasser, S. Wiesner, R.M. Golsteyn, M.-F. Carlier, and C. Sykes The dynamics of actin-based motility depend on surface parameters Nature 417 2002 308 311
29. J.H. Shin, M.L. Gardel, L. Mahadevan, P. Matsudaira, and D.A. Weitz Relating microstructure to rheology of a bundled and cross-linked F-actin network in vitro Proc Natl Acad Sci USA 101 2004 9636 9641
30. M.L. Gardel, J.H. Shin, F.C. MacKintosh, L. Mahadevan, P. Matsudaira, and D.A. Weitz Elastic behavior of cross-linked and bundled actin networks Science 304 2004 1301 1305 The cross-linking protein scruin is used to fine tune the mechanical properties of actin networks in vitro. The elastic behavior of actin meshes is shown to vary with filament concentration, cross-link density and actin bundle thickness.
31. R.E. Mahaffy, S. Park, E. Gerde, J. Kas, and C.K. Shih Quantitative analysis of the viscoelastic properties of thin regions of fibroblasts using atomic force microscopy Biophys J 86 2004 1777 1793
32. L. Limozin, M. Barmann, and E. Sackmann On the organization of self-assembled actin networks in giant vesicles Eur Phys J E 10 2003 319 330
33. C.I. Lacayo, and J.A. Theriot Listeria monocytogenes actin-based motility varies depending on subcellular location: a kinematic probe for cytoarchitecture Mol Biol Cell 15 2004 2164 2175 This is a study of the sensitivity of Listeria movement to the presence of cellular obstacles such as mitochondria within a cell. Bacteria move slightly faster in the presence of mitochondria where the F-actin network is less dense, although their paths are more curved than in the absence of mitochondria.
34. V. Noireaux, R.M. Golsteyn, E. Friederich, J. Prost, C. Antony, D. Louvard, and C. Sykes Growing an actin gel on spherical surfaces Biophys J 78 2000 1643 1654
35. F. Gerbal, P. Chaikin, Y. Rabin, and J. Prost An elastic analysis of Listeria monocytogenes propulsion Biophys J 79 2000 2259 2279
36. A. Upadhyaya, J.R. Chabot, A. Andreeva, A. Samadani, and A. van Oudenaarden Probing polymerization forces by using actin-propelled vesicles Proc Natl Acad Sci USA 100 2003 4521 4526 This paper reports experimental observation of the 'squeezing effect' in actin-based motility. By examining the movement and the contour of liposomes propelled by actin comets, the authors obtain an estimate of the stress (force per surface area) that the actin gel exerts on the liposomes.
37. P.A. Giardini, D.A. Fletcher, and J.A. Theriot Compression forces generated by actin comet tails on lipid vesicles Proc Natl Acad Sci USA 100 2003 6493 6498
38. J. Taunton, B.A. Rowning, M.L. Coughlin, M. Wu, R.T. Moon, T.J. Mitchison, and C.A. Larabell Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP J Cell Biol 148 2000 519 530
39. H. Boukellal, J. Plastino, V. Noireaux, and C. Sykes Propelling soft objects C R Phys 4 2003 275 280
40. H. Boukellal, O. Campas, J.-F. Joanny, J. Prost, and C. Sykes Soft Listeria: actin-based propulsion of liquid drops Phys Rev E 69 2004 061906 The authors use a system of soft oil droplets propelled by actin polymerization to provide evidence for the squeezing effect produced by an elastic actin gel. Droplet deformation allows for a precise determination of the local stress exerted by the actin gel as the surface tension can be estimated independently.
41. W.M. Brieher, M. Coughlin, and T.J. Mitchison Fascin-mediated propulsion of Listeria monocytogenes independent of frequent nucleation by the Arp2/3 complex J Cell Biol 165 2004 233 242
42. I.M. Schwartz, M. Ehrenberg, M. Bindschadler, and J.L. McGrath The role of substrate curvature in actin-based pushing forces Curr Biol 14 2004 1094 1098
43. J.L. McGrath, N.J. Eungdamrong, C.I. Fisher, F. Peng, L. Mahadevan, T.J. Mitchison, and S.C. Kuo The force-velocity relationship for the actin-based motility of Listeria monocytogenes Curr Biol 13 2003 329 332
44. S. Wiesner, E. Helfer, D. Didry, G. Ducouret, F. Lafuma, M.-F. Carlier, and D. Pantaloni A biomimetic motility assay provides insight into the mechanism of actin-based motility J Cell Biol 160 2003 387 398
45. J.L. Tan, J. Tien, D.M. Pirone, D.S. Gray, K. Bhadriraju, and C.S. Chen Cells lying on a bed of microneedles: An approach to isolate mechanical force Proc Natl Acad Sci USA 100 2003 1484 1489
46. J. Plastino, I. Lelidis, J. Prost, and C. Sykes The effect of diffusion, depolymerization and nucleation promoting factors on actin gel growth Eur Biophys J 33 2004 310 320
47. K. Sekimoto, J. Prost, F. Julicher, H. Boukellal, and A. Bernheim-Grosswasser Role of tensile stress in actin gels and a symmetry-breaking instability Eur Phys J E 13 2004 247 259
48. Jarroux N, Keller P, Mingotaud A-F, Mingotaud C, Sykes C: Shape-tunable polymer nodules grown from liposomes via ring opening metathesis polymerization. J Am Chem Soc, doi: 10.1021/ja045482j.
49. L. Miao, O. Vanderlinde, M. Stewart, and T.M. Roberts Retraction in amoeboid cell motility powered by cytoskeletal dynamics Science 302 2003 1405 1407