Cellular motility driven by assembly and disassembly of actin filaments

Cell

Volumn 112, Issue 4, 2003, Pages 453-465

  Pollard, Thomas D ^a   Borisy, Gary G ^b  

^a YALE UNIVERSITY   (United States)

^b NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CAPPING PROTEIN; CELL PROTEIN; COFILIN; PHOSPHATE; POLYMER; PROFILIN; PROTEIN ARP2 3; UNCLASSIFIED DRUG; WISKOTT ALDRICH SYNDROME PROTEIN;

ACTIN FILAMENT; CATALYSIS; CELL GROWTH; CELL MEMBRANE; CELL MOTILITY; DEPOLYMERIZATION; GROWTH RATE; HYDROLYSIS; MATHEMATICAL MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN FUNCTION; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION;

VESPIDAE;

EID: 0037459075     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00120-X     Document Type: Review

References (128)

1. Abraham V.C., Krishnamurthi V., Taylor D.L., Lanni F. The actin-based nanomachine at the leading edge of migrating cells. Biophys. J. 77:1999;1721-1732.
2. Amann K.J., Pollard T.D. Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection microscopy. Proc. Natl. Acad. Sci. USA. 98:2001;15009-15013.
3. Arber S., Barbayannis F.A., Hanser H., Schneider C., Stanyon C.A., Bernard O., Caroni P. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature. 393:1998;805-809.
4. Bamburg J.R., McGough A., Ono S. Putting a new twist on actin. ADF/cofilins modulate actin dynamics Trends Cell Biol. 9:1999;364-370.
5. Bear J.E., Svitkina T.M., Krause M., Schafer D.A., Loureiro J.J., Strasser G.A., Maly I.V., Chaga O.Y., Cooper J.A., Borisy G.G., Gertler F.B. Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell. 109:2002;509-521.
6. Blanchoin L., Pollard T.D. Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J. Biol. Chem. 274:1999;15538-15546.
7. Blanchoin L., Pollard T.D. Hydrolysis of bound ATP by polymerized actin depends on the bound divalent cation but not profilin. Biochemistry. 41:2002;597-602.
8. Blanchoin L., Amann K.J., Higgs H.N., Marchand J.B., Kaiser D.A., Pollard T.D. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASp/Scar proteins. Nature. 404:2000;1007-1011. a.
9. Blanchoin L., Pollard T.D., Mullins R.D. Interaction of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks. Curr. Biol. 10:2000;1273-1282. b.
10. Blanchoin L., Robinson R.C., Choe S., Pollard T.D. Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure. J. Mol. Biol. 295:2000;203-211. c.
11. Bourne H.R., Weiner O. A chemical compass. Nature. 419:2002;21.
12. Cameron L.A., Svitkina T.M., Vignjevic D., Theriot J.A., Borisy G.G. Dendritic organization of actin comet tails. Curr. Biol. 11:2001;130-135.
13. Carlier M.F. Measurement of Pi dissociation from actin-filaments following ATP hydrolysis using a linked enzyme assay. Biochem. Biophys. Res. Commun. 143:1987;1069-1075.
14. Carlier M.F., Pantaloni D. 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.
15. Carlier M.F., Pantaloni D. Control of actin dynamics in cell motility. J. Mol. Biol. 269:1997;459-467.
16. Carlier M.F., Pantaloni D., Evans J.A., Lambooy P.K., Korn E.D., Webb M.R. The hydrolysis of ATP that accompanies actin polymerization is essentially irreversible. FEBS Lett. 235:1988;211-214.
17. Carlier M.F., Laurent V., Santolini J., Melki R., Didry D., Xia G.X., Hong Y., Chua N.H., Pantaloni D. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover. implication in actin-based motility J. Cell Biol. 136:1997;1307-1322.
18. Carlier M.F., Nioche P., Broutin-L'Hermite I., Boujemaa R., Le Clainche C., Egile C., Garbay C., Ducruix A., Sansonetti P.J., Pantaloni D. Grb2 links signalling to actin assembly by enhancing interaction of neural Wiskott-Aldrich Syndrome protein (N-WASP) with actin-related-protein (Arp2/3) complex. J. Biol. Chem. 275:2000;21946-21952.
19. Chan A.Y., Bailly M., Zebda N., Segall J.E., Condeelis J.S. Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J. Cell Biol. 148:2000;531-542.
20. Condeelis J. Life at the leading edge. the formation of cell protrusions Annu. Rev. Cell Biol. 9:1993;411-444.
21. Cooper J.A., Schafer D.A. Control of actin assembly and disassembly at filament ends. Curr. Opin. Cell Biol. 12:2000;97-103.
22. Cunningham C.C., Gorlin J.B., Kwiatkowski D.J., Hartwig J.H., Janmey P.A., Byers H.R., Stossel T.P. Actin-binding protein requirement for cortical stability and efficient locomotion. Science. 255:1992;325-327.
23. Dayel M.J., Holleran R.D., Mullins D.M. Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments. Proc. Natl. Acad. Sci. USA. 98:2001;14871-14876.
24. De La Cruz E.M., Mandinova A., Steinmetz M.O., Stoffler D., Aebi U., Pollard T.D. Polymerization and structure of nucleotide-free actin filaments. J. Mol. Biol. 295:2000;517-526. a.
25. De La Cruz E.M., Ostap E.M., Brundage R.A., Reddy K.S., Sweeney H.L., Safer D. Thymosin-beta(4) changes the conformation and dynamics of actin monomers. Biophys. J. 78:2000;2516-2527. b.
26. DesMarais V., Ichetovkin I., Condeelis J., Hitchcock-DeGregori S.E. Spatial regulation of actin dynamics. a tropomyosin-free, actin-rich compartment at the leading edge J. Cell Sci. 115:2003;4649-4660.
27. Drenckhahn D., Pollard T.D. Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J. Biol. Chem. 261:1986;12754-12758.
28. Duncan M.C., Cope M.J., Goode B.L., Wendland B., Drubin D.G. Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex. Nat. Cell Biol. 3:2001;687-690.
29. Edds K.T. Effects of cytochalasin and colcemid on cortical flow in coelomocytes. Cell Motil. Cytoskeleton. 26:1993;262-273.
30. Eden S., Rohatgi R., Podtelejnikov A.V., Mann M., Kirschner M.W. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature. 418:2002;790-793.
31. Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. Activation of LIM-kinase by Pak1 couples Rac/Cdc4242 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. 1:1999;253-259.
32. Egile C., Loisel T.P., Laurent V., Li R., Pantaloni D., Sansonetti P.J., Carlier M.F. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146:1999;1319-1332.
33. Euteneuer U., Schliwa M. Persistent, directional motility of cells and cytoplasmic fragments in the absence of microtubules. Nature. 310:1984;58-61.
34. Evangelista M., Klebl B.M., Tong A.H., Webb B.A., Leeuw T., Leberer E., Whiteway M., Thomas D.Y., Boone C. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J. Cell Biol. 148:2000;353-362.
35. Falet H., Hoffmeister K.M., Neujahr R., Italiano J.E., Stossel T.P., Southwick F.S., Hartwig J.H. Importance of free actin filament barbed ends for Arp2/3 complex function in platelets and fibroblasts. Proc. Natl. Acad. Sci. USA. 99:2002;16782-16787.
36. Frischknecht F., Moreau V., Rottger S., Gonfloni S., Reckmann I., Superti-Furga G., Way M. Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling. Nature. 401:1999;926-929.
37. Fujiwara I., Suetsugu S., Uemura S., Takenawa T., Ishiwata S. Visualization and force measurement of branching by Arp2/3 complex and N-WASP in actin filament. Biochem. Biophys. Res. Commun. 293:2002;1550-1555. a.
38. Fujiwara I., Takahashi S., Tadakuma H., Funatsu T., Ishiwata S. Microscopic analysis of polymerization dynamics with individual actin filaments. Nat. Cell Biol. 4:2002;666-673. b.
39. Gittes F., Mickey B., Nettleton J., Howard J. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 120:1993;923-934.
40. Goode B.L., Rodal A.A., Barnes G., Drubin D.G. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J. Cell Biol. 153:2001;627-634.
41. Henson J.H., Svitkina T.M., Burns A.R., Hughes H.E., MacPartland K.J., Nazarian R. Two components of actin-based retrograde flow in sea urchin coelomocytes. Mol. Biol. Cell. 10:1999;4075-4090.
42. Higgs H.N., Pollard T.D. Wiskott-Aldrich syndrome protein (WASp) activation of Arp2/3 complex. effects of phosphatidylinositol-4,5-bisphosphate and Cdc42 J. Cell Biol. 150:2000;1311-1320.
43. Higgs N.H., Pollard T.D. Regulation of actin filament network formation through Arp2/3 complex. activation by a diverse array of proteins Annu. Rev. Biochem. 70:2001;649-676.
44. Higgs H.N., Blanchoin L., Pollard T.D. Influence of the Wiskott-Aldrich syndrome protein (WASp) C terminus and Arp2/3 complex on actin polymerization. Biochemistry. 38:1999;15212-15222.
45. Huang M., Yang C., Schafer D.A., Cooper J.A., Higgs H.N., Zigmond S.H. Cdc42-induced actin filaments are protected from capping protein. Curr. Biol. 9:1999;979-982.
46. Ichetovkin I., Han J., Pang K.M., Knecht D.A., Condeelis J.S. Actin filaments are severed by both native and recombinant dictyostelium cofilin but to different extents. Cell Motil. Cytoskeleton. 45:2000;293-306.
47. Ichetovkin I., Grant W., Condeelis J. Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr. Biol. 12:2002;79-84.
48. Janmey P.A., Stossel T.P. Modulation of gelsolin function by phosphatidylinositol 4,5-biphosphate. Nature. 325:1987;362-364.
49. Kaiser D.A., Vinson V.K., Murphy D.B., Pollard T.D. Profilin is predominantly associated with monomeric actin in Acanthamoeba. J. Cell Sci. 112:1999;3779-3790.
50. Kim A.S., Kakalis L.T., Abdul-Manan N., Liu G.A., Rosen M.K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature. 404:2000;151-158.
51. Kocks C., Gouin E., Tabouret M., Berche P., Ohayon H., Cossart P. L. monocytogenese induced actin assembly requires the actA gene product, a surface protein. Cell. 68:1992;521-531.
52. Le Clainche C., Didry D., Carlier M.F., Pantaloni C. Activation of Arp2/3 complex by Wiskott-Aldrich syndrome protein is linked to enhanced binding of ATP to Arp2. J. Biol. Chem. 276:2001;46689-46692.
53. Lechler T., Shevchenko A., Li R. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J. Cell Biol. 148:2000;363-373.
54. Lee W.L., Bezanilla M., Pollard T.D. Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp. J. Cell Biol. 151:2000;789-800.
55. Lin C.H., Forscher P. Growth cone advance is inversely proportional to retrograde F-actin flow. Neuron. 14:1995;763-771.
56. Loisel T.P., Boujemaa R., Pantaloni D., Carlier M.F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature. 401:1999;613-616.
57. Lu J., Pollard T.D. Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast. Mol. Biol. Cell. 12:2001;1161-1175.
58. Machesky L.M., Insall R.H. Scar1 and the related Wiskott-Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8:1998;1347-1356.
59. Machesky L.M., Atkinson S.J., Ampe C., Vandekerckhove J., Pollard T.D. Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose. J. Cell Biol. 127:1994;107-115.
60. Machesky L.M., Mullins D.M., Higgs H.N., Kaiser D.A., Blanchoin L., May R.C., Hall M.E., Pollard T.D. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc. Natl. Acad. Sci. USA. 96:1999;3739-3744.
61. Maciver S.K., Zot H.G., Pollard T.D. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol. 115:1991;1611-1620.
62. Maciver S.K., Pope B.J., Whytock S., Weeds A.G. The effect of two actin depolymerizing factors (ADF/Cofilins) on actin filament turnover. pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin Eur. J. Biochem. 256:1998;388-397.
63. Maly I.V., Borisy G.G. Self-organization of a propulsive actin network as an evolutionary process. Proc. Natl. Acad. Sci. USA. 98:2001;11324-11329.
64. Marchand J.B., Kaiser D.A., Pollard T.D., Higgs H.N. Interaction of WASp/Scar proteins with actin and vertebrate Arp2/3 complex., Nat. Cell Biol. 3:2001;76-82.
65. McGough A., Pope B., Chiu W., Weeds A. Cofilin changes the twist of F-actin. implications for actin filament dynamics and cellular function J. Cell Biol. 138:1997;771-781.
66. Merrifield C.J., Moss S.E., Ballestrem C., Imhof B.A., Giese G., Wunderlich I., Almers W. Endocytic vesicles move at the tips of actin tails in cultured mast cells. Nat. Cell Biol. 1:1999;72-74.
67. Miki H., Takenawa T. Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization. Biochem. Biophys. Res. Commun. 243:1998;73-78.
68. Miki H., Suetsugu S., Takenawa T. WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 17:1998;6932-6941.
69. Miki H., Yamaguchi H., Suetsugu S., Takenaka T. IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 408:2000;732-735.
70. Mockrin S.C., Korn R.D. Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry. 19:1980;5359-5362.
71. Mogilner A., Oster G. Cell motility driven by actin polymerization. Biophys. J. 71:1996;3030-3045.
72. Mogilner A., Edelstein-Keshet L. Regulation of actin dynamics in rapidly moving cells. a quantitative analysis Biophys. J. 83:2002;1237-1258.
73. Mullins R.D., Heuser J.A., Pollard T.D. 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.
74. Nishida E., Maekawa S., Sakai H. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry. 23:1984;5307-5313.
75. Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell. 108:2002;233-246.
76. Nyakern-Meazza M., Narayan K., Schutt C.E., Lindberg U. Tropomyosin and gelsolin cooperate in controlling the microfilament system. J. Biol. Chem. 277:2002;28774-28779.
77. Okada K., Blanchoin L., Abe H., Chen H., Pollard T.D., Bamburg J.R. Xenopus actin interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends. J. Biol. Chem. in press:2002.
78. Pantaloni D., Boujemaa R., Didry D., Gounon P., Carlier M.F. The Arp2/3 complex branches filament barbed ends. functional antagonism with capping proteins Nat. Cell Biol. 2:2000;385-391.
79. Pollard T.D. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103:1986;2747-2754.
80. Pollard T.D. Introduction to actin and actin-binding proteins. Second Edition T., Kreis and R., Vale Guidebook to the Cytoskeletal and Motor Proteins. 1999;Oxford University Press, New York. 3-11.pp.
81. Pollard T.D., Beltzner C.C. Structure and function of the Arp2/3 complex. Curr. Opin. Struct. Biol. 12:2002;768-774.
82. Pollard T.D., Earnshaw W.C. Cell Biology. 2002;W.B. Saunders, New York.
83. Pollard T.D., Blanchoin L., Mullins R.D. Biophysics of actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29:2000;545-576.
84. Prehoda K.E., Scott J.A., Mullins R.D., Lim W.A. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science. 290:2000;801-806.
85. Pruyne D., Evangelista M., Yang C., Bi E., Zigmond S., Bretscher A., Boone C. Role of formins in actin assembly. nucleation and barbed end association Science. 297:2002;612-615.
86. Rengan R., Ochs H.D., Sweet L.I., Keil M.L., Gunning W.T., Lachant N.A., Boxer L.A., Omann G.M. Actin cytoskeletal function is spared, but apoptosis is increased, in WAS patient hematopoetic cells. Blood. 95:2000;1283-1292.
87. Robinson R.C., Turbedsky K., Kaiser D., Higgs H., Marchand J.B., Choe S., Pollard T.D. Crystal structure of Arp2/3 complex. Science. 294:2001;1660-1661.
88. Rohatgi R., Ma L., Miki H., Lopez M., Kirchhausen T., Takenawa T., Kirschner M.W. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell. 97:1999;221-231.
89. Rohatgi R., Ho H.-Y.H., Kirschner M.W. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate. J. Cell Biol. 150:2000;1299-1310.
90. Rohatgi R., Nollau P., Ho H.Y., Kirschner M.W., Mayer B.J. Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway. J. Biol. Chem. 276:2001;26448-26452.
91. Rosenblatt J., Peluso P., Mitchison T.J. The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound. Mol. Biol. Cell. 6:1995;227-236.
92. Rosenblatt J., Agnew B.J., Abe H., Bamburg J.R., Mitchison T.J. Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails. J. Cell Biol. 136:1997;1323-1332.
93. Rozelle A.L., Machesky L.M., Yamamoto M., Driessens M.H., Insall R.H., Roth M.G., Luby-Phelps K., Marriott G., Hall A., Yin H.L. Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3. Curr. Biol. 10:2000;311-320.
94. Safer D., Nachmias V.T. Beta thymosins as actin binding peptides. Bioessays. 16:1994;473-479.
95. Sagot I., Rodal A.A., Moseley J., Goode B.L., Pellman D. An actin nulceation mechanism mediated by Bni 1 and Profilin. Nat. Cell Biol. 4:2002;626-631.
96. Salmon W.C., Adams M.C., Waterman-Storer C.M. Dual-wavelength fluorescent speckle microscopy reveals coupling of microtubule and actin movements in migrating cells. J. Cell Biol. 158:2002;31-37.
97. Schafer D.A., Jennings P.B., Cooper J.A. Dynamics of capping protein and actin assembly in vitro. uncapping barbed ends by polyphosphoinositides J. Cell Biol. 135:1996;169-179.
98. Schluter K., Jockusch B.M., Rothkegel M. Profilins as regulators of actin dynamics. Biochim. Biophys. Acta. 1359:1997;97-109.
99. Skoble J., Portnoy D.A., Welch M.D. Three regions within ActA promote Arp2/3 complex-mediated actin nucleation and Listeria monocytogenes motility. J. Cell Biol. 150:2000;527-538.
100. Small J.V., Isenberg G., Celis J.E. Polarity of actin at the leading edge of cultured cells. Nature. 272:1978;638-639.
101. Smith G.A., Portnoy D.A., Theriot J.A. Asymmetric distribution of the Listeria monocytogenes ActA protein is required and sufficient to direct actin-based motility. Mol. Microbiol. 17:1995;945-951.
102. Sun H.Q., Yamamoto M., Mejillano M., Yin H.L. Gelsolin, multifunctional actin regulatory protein. J. Biol. Chem. 274:1999;33179-33182.
103. Svitkina T.M., Borisy G.G. 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.
104. Svitkina T.M., Verkhovsky A.B., McQuade K.M., Borisy G.G. Analysis of the actin-myosin II system in fish epidermal keratocytes. mechanism of cell body translocation J. Cell Biol. 139:1997;397-415.
105. Symons M.H., Mitchison T.J. Control of actin polymerization in live and permeabilized fibroblasts. J. Cell Biol. 114:1991;503-513.
106. Theriot J.A., Mitchison T.J. Actin microfilament dynamics in locomoting cells. Nature. 352:1991;126-131.
107. Theriot J.A., Mitchison T.J. Comparison of actin and cell surface dynamics in motile fibroblasts. J. Cell Biol. 119:1992;367-377.
108. Theriot J.A., Mitchison T.J., Tilney L.G., Portnoy D.A. The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature. 357:1992;257-260.
109. Tilney L.G., DeRosier D.J., Tilney M.S. How Listeria exploits host cell actin to form its own cytoskeleton. I. Formation of a tail and how that tail might be involved in movement. J. Cell Biol. 118:1992;71-81.
110. Uruno T., Liu J., Zhang P., Fan X., Egile C., Li R., Mueller S.C., Zhan X. Activation of Arp2/3 complex mediated actin polymerization by cortactin. Nat. Cell Biol. 3:2001;259-266.
111. Verkhovsky A.B., Svitkina T.M., Borisy G.G. Self-polarization and directional motility of cytoplasm. Curr. Biol. 9:1999;11-20.
112. Vinson V.K., De La Cruz E.M., Higgs H.N., Pollard T.D. Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry. 37:1998;10871-10880.
113. Volkmann N., Amann K.J., Stoilova-McPhie S., Egile C., Winter D.C., Hazelwood L., Heuser J.E., Li R., Pollard T.D., Hanein D. Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science. 293:2001;2456-2459.
114. Wang Y. Exchange of actin subunits at the leading edge of living fibroblasts. possible role of treadmilling J. Cell Biol. 101:1985;597-602.
115. Watanabe N., Mitchison T.J. Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science. 295:2002;1083-1086.
116. Weaver A.M., Karginov A.V., Kinley A.W., Weed S.A., Li Y., Parsons J.T., Cooper J.A. Cortactin promotes and stabilizes Arp2/3-induced actin filament network formation. Curr. Biol. 11:2001;370-374.
117. Weaver A.M., Heuser J.E., Karginov A.V., Lee W.L., Parsons J.T., Cooper J.A. Interaction of cortactin and N-WASp with Arp2/3 complex. Curr. Biol. 12:2002;1270-1278.
118. Weaver A.M., Young M.E., Lee W.-L., Copper J.A. Integration of signals to the Arp2/3 complex. Curr. Opin. Cell Biol. 15:2003;23-30.
119. Weed S.A., Kariginov A.V., Schafer D.A., Weaver A.M., Kinley A.W., Cooper J.A., Parsons J.T. Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex. J. Cell Biol. 151:2000;29-40.
120. Welch M.D., Rosenblatt J., Skoble J., Portnoy D.A., Mitchison T.J. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science. 281:1998;105-108.
121. Winter D., Lechler T., Li R. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9:1999;501-504.
122. Yang N., Higuchi O., Ohashi K., Nagata K., Wada A., Kangawa K., Nishida E., Mizuno K. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature. 393:1998;809-812.
123. Yang C., Huang M., DeBiasio J., Pring M., Joyce M., Miki H., Takenawa T., Zigmond S.H. Profilin enhances Cdc42-induced nucleation of actin polymerization. J. Cell Biol. 150:2000;1001-1012.
124. Yarar D., To W., Abo A., Welch M.D. The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9:1999;555-558.
125. Zalevsky J., Grigorova I., Mullins R.D. Activation of the Arp2/3 complex by the Listeria ActA protein. ActA binds two actin monomers and three subunits of the Arp2/3 complex J. Biol. Chem. 276:2001;3468-3475. a.
126. Zalevsky J., Lempert L., Kranitz H., Mullins R.D. Different WASP family proteins stimulate different ARP2/3 complex-dependent actin-nucleating activities. Curr. Biol. 11:2001;1903-1913. b.
127. Zebda N., Bernard O., Bailly M., Welti S., Lawrence D.S., Condeelis J.S. Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequence lamellipod extension. J. Cell Biol. 151:2000;1119-1127.
128. Zigmond S.H. Signal transduction and actin filament organization. Curr. Opin. Cell Biol. 8:1996;66-73.