Control of actin assembly and disassembly at filament ends

Current Opinion in Cell Biology

Volumn 12, Issue 1, 2000, Pages 97-103

  Cooper, John A ^a   Schafer, Dorothy A ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ADAPTOR PROTEIN; COFILIN; GELSOLIN; GUANINE NUCLEOTIDE BINDING PROTEIN; TROPOMODULIN;

ACTIN FILAMENT; ACTIN POLYMERIZATION; CELL MOTION; LISTERIA; PRIORITY JOURNAL; PROTEIN ASSEMBLY; REVIEW;

ACTIN DEPOLYMERIZING FACTORS; ACTIN-RELATED PROTEIN 2; ACTIN-RELATED PROTEIN 3; ACTINS; ANIMALS; CAPZ ACTIN CAPPING PROTEIN; CARRIER PROTEINS; CELL MOVEMENT; CYTOSKELETAL PROTEINS; GELSOLIN; HUMANS; MICROFILAMENT PROTEINS; MICROFILAMENTS; MOLECULAR MOTOR PROTEINS; MUSCLE PROTEINS; TROPOMODULIN;

LISTERIA;

EID: 0033965314     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)00062-9     Document Type: Review

References (73)

1. Loisel T., Boujemaa R., Pantaloni D., Carlier M-F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature. 401:1999;613-616. This is the first description of a synthetic system able to mediate actin polymerization and motility of bacteria. Actin and three actin binding proteins - Arp2/3 complex, capping protein and cofilin - are sufficient.
2. Schafer D.A., Cooper J.A. Control of actin assembly at filament ends. Annu Rev Cell Dev Biol. 11:1995;497-518.
3. Littlefield R., Fowler V.M. Defining actin filament length in striated muscle: rulers and caps or dynamic stability? Annu Rev Cell Dev Biol. 14:1998;487-525.
4. Machesky L.M., Insall R.H. Signaling to actin dynamics. J Cell Biol. 146:1999;267-272.
5. Bi E., Zigmond S.H. Actin polymerization: where the WASP stings. Curr Biol. 9:1999;160-163.
6. Machesky L.M., Way M. Cell motility - actin branches out. Nature. 394:1998;125-126.
7. Machesky L.M., Gould K.L. The Arp2/3 complex: a multifunctional actin organizer. Curr Opin Cell Biol. 11:1999;117-121.
8. Mullins R.D., Pollard T.D. Structure and function of the Arp2/3 complex. Curr Opin Struct Biol. 9:1999;244-249.
9. Maciver S.K. How ADF/cofilin depolymerizes actin filaments. Curr Opin Cell Biol. 10:1998;140-144.
10. 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.
11. Kwiatkowski D.J. Functions of gelsolin: motility, signaling, apoptosis, cancer. Curr Opin Cell Biol. 11:1999;103-108.
12. Carlier M.F., Pantaloni D. Control of actin dynamics in cell motility. J Mol Biol. 269:1997;459-467.
13. David V., Gouin E., Troys M.V., Grogan A., Segal A.W., Ampe C., Cossart P. Identification of cofilin, coronin, Rac and capZ in actin tails using a Listeria affinity approach. J Cell Sci. 111:1998;2877-2884.
14. Hug C., Jay P.Y., Reddy I., McNally J.G., Bridgman P.C., Elson E.L., Cooper J.A. Capping protein levels influence actin assembly and cell motility in Dictyostelium. Cell. 81:1995;591-600.
15. 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.
16. Barkalow K., Witke W., Kwiatkowski D.J., Hartwig J.H. Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J Cell Biol. 134:1996;389-399.
17. Eddy R.J., Han J., Condeelis J.S. Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium. J Cell Biol. 139:1997;1243-1253.
18. DiNubile M.J. Erythrocyte membrane fractions contain free barbed filament ends despite sufficient concentrations of retained capper(s) to prevent barbed end growth. Cell Motil Cytoskeleton. 43:1999;10-22.
19. 2+ ghosts suggest that erythrocyte actin filaments are capped by adducin. Biochemistry. 36:1997;13461-13472.
20. 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. This paper describes evidence that capping protein is inhibited from binding to barbed ends that were induced by Cdc42 in a cell extract system of actin polymerization.
21. Hart M.C., Cooper J.A. Verterbrate isoforms of actin capping protein β have distinct functions in vivo. J Cell Biol. 147:1999;1287-1289.
22. Arcaro A. The small GTP-binding protein Rac promotes the dissociation of gelsolin from actin filaments in neutrophils. J Biol Chem. 273:1998;805-813.
23. Azuma T., Witke W., Stossel T.P., Hartwig J.H., Kwiatkowski D.J. Gelsolin is a downstream effector of rac for fibroblast motility. EMBO J. 17:1998;1362-1370.
24. Arora P.D., Janmey P.A., McCulloch C.A. A role for gelsolin in stress fiber-dependent cell contraction. Exp Cell Res. 250:1999;155-167.
25. Friederich E., Vancompernolle K., Louvard D., Vandekerckhove J. Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro. J Biol Chem. 274:1999;26751-26760.
26. Cant K., Knowles B.A., Mahajan-Miklos S., Heintzelman M., Cooley L. Drosophila fascin mutants are rescued by overexpression of the villin- like protein, quail. J Cell Sci. 111:1998;213-221.
27. Pinson K.I., Dunbar L., Samuelson L., Gumucio D.L. Targeted disruption of the mouse villin gene does not impair the morphogenesis of microvilli. Dev Dyn. 211:1998;109-121.
28. Ferrary E., Cohen-Tannoudji M., Pehau-Arnaudet G., Lapillonne A., Athman R., Ruiz T., Boulouha L., EI Marjou F., Doye A., Fontaine J.J.et al. In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders. J Cell Biol. 146:1999;819-830. The villin knockout mouse has normal actin bundles in microvilli of intestinal epithelia. However, the response of the epithelium to an injury that involves loss of actin is impaired in the villin knockout mouse. Thus, villin appears to play a role in disassembling actin filaments of the microvilli.
29. Marks P.W., Arai M., Bandura J.L., Kwiatkowski D.J. Advillin (p92): a new member of the gelsolin/villin family of actin regulatory proteins. J Cell Sci. 111:1998;2129-2136.
30. Wulfkuhle J.D., Donina I.E., Stark N.H., Pope R.K., Pestonjamasp K.N., Niswonger M.L., Luna E.J. Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals. J Cell Sci. 112:1999;2125-2136.
31. 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. Arp2/3 complex nucleates actin polymerization and caps pointed ends. It simultaneously binds the sides of actin filaments, creating a branching network.
32. 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. This is an elegant morphologic study of the actin filament network in the cortex of motile cells. Arp2/3 was found at branch points, similar to what was found with pure proteins.
33. Schafer D.A., Welch M.D., Machesky L.M., Bridgman P.C., Meyer S.M., Cooper J.A. Visualization and molecular analysis of actin assembly in living cells. J Cell Biol. 143:1998;1919-1930. Actin polymerization and motility visualized in living cells is associated with Arp2/3 and capping protein. The role of cofilin and signaling molecules is demonstrated.
34. Machesky L.M., Reeves E., Wientjes F., Mattheyse F.J., Grogan A., Totty N.F., Burlingame A.L., Hsuan J.J., Segal A.W. Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins. Biochem J. 328:1997;105-112.
35. Bailly M., Macaluso F., Cammer M., Chan A., Segall J.E., Condeelis J.S. Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation. J Cell Biol. 145:1999;331-345.
36. 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.
37. Machesky L.M., Mullins R.D., Higgs H.N., Kaiser D.A., Blanchoin L., May R.C., Hall M.E., Pollard T.B. Scar, a WASP-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc Natl Acad Sci USA. 96:1999;3739-3744. WASP family proteins stimulate the nucleation activity of Arp2/3 complex.
38. 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. WASP-coated beads polymerize actin and move in a cell extract. This activity requires Arp2/3 complex.
39. Mullins R.D., Pollard T.D. Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerizationin Acanthamoeba extracts. Curr Biol. 9:1999;405-415.
40. Ma L., Rohatgi R., Kirschner M.W. The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42. Proc Natl Acad Sci USA. 95:1998;15362-15377.
41. 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. N-WASP is necessary for the stimulation of actin polymerization by Cdc42 in a cell extract. N-WASP binds and stimulates Arp2/3 complex.
42. 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 (Wash DC). 281:1998;105-108. The Listeria surface protein ActA stimulates the nucleation activity of Arp2/3 complex.
43. May R.C., Hall M.E., Higgs H.N., Pollard T.D., Chakraborty T., Wehland J.et al. The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes. Curr Biol. 9:1999;759-762.
44. 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.
45. Winter D., Podtelejnikov A.V., Mann M., Li R. The complex containing actin-related proteins arp2 and arp3 is required for the motility and integrity of yeast actin patches. Curr Biol. 7:1997;519-529.
46. Belmont L.D., Drubin D.G. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J Cell Biol. 142:1998;1289-1299.
47. Lappalainen P., Drubin D.G. Cofilin promotes rapid actin filament turnover in vivo. Nature. 388:1997;78-82.
48. i- actin to ADP-actin at all pointed filament ends. J Biol Chem. 274:1999;34637-34645.
49. Almenar-Queralt A., Gregorio C.C., Fowler V.M. Tropomodulin assembles early in myofibrillogenesis in chick skeletal muscle: evidence that thin filaments rearrange to form striated myofibrils. J Cell Sci. 112:1999;1111-1123.
50. Skeath J.B., Doe C.Q. Sanpodo and Notch act in opposition to Numb to distinguish sibling neuron fates in the Drosophila CNS. Development. 125:1998;1857-1865.
51. Dye C.A., Lee J.K., Atkinson R.C., Brewster R., Han P.L., Bellen H.J. The Drosophila sanpodo gene controls sibling cell fate and encodes a tropomodulin homolog, an actin/tropomyosin-associated protein. Development. 125:1998;1845-1856.
52. Park M., Yaich L.E., Bodmer R. Mesodermal cell fate decisions in Drosophila are under the control of the lineage genes numb, Notch, and sanpodo. Mech Dev. 75:1998;117-126.
53. Fischer R., Lee A., Fowler V. Tropomodulin and tropomyosin help to reorganize the actin cytoskeleton during lens cell morphogenesis. Invest Ophthalmol Vis Sci. 2000;. in press.
54. 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.
55. 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. Severing by ADF/cofilin is more likely with long filaments than short ones. ADF/cofilin increases the dissociation of subunits from the pointed end.
56. Du J., Frieden C. Kinetic studies on the effect of yeast cofilin on yeas actin polymerization. Biochemistry. 37:1998;13276-13284.
57. Blanchoin L., Pollard T.D. Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments. J Biol Chem. 274:1999;15538-15546.
58. 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.
59. Ressad F., Didry D., Egile C., Pantaloni D., Carlier M.F. Control of actin filament length and turnover by actin depolymerizing factor (ADF/cofilin) in the presence of capping proteins and ARP2/3 complex. J Biol Chem. 274:1999;20970-20976.
60. Theriot J.A. Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton. J Cell Biol. 136:1997;1165-1168.
61. 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.
62. McGough A., Chiu W. ADF/cofilin weakens lateral contacts in the actin filament. J Mol Biol. 291:1999;513-519.
63. 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.
64. 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.
65. Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. Activation of LIM kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol. 1:1999;253-259. This paper shows that inhibition of cofilin by LIM kinase is linked to Rac via Pak1.
66. Maekawa M., Ishizaki T., Boku S., Watanabe N., Fujita A., Iwamatsu A., Obinata T., Ohashi K., Mizuno K., Narumiya S. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science. 285:1999;895-898. This paper shows that inhibition of cofilin by LIM kinase is linked to Rho via ROCK.
67. Rodal A.A., Tetreault J.W., Lappalainen P., Drubin D.G., Amberg D.C. Aip1p interacts with cofilin to disassemble actin filaments. J Cell Biol. 145:1999;1251-1264.
68. Okada K., Obinata T., Abe H. XAIP1: a Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins. J Cell Sci. 112:1999;1553-1565.
69. Konzok A., Weber I., Simmeth E., Hacker U., Maniak M., Muller-Taubenberger A. DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1, is involved in endocytosis, cytokinesis, and motility. J Cell Biol. 146:1999;453-464.
70. 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.
71. Didry D., Carlier M.F., Pantaloni D. Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J Biol Chem. 273:1998;25602-25611.
72. Heinzen R.A., Grieshaber S.S., Van Kirk L.S., Devin C.J. Dynamics of actin-based movement by Rickettsia rickettsii in vero cells. Infect Immun. 67:1999;4201-4207.
73. Gouin E., Gantelet H., Egile C., Lasa I., Ohayon H., Villiers V., Gounon P., Sansonetti P.S., Cossart P. A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii. J Cell Sci. 112:1999;1697-1708.