-
1
-
-
0024741693
-
Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes
-
Tilney L.G., Portnoy D.A. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol. 109:1989;1597-1608.
-
(1989)
J Cell Biol
, vol.109
, pp. 1597-1608
-
-
Tilney, L.G.1
Portnoy, D.A.2
-
2
-
-
0029589267
-
The cell biology of infection by intracellular bacterial pathogens
-
Theriot J. The cell biology of infection by intracellular bacterial pathogens. Annu Rev Cell Dev Biol. 11:1995;213-239.
-
(1995)
Annu Rev Cell Dev Biol
, vol.11
, pp. 213-239
-
-
Theriot, J.1
-
3
-
-
0032407404
-
Intracellular pathogens and the actin cytoskeleton
-
Dramsi S., Cossart P. Intracellular pathogens and the actin cytoskeleton. Annu Rev Cell Dev Biol. 14:1998;137-166.
-
(1998)
Annu Rev Cell Dev Biol
, vol.14
, pp. 137-166
-
-
Dramsi, S.1
Cossart, P.2
-
4
-
-
0033126054
-
Endocytic vesicles move at the tips of actin tails in cultured mast cells
-
This study demonstrates a rocketing motion of pinosomes after they pinch off from the membrane, suggesting that the rocketing motion of Listeria and other parasites through the cytoplasm may have an endogenous cellular equivalent
-
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. This study demonstrates a rocketing motion of pinosomes after they pinch off from the membrane, suggesting that the rocketing motion of Listeria and other parasites through the cytoplasm may have an endogenous cellular equivalent.
-
(1999)
Nat Cell Biol
, vol.1
, pp. 72-74
-
-
Merrifield, C.J.1
Moss, S.E.2
Ballestrem, C.3
Imhof, B.A.4
Giese, G.5
Wunderlich, I.6
Almers, W.7
-
5
-
-
0030474687
-
An Aplysia cell adhesion molecule associated with site-directed actin filament assembly in neuronal growth cones
-
Thompson C., Lin C.H., Forscher P. An Aplysia cell adhesion molecule associated with site-directed actin filament assembly in neuronal growth cones. J Cell Sci. 109:1996;2843-2854.
-
(1996)
J Cell Sci
, vol.109
, pp. 2843-2854
-
-
Thompson, C.1
Lin, C.H.2
Forscher, P.3
-
6
-
-
0032853428
-
Polymerizing microtubules activate site-directed F-actin assembly in nerve growth cones
-
Rochlin M.W., Dailey M.E., Bridgman P.C. Polymerizing microtubules activate site-directed F-actin assembly in nerve growth cones. Mol Biol Cell. 10:1999;2309-2327.
-
(1999)
Mol Biol Cell
, vol.10
, pp. 2309-2327
-
-
Rochlin, M.W.1
Dailey, M.E.2
Bridgman, P.C.3
-
7
-
-
0033143333
-
Spatial control of actin polymerization during neutrophil chemotaxis
-
Using chemotactic motility of neutrophils as a model system, the authors show that actin assembly in permeabilized cells and the distribution of the Arp2/3 complex are confined to discrete foci at the tips of radial actin projections. These findings raise the possibility that the neutrophil leading edge represents a collection of discrete foci of actin polymerization similar to those formed at the rear of Listeria
-
Weiner O.D., Guy Servant S., Welch M.D., Mitchison T.J., Sedat J.W., Bourne H.R. Spatial control of actin polymerization during neutrophil chemotaxis. Nat Cell Biol. 1:1999;75-81. Using chemotactic motility of neutrophils as a model system, the authors show that actin assembly in permeabilized cells and the distribution of the Arp2/3 complex are confined to discrete foci at the tips of radial actin projections. These findings raise the possibility that the neutrophil leading edge represents a collection of discrete foci of actin polymerization similar to those formed at the rear of Listeria.
-
(1999)
Nat Cell Biol
, vol.1
, pp. 75-81
-
-
Weiner, O.D.1
Guy Servant, S.2
Welch, M.D.3
Mitchison, T.J.4
Sedat, J.W.5
Bourne, H.R.6
-
8
-
-
0028173688
-
Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts
-
Theriot J.A., Rosenblatt J., Portnoy D.A., Goldschmidt-Clermont P.J., Mitchison T.J. Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts. Cell. 76:1994;505-5317.
-
(1994)
Cell
, vol.76
, pp. 505-5317
-
-
Theriot, J.A.1
Rosenblatt, J.2
Portnoy, D.A.3
Goldschmidt-Clermont, P.J.4
Mitchison, T.J.5
-
9
-
-
0032585538
-
Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
-
This study identifies cellular interacting partners of the Arp2/3 complex, which turn out to be proteins of the WASP family. Two members of this family, WASP itself and Scar1, directly bind the p21 subunit of the Arp2/3 complex and block lamellipodial formation upon overexpression in cultured cells. This finding opens the way for investigation of the Arp2/3 complex/WASP interaction from a biochemical point of view
-
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. This study identifies cellular interacting partners of the Arp2/3 complex, which turn out to be proteins of the WASP family. Two members of this family, WASP itself and Scar1, directly bind the p21 subunit of the Arp2/3 complex and block lamellipodial formation upon overexpression in cultured cells. This finding opens the way for investigation of the Arp2/3 complex/WASP interaction from a biochemical point of view.
-
(1998)
Curr Biol
, vol.8
, pp. 1347-1356
-
-
Machesky, L.M.1
Insall, R.H.2
-
10
-
-
0033616763
-
Scar, a WASP-related protein, activates nucleation of actin filaments by the Arp2/3 complex
-
••] showing that different members of the WASP family, in this case Scar, increase the nucleating activity of the Arp2/3 complex in vitro, which suggests that they may be cellular analogs of the listerial ActA protein. Importantly, the most efficient nucleation was observed after pre-incubation of Scar and Arp2/3 complex with actin filaments, suggesting a dendritic mechanism of nucleation in which assembly of new filaments occurs at the sides of pre-existing filaments
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••] showing that different members of the WASP family, in this case Scar, increase the nucleating activity of the Arp2/3 complex in vitro, which suggests that they may be cellular analogs of the listerial ActA protein. Importantly, the most efficient nucleation was observed after pre-incubation of Scar and Arp2/3 complex with actin filaments, suggesting a dendritic mechanism of nucleation in which assembly of new filaments occurs at the sides of pre-existing filaments.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 3739-3744
-
-
Machesky, L.M.1
Mullins, R.D.2
Higgs, H.N.3
Kaiser, D.A.4
Blanchoin, L.5
May, R.C.6
Hall, M.E.7
Pollard, T.D.8
-
12
-
-
0033528995
-
Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein
-
••]. In this case a yeast protein Bee1p/Las17p is shown to increase the nucleating activity of the Arp2/3 complex in vitro
-
••]. In this case a yeast protein Bee1p/Las17p is shown to increase the nucleating activity of the Arp2/3 complex in vitro.
-
(1999)
Curr Biol
, vol.9
, pp. 501-504
-
-
Winter, D.1
Lechler, T.2
Li, R.3
-
13
-
-
0033587188
-
The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex
-
••]. In this case WASP itself is shown to increase the nucleating activity of the Arp2/3 complex in vitro. In addition, motility of WASP-coated beads in cytoplasmic extracts is demonstrated in the presence, but not the absence, of the Arp2/3 complex
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••]. In this case WASP itself is shown to increase the nucleating activity of the Arp2/3 complex in vitro. In addition, motility of WASP-coated beads in cytoplasmic extracts is demonstrated in the presence, but not the absence, of the Arp2/3 complex.
-
(1999)
Curr Biol
, vol.9
, pp. 555-558
-
-
Yarar, D.1
To, W.2
Abo, A.3
Welch, M.D.4
-
14
-
-
0033005974
-
Regulation of cortical structure by the ezrin-radixin-moesin protein family
-
Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr Opin Cell Biol. 11:1999;109-116.
-
(1999)
Curr Opin Cell Biol
, vol.11
, pp. 109-116
-
-
Bretscher, A.1
-
15
-
-
0030908903
-
The isolated comet tail pseudopodium of Listeria monocytogenes: A tail of two actin filament populations, long and axial and short and random
-
Sechi A.S., Wehland J., Small J.V. The isolated comet tail pseudopodium of Listeria monocytogenes: a tail of two actin filament populations, long and axial and short and random. J Cell Biol. 137:1997;155-167.
-
(1997)
J Cell Biol
, vol.137
, pp. 155-167
-
-
Sechi, A.S.1
Wehland, J.2
Small, J.V.3
-
16
-
-
0033055077
-
Comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii
-
The actin-based motility of Rickettsia was compared with those of Listeria and Shigella. Striking differences were seen in the rate of movement, protein composition and structural organization of the tail, suggesting that Rickettsia may use a filopodial-type mechanism of motility in contrast to the apparently lamellipodial-type mechanism characteristic for the other two bacteria
-
Gouin E., Gantelet H., Egile C., Lasa I., Ohayon H., Villiers V., Gounon P., Sansonetti P.J., 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. The actin-based motility of Rickettsia was compared with those of Listeria and Shigella. Striking differences were seen in the rate of movement, protein composition and structural organization of the tail, suggesting that Rickettsia may use a filopodial-type mechanism of motility in contrast to the apparently lamellipodial-type mechanism characteristic for the other two bacteria.
-
(1999)
J Cell Sci
, vol.112
, pp. 1697-1708
-
-
Gouin, E.1
Gantelet, H.2
Egile, C.3
Lasa, I.4
Ohayon, H.5
Villiers, V.6
Gounon, P.7
Sansonetti, P.J.8
Cossart, P.A.9
-
17
-
-
0033040630
-
In vitro approaches to study actin and microtubule dependent cell processes
-
Moreau V., Way M. In vitro approaches to study actin and microtubule dependent cell processes. Curr Opin Cell Biol. 11:1999;152-158.
-
(1999)
Curr Opin Cell Biol
, vol.11
, pp. 152-158
-
-
Moreau, V.1
Way, M.2
-
18
-
-
0020334993
-
Bioenergetics and kinetics of microtubule and actin filament assembly and disassembly
-
Hill T., Kirschner M. Bioenergetics and kinetics of microtubule and actin filament assembly and disassembly. Int Rev Cytol. 78:1982;1-125.
-
(1982)
Int Rev Cytol
, vol.78
, pp. 1-125
-
-
Hill, T.1
Kirschner, M.2
-
19
-
-
0029775654
-
Cell motility driven by actin polymerization
-
Mogilner A., Oster G. Cell motility driven by actin polymerization. Biophys J. 71:1996;3030-3045.
-
(1996)
Biophys J
, vol.71
, pp. 3030-3045
-
-
Mogilner, A.1
Oster, G.2
-
20
-
-
0032819362
-
The actin-based nanomachine at the leading edge of migrating cells
-
Actin filament density in the lamellipodium is estimated by image-based photometry, and numerous biophysical parameters that are important for protrusive motility are computed
-
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. Actin filament density in the lamellipodium is estimated by image-based photometry, and numerous biophysical parameters that are important for protrusive motility are computed.
-
(1999)
Biophys J
, vol.77
, pp. 1721-1732
-
-
Abraham, V.C.1
Krishnamurthi, V.2
Taylor, D.L.3
Lanni, F.4
-
21
-
-
0033533789
-
Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
-
This paper is a major breakthrough in the field. The sustained motility of two types of bacteria is reconstituted in vitro from pure proteins. Arp2/3 complex, capping protein and cofilin are found to be necessary and sufficient for Listeria and N-WASP-coated Shigella movement. VASP significantly improved Listeria motility and profilin increased the rate of movement of both bacteria
-
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. This paper is a major breakthrough in the field. The sustained motility of two types of bacteria is reconstituted in vitro from pure proteins. Arp2/3 complex, capping protein and cofilin are found to be necessary and sufficient for Listeria and N-WASP-coated Shigella movement. VASP significantly improved Listeria motility and profilin increased the rate of movement of both bacteria.
-
(1999)
Nature
, vol.401
, pp. 613-616
-
-
Loisel, T.P.1
Boujemaa, R.2
Pantaloni, D.3
Carlier, M.-F.4
-
22
-
-
0032479578
-
Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
-
This work provides the first evidence that the intrinsically weak nucleating activity of the Arp2/3 complex can be activated and that Listeria protein ActA is a potent activator of the Arp2/3 complex
-
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. This work provides the first evidence that the intrinsically weak nucleating activity of the Arp2/3 complex can be activated and that Listeria protein ActA is a potent activator of the Arp2/3 complex.
-
(1998)
Science
, vol.281
, pp. 105-108
-
-
Welch, M.D.1
Rosenblatt, J.2
Skoble, J.3
Portnoy, D.A.4
Mitchison, T.J.5
-
23
-
-
0031021153
-
Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
-
Welch M.D., Iwamatsu A., Mitchison T.J. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature. 385:1997;265-269.
-
(1997)
Nature
, vol.385
, pp. 265-269
-
-
Welch, M.D.1
Iwamatsu, A.2
Mitchison, T.J.3
-
24
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0032525132
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Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri
-
This paper demonstrates that N-WASP is a critical host molecule recruited by Shigella to promote its intracellular motility
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Suzuki T., Miki H., Takenawa T., Sasakawa C. Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri. EMBO J. 17:1998;2767-2776. This paper demonstrates that N-WASP is a critical host molecule recruited by Shigella to promote its intracellular motility.
-
(1998)
EMBO J
, vol.17
, pp. 2767-2776
-
-
Suzuki, T.1
Miki, H.2
Takenawa, T.3
Sasakawa, C.4
-
25
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0033609062
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Motility of ActA protein-coated microspheres driven by actin polymerization
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Small synthetic beads coated with ActA are sufficient to induce rocket motility in cytoplasmic extracts. This paper investigates the significance of symmetry of coating and demonstrates that symmetry breaking and self-polarization are intrinsic properties of the actin machinery
-
Cameron L.A., Footer M.J., van Oudenaarden A., Theriot J.A. Motility of ActA protein-coated microspheres driven by actin polymerization. Proc Natl Acad Sci USA. 96:1999;4908-4913. Small synthetic beads coated with ActA are sufficient to induce rocket motility in cytoplasmic extracts. This paper investigates the significance of symmetry of coating and demonstrates that symmetry breaking and self-polarization are intrinsic properties of the actin machinery.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 4908-4913
-
-
Cameron, L.A.1
Footer, M.J.2
Van Oudenaarden, A.3
Theriot, J.A.4
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26
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0033594081
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Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes
-
This paper introduces the important idea that VASP may serve as a sliding connector which holds the barbed ends of growing actin filaments close to the bacterial surface
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Laurent V., Loisel T.P., Harbeck B., Wehman A., Grobe L., Jockusch B.M., Wehland J., Gertler F.B., Carlier M.F. Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. J Cell Biol. 144:1999;1245-1258. This paper introduces the important idea that VASP may serve as a sliding connector which holds the barbed ends of growing actin filaments close to the bacterial surface.
-
(1999)
J Cell Biol
, vol.144
, pp. 1245-1258
-
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Laurent, V.1
Loisel, T.P.2
Harbeck, B.3
Wehman, A.4
Grobe, L.5
Jockusch, B.M.6
Wehland, J.7
Gertler, F.B.8
Carlier, M.F.9
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27
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0033588990
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Activation of the Cdc42 effector N-WASP by the Shigella IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
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Using Shigella motility in platelet extracts as a model system, the authors identify new activities of N-WASP: a profilin-like activity of the carboxy-terminal VCA domain, and F-actin binding and stabilizing activity located at the amino terminus, which can be unmasked by Shigella protein IcsA
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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 IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J Cell Biol. 146:1999;1319-1332. Using Shigella motility in platelet extracts as a model system, the authors identify new activities of N-WASP: a profilin-like activity of the carboxy-terminal VCA domain, and F-actin binding and stabilizing activity located at the amino terminus, which can be unmasked by Shigella protein IcsA.
-
(1999)
J Cell Biol
, vol.146
, pp. 1319-1332
-
-
Egile, C.1
Loisel, T.P.2
Laurent, V.3
Li, R.4
Pantaloni, D.5
Sansonetti, P.J.6
Carlier, M.-F.7
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28
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0033082452
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Mena is required for neurulation and commissure formation
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This paper reports the generation of mice deficient in Mena (a protein related to VASP), which had problems with axon guidance. In wild-type cultured neurons, Mena localized to the tips of filopodia in growth cones distal to actin and proteins of the ezrin-radixin-moezin family
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Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M., Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B. Mena is required for neurulation and commissure formation. Neuron. 22:1999;313-325. This paper reports the generation of mice deficient in Mena (a protein related to VASP), which had problems with axon guidance. In wild-type cultured neurons, Mena localized to the tips of filopodia in growth cones distal to actin and proteins of the ezrin-radixin-moezin family.
-
(1999)
Neuron
, vol.22
, pp. 313-325
-
-
Lanier, L.M.1
Gates, M.A.2
Witke, W.3
Menzies, A.S.4
Wehman, A.M.5
Macklis, J.D.6
Kwiatkowski, D.7
Soriano, P.8
Gertler, F.B.9
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29
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0033194199
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VASP dynamics during lamellipodia protrusion
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The localization of GFP-VASP to lamellipodial and filopodial tips in locomoting cells is reported. Importantly, protruding lamellipodia contained VASP in amounts linearly related with the rate of protrusion
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Rottner K., Behrendt B., Small J.V., Wehland J. VASP dynamics during lamellipodia protrusion. Nat Cell Biol. 1:1999;321-322. The localization of GFP-VASP to lamellipodial and filopodial tips in locomoting cells is reported. Importantly, protruding lamellipodia contained VASP in amounts linearly related with the rate of protrusion.
-
(1999)
Nat Cell Biol
, vol.1
, pp. 321-322
-
-
Rottner, K.1
Behrendt, B.2
Small, J.V.3
Wehland, J.4
-
30
-
-
0031281898
-
Zyxin: Zinc fingers at sites of cell adhesion
-
Beckerle M.C. Zyxin: zinc fingers at sites of cell adhesion. Bioessays. 19:1997;949-957.
-
(1997)
Bioessays
, vol.19
, pp. 949-957
-
-
Beckerle, M.C.1
-
31
-
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0032872870
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Microtubule targeting of substrate contacts promotes their relaxation and dissociation
-
This paper is primarily about negative regulation of focal contacts by microtubules, but it also shows that GFP-zyxin is localized to focal contacts, but not the leading edge
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Kaverina I., Krylyshkina O., Small J.V. Microtubule targeting of substrate contacts promotes their relaxation and dissociation. J Cell Biol. 146:1999;1033-1044. This paper is primarily about negative regulation of focal contacts by microtubules, but it also shows that GFP-zyxin is localized to focal contacts, but not the leading edge.
-
(1999)
J Cell Biol
, vol.146
, pp. 1033-1044
-
-
Kaverina, I.1
Krylyshkina, O.2
Small, J.V.3
-
32
-
-
0033613455
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Actin-based motility of Vaccinia virus mimics receptor tyrosine kinase signalling
-
The authors identify a viral protein, A36R, that is essential for actin-tail assembly on Vaccinia particles and demonstrate that, after being tyrosine phosphorylated, A36R recruits an adapter protein, Nck, and N-WASP. These data place Vaccinia virus on the same signalling pathway leading to actin polymerization as Listeria or Shigella, but suggest that Vaccinia intervenes in this cellular pathway at an earlier step
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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. The authors identify a viral protein, A36R, that is essential for actin-tail assembly on Vaccinia particles and demonstrate that, after being tyrosine phosphorylated, A36R recruits an adapter protein, Nck, and N-WASP. These data place Vaccinia virus on the same signalling pathway leading to actin polymerization as Listeria or Shigella, but suggest that Vaccinia intervenes in this cellular pathway at an earlier step.
-
(1999)
Nature
, vol.401
, pp. 926-929
-
-
Frischknecht, F.1
Moreau, V.2
Rottger, S.3
Gonfloni, S.4
Reckmann, I.5
Superti Furga, G.6
Way, M.7
-
33
-
-
0028237089
-
Intact alpha-actinin molecules are needed for both the assembly of actin into the tails and the locomotion of Listeria monocytogenes inside infected cells
-
Dold F.G., Sanger J.M., Sanger J.W. Intact alpha-actinin molecules are needed for both the assembly of actin into the tails and the locomotion of Listeria monocytogenes inside infected cells. Cell Motil Cytoskeleton. 28:1994;97-107.
-
(1994)
Cell Motil Cytoskeleton
, vol.28
, pp. 97-107
-
-
Dold, F.G.1
Sanger, J.M.2
Sanger, J.W.3
-
34
-
-
0033040628
-
The Arp2/3 complex: A multifunctional actin organizer
-
A clear and concise review of the molecular interactions of the Arp2/3 complex
-
Machesky L.M., Gould K.L. The Arp2/3 complex: a multifunctional actin organizer. Curr Opin Cell Biol. 11:1999;117-121. A clear and concise review of the molecular interactions of the Arp2/3 complex.
-
(1999)
Curr Opin Cell Biol
, vol.11
, pp. 117-121
-
-
Machesky, L.M.1
Gould, K.L.2
-
35
-
-
0033231935
-
The world according to Arp: Regulation of actin nucleation by the Arp2/3 complex
-
Another clear review of the Arp2/3 complex, focusing on the molecular aspects of nucleation
-
Welch M.D. The world according to Arp: regulation of actin nucleation by the Arp2/3 complex. Trends Cell Biol. 9:1999;423-427. Another clear review of the Arp2/3 complex, focusing on the molecular aspects of nucleation.
-
(1999)
Trends Cell Biol
, vol.9
, pp. 423-427
-
-
Welch, M.D.1
-
36
-
-
0032568650
-
The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
-
This is the first demonstration that Arp2/3 complex can nucleate actin filaments and can cap pointed ends in addition to the binding of filament sides. The authors propose a dendritic nucleation model
-
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. This is the first demonstration that Arp2/3 complex can nucleate actin filaments and can cap pointed ends in addition to the binding of filament sides. The authors propose a dendritic nucleation model.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 6181-6186
-
-
Mullins, R.D.1
Heuser, J.A.2
Pollard, T.D.3
-
37
-
-
0033231171
-
Progress in protrusion: The tell-tale Scar
-
A discussion of how the actin machinery interprets signaling pathways to result in protrusion
-
Svitkina T.M., Borisy G.G. Progress in protrusion: the tell-tale Scar. Trends Biochem Sci. 24:1999;432-436. A discussion of how the actin machinery interprets signaling pathways to result in protrusion.
-
(1999)
Trends Biochem Sci
, vol.24
, pp. 432-436
-
-
Svitkina, T.M.1
Borisy, G.G.2
-
38
-
-
0033620689
-
Arp2/3 complex and ADF/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
-
This study demonstrates a highly branched organization of actin filaments in lamellipodia in situ. The Arp2/3 complex is localized to actin filament branch points consistent with the dendritic nucleation model. Compared with more posterior lamellipodial regions, the actin brush is significantly protected from depolymerization despite the presence of ADF/cofilin, suggesting that Arp2/3 complex functions as a pointed end capper in vivo. The authors propose an array treadmilling model for actin dynamics in lamellipodia
-
Svitkina T.M., Borisy G.G. Arp2/3 complex and ADF/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J Cell Biol. 145:1999;1009-1026. This study demonstrates a highly branched organization of actin filaments in lamellipodia in situ. The Arp2/3 complex is localized to actin filament branch points consistent with the dendritic nucleation model. Compared with more posterior lamellipodial regions, the actin brush is significantly protected from depolymerization despite the presence of ADF/cofilin, suggesting that Arp2/3 complex functions as a pointed end capper in vivo. The authors propose an array treadmilling model for actin dynamics in lamellipodia.
-
(1999)
J Cell Biol
, vol.145
, pp. 1009-1026
-
-
Svitkina, T.M.1
Borisy, G.G.2
-
39
-
-
0026719663
-
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
-
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.
-
(1992)
J Cell Biol
, vol.118
, pp. 71-81
-
-
Tilney, L.G.1
Derosier, D.J.2
Tilney, M.S.3
-
40
-
-
0028945221
-
Organization and structure of actin filament bundles in Listeria-infected cells
-
Zhukarev V., Ashton F., Sanger J.M., Sanger J.W., Shuman H. Organization and structure of actin filament bundles in Listeria-infected cells. Cell Motil Cytoskeleton. 30:1995;229-246.
-
(1995)
Cell Motil Cytoskeleton
, vol.30
, pp. 229-246
-
-
Zhukarev, V.1
Ashton, F.2
Sanger, J.M.3
Sanger, J.W.4
Shuman, H.5
-
41
-
-
0032768668
-
Dynamics of actin-based movement by Rickettsia rickettsii in Vero cells
-
Analysis of actin dynamics in comet tails induced by Rickettsia in cells expressing GFP-actin fusion protein demonstrates a much slower rate of actin turnover as compared with Listeria tails, suggesting a different mechanism of actin disassembly in the two systems
-
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. Analysis of actin dynamics in comet tails induced by Rickettsia in cells expressing GFP-actin fusion protein demonstrates a much slower rate of actin turnover as compared with Listeria tails, suggesting a different mechanism of actin disassembly in the two systems.
-
(1999)
Infect Immun
, vol.67
, pp. 4201-4207
-
-
Heinzen, R.A.1
Grieshaber, S.S.2
Van Kirk, L.S.3
Devin, C.J.4
-
42
-
-
0032825265
-
Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction
-
Treadmilling of actin in growth-cone filopodia is demonstrated using photobleaching and photoactivation techniques, and important characteristics of end behavior are presented. Barbed ends display fluctuating rates of elongation, but no disassembly is obvious. Persistence of fluorescent marks suggests a low level of actin depolymerization along the length of filopodia
-
Mallavarapu A., Mitchison T.J. Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction. J Cell Biol. 146:1999;1097-1106. Treadmilling of actin in growth-cone filopodia is demonstrated using photobleaching and photoactivation techniques, and important characteristics of end behavior are presented. Barbed ends display fluctuating rates of elongation, but no disassembly is obvious. Persistence of fluorescent marks suggests a low level of actin depolymerization along the length of filopodia.
-
(1999)
J Cell Biol
, vol.146
, pp. 1097-1106
-
-
Mallavarapu, A.1
Mitchison, T.J.2
-
43
-
-
0033529192
-
Arrangement of radial actin bundles in the growth cone of Aplysia bag cell neurons shows the immediate past history of filopodial behavior
-
Using a new type of polarized-light microscope, which displays the birefringent structure of living cells at high resolution, the authors analyze kymograms of time-lapse images of filopodial actin bundles in Aplysia growth cones, providing strong indication of actin treadmilling in these structures
-
Katoh K., Hammar K., Smith P.J., Oldenbourg R. Arrangement of radial actin bundles in the growth cone of Aplysia bag cell neurons shows the immediate past history of filopodial behavior. Proc Natl Acad Sci USA. 96:1999;7928-7931. Using a new type of polarized-light microscope, which displays the birefringent structure of living cells at high resolution, the authors analyze kymograms of time-lapse images of filopodial actin bundles in Aplysia growth cones, providing strong indication of actin treadmilling in these structures.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 7928-7931
-
-
Katoh, K.1
Hammar, K.2
Smith, P.J.3
Oldenbourg, R.4
-
44
-
-
0031908252
-
EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells
-
Chan A.Y., Raft S., Bailly M., Wyckoff J.B., Segall J.E., Condeelis J.S. EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells. J Cell Sci. 111:1998;199-211.
-
(1998)
J Cell Sci
, vol.111
, pp. 199-211
-
-
Chan, A.Y.1
Raft, S.2
Bailly, M.3
Wyckoff, J.B.4
Segall, J.E.5
Condeelis, J.S.6
-
45
-
-
0344299281
-
Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation
-
High-resolution localization of actin filament barbed ends which are able to assemble exogenous actin is performed in lamellipodia of epidermal growth factor stimulated cells. Open barbed ends are found only within 100-200 nm from the leading edge, whereas Arp2/3 complex has a broader distribution, suggesting that Arp2/3 complex may lose its nucleating activity away from the membrane
-
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. High-resolution localization of actin filament barbed ends which are able to assemble exogenous actin is performed in lamellipodia of epidermal growth factor stimulated cells. Open barbed ends are found only within 100-200 nm from the leading edge, whereas Arp2/3 complex has a broader distribution, suggesting that Arp2/3 complex may lose its nucleating activity away from the membrane.
-
(1999)
J Cell Biol
, vol.145
, pp. 331-345
-
-
Bailly, M.1
Macaluso, F.2
Cammer, M.3
Chan, A.4
Segall, J.E.5
Condeelis, J.S.6
-
46
-
-
0029117595
-
Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
-
Hartwig J.H., Bokoch G.M., Carpenter C.L., Janmey P.A., Taylor L.A., Toker A., Stossel T.P. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell. 82:1995;643-653.
-
(1995)
Cell
, vol.82
, pp. 643-653
-
-
Hartwig, J.H.1
Bokoch, G.M.2
Carpenter, C.L.3
Janmey, P.A.4
Taylor, L.A.5
Toker, A.6
Stossel, T.P.7
-
47
-
-
0029954225
-
Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
-
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.
-
(1996)
J Cell Biol
, vol.134
, pp. 389-399
-
-
Barkalow, K.1
Witke, W.2
Kwiatkowski, D.J.3
Hartwig, J.H.4
-
48
-
-
0028797231
-
Getting the actin filaments straight: Nucleation-release or treadmilling?
-
Small J.V. Getting the actin filaments straight: nucleation-release or treadmilling? Trends Cell Biol. 5:1995;52-55.
-
(1995)
Trends Cell Biol
, vol.5
, pp. 52-55
-
-
Small, J.V.1
-
51
-
-
0033198879
-
Putting a new twist on actin: ADF/cofilins modulate actin dynamics
-
An up-to-date review addressing aspects of ADF/cofilin structure, dynamics, regulation and function
-
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. An up-to-date review addressing aspects of ADF/cofilin structure, dynamics, regulation and function.
-
(1999)
Trends Cell Biol
, vol.9
, pp. 364-370
-
-
Bamburg, J.R.1
McGough, A.2
Ono, S.3
-
52
-
-
0032971134
-
Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms
-
A biochemically-orientated discussion of how different actin-binding proteins control actin assembly and disassembly by altering the critical concentration and by changing the kinetics of polymerization
-
Weber A. Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms. Mol Cell Biochem. 190:1999;67-74. A biochemically-orientated discussion of how different actin-binding proteins control actin assembly and disassembly by altering the critical concentration and by changing the kinetics of polymerization.
-
(1999)
Mol Cell Biochem
, vol.190
, pp. 67-74
-
-
Weber, A.1
-
53
-
-
0032475981
-
Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover
-
Kinetic studies show that profilin, by blocking the back association reaction at the pointed end, increases the net dissociation rate and, therefore, working together with cofilin, speeds up the turnover of actin filaments up to 125-fold as compared with pure actin filaments
-
Didry D., Carlier M-F., Pantaloni D. Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J Biol Chem. 278:1998;25602-25611. Kinetic studies show that profilin, by blocking the back association reaction at the pointed end, increases the net dissociation rate and, therefore, working together with cofilin, speeds up the turnover of actin filaments up to 125-fold as compared with pure actin filaments.
-
(1998)
J Biol Chem
, vol.278
, pp. 25602-25611
-
-
Didry, D.1
Carlier, M.-F.2
Pantaloni, D.3
-
54
-
-
0030843484
-
Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
-
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.
-
(1997)
J Cell Biol
, vol.136
, pp. 1307-1322
-
-
Carlier, M.-F.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
-
55
-
-
0030821155
-
Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails
-
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.
-
(1997)
J Cell Biol
, vol.136
, pp. 1323-1332
-
-
Rosenblatt, J.1
Agnew, B.J.2
Abe, H.3
Bamburg, J.R.4
Mitchison, T.J.5
-
56
-
-
0030798735
-
Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton
-
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.
-
(1997)
J Cell Biol
, vol.136
, pp. 1165-1168
-
-
Theriot, J.A.1
-
57
-
-
0031887131
-
How ADF/cofilin depolymerizes actin filaments
-
Maciver S.K. How ADF/cofilin depolymerizes actin filaments. Curr Opin Cell Biol. 10:1998;140-144.
-
(1998)
Curr Opin Cell Biol
, vol.10
, pp. 140-144
-
-
Maciver, S.K.1
-
58
-
-
0033060250
-
Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments
-
A systematic comparison of the interaction of ADF/cofilin with cytoplasmic and muscle actin filaments. Evidence is presented that ADF/cofilin binds cooperatively to muscle but not to cytoplasmic actin filaments and that the higher affinity for ADP as opposed to ATP actin provides the thermodynamic driving force for disassembly
-
Blanchoin L., Pollard T.D. Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J Biol Chem. 274:1999;15538-15546. A systematic comparison of the interaction of ADF/cofilin with cytoplasmic and muscle actin filaments. Evidence is presented that ADF/cofilin binds cooperatively to muscle but not to cytoplasmic actin filaments and that the higher affinity for ADP as opposed to ATP actin provides the thermodynamic driving force for disassembly.
-
(1999)
J Biol Chem
, vol.274
, pp. 15538-15546
-
-
Blanchoin, L.1
Pollard, T.D.2
-
59
-
-
0032695844
-
Profilin is predominantly associated with monomeric actin in Acanthamoeba
-
Cell fractionation and immunolabeling studies show that profilin is distributed throughout the cytoplasm, not only at the leading edge as previously thought. Furthermore, its primary binding partner in situ is actin
-
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. Cell fractionation and immunolabeling studies show that profilin is distributed throughout the cytoplasm, not only at the leading edge as previously thought. Furthermore, its primary binding partner in situ is actin.
-
(1999)
J Cell Sci
, vol.112
, pp. 3779-3790
-
-
Kaiser, D.A.1
Vinson, V.K.2
Murphy, D.B.3
Pollard, T.D.4
-
60
-
-
0032566659
-
Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
-
Binding studies show that ADF/cofilin and profilin compete for binding actin monomers
-
Blanchoin L., Pollard T.D. Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. J Biol Chem. 273:1998;25106-25111. Binding studies show that ADF/cofilin and profilin compete for binding actin monomers.
-
(1998)
J Biol Chem
, vol.273
, pp. 25106-25111
-
-
Blanchoin, L.1
Pollard, T.D.2
-
61
-
-
0029612323
-
Control of actin assembly at filament ends
-
Schafer D.A., Cooper J.A. Control of actin assembly at filament ends. Annu Rev Cell Dev Biol. 11:1995;497-518.
-
(1995)
Annu Rev Cell Dev Biol
, vol.11
, pp. 497-518
-
-
Schafer, D.A.1
Cooper, J.A.2
-
62
-
-
0032576597
-
Visualization and molecular analysis of actin assembly in living cells
-
Using GFP-tagged proteins, the authors study the distribution and dynamics of capping protein in crawling cells and demonstrate its colocalization with the Arp2/3 complex and with sites of actin assembly in permeabilized cells in lamellipodia and numerous spots throughout the lamella. These findings suggest that capping protein is an integral part of the protrusive mechanism rather than a means to stop actin polymerization
-
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. Using GFP-tagged proteins, the authors study the distribution and dynamics of capping protein in crawling cells and demonstrate its colocalization with the Arp2/3 complex and with sites of actin assembly in permeabilized cells in lamellipodia and numerous spots throughout the lamella. These findings suggest that capping protein is an integral part of the protrusive mechanism rather than a means to stop actin polymerization.
-
(1998)
J Cell Biol
, vol.143
, pp. 1919-1930
-
-
Schafer, D.A.1
Welch, M.D.2
Machesky, L.M.3
Bridgman, P.C.4
Meyer, S.M.5
Cooper, J.A.6
-
63
-
-
0027489905
-
Focusing on unpolymerized actin
-
Fechheimer M., Zigmond S.H. Focusing on unpolymerized actin. J Cell Biol. 123:1993;1-5.
-
(1993)
J Cell Biol
, vol.123
, pp. 1-5
-
-
Fechheimer, M.1
Zigmond, S.H.2
-
64
-
-
0031580210
-
Control of actin dynamics in cell motility
-
Carlier M-F., Pantaloni D. Control of actin dynamics in cell motility. J Mol Biol. 269:1997;459-467.
-
(1997)
J Mol Biol
, vol.269
, pp. 459-467
-
-
Carlier, M.-F.1
Pantaloni, D.2
-
65
-
-
0032006817
-
Control of actin dynamics
-
Carlier M-F. Control of actin dynamics. Curr Opin Cell Biol. 10:1998;45-51.
-
(1998)
Curr Opin Cell Biol
, vol.10
, pp. 45-51
-
-
Carlier, M.-F.1
-
66
-
-
0029965630
-
How profilin/barbed-end synergy controls actin polymerization: A kinetic model of the ATP hydrolysis circuit
-
Dufort P.A., Lumsden C.J. How profilin/barbed-end synergy controls actin polymerization: a kinetic model of the ATP hydrolysis circuit. Cell Motil Cytoskeleton. 35:1996;309-330.
-
(1996)
Cell Motil Cytoskeleton
, vol.35
, pp. 309-330
-
-
Dufort, P.A.1
Lumsden, C.J.2
-
67
-
-
0033568844
-
Calcium influx alters actin bundle dynamics and retrograde flow in helisoma growth cones
-
Welnhofer E.A., Zhao L., Cohan C.S. Calcium influx alters actin bundle dynamics and retrograde flow in helisoma growth cones. J Neurosci. 19:1999;7971-7982.
-
(1999)
J Neurosci
, vol.19
, pp. 7971-7982
-
-
Welnhofer, E.A.1
Zhao, L.2
Cohan, C.S.3
-
68
-
-
0032473498
-
Gelsolin is a downstream effector of rac for fibroblast motility
-
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;1361-1370.
-
(1998)
EMBO J
, vol.17
, pp. 1361-1370
-
-
Azuma, T.1
Witke, W.2
Stossel, T.P.3
Hartwig, J.H.4
Kwiatkowski, D.J.5
-
69
-
-
0030754673
-
Delayed retraction of filopodia in gelsolin null mice
-
Lu M., Witke W., Kwiatkowski D.J., Kosik K.S. Delayed retraction of filopodia in gelsolin null mice. J Cell Biol. 138:1997;1279-1287.
-
(1997)
J Cell Biol
, vol.138
, pp. 1279-1287
-
-
Lu, M.1
Witke, W.2
Kwiatkowski, D.J.3
Kosik, K.S.4
-
70
-
-
0033539020
-
Cdc42-induced actin filaments are protected from capping protein
-
The length distribution of actin filaments induced in cytoplasmic extracts by Cdc42, surprisingly, is not affected by depletion or doubling the concentration of capping protein, in contrast to actin filaments polymerized on external actin-spectrin seeds in the same extracts. These data suggest protection from capping of filaments induced to polymerize by a Cdc42-dependent mechanism
-
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. The length distribution of actin filaments induced in cytoplasmic extracts by Cdc42, surprisingly, is not affected by depletion or doubling the concentration of capping protein, in contrast to actin filaments polymerized on external actin-spectrin seeds in the same extracts. These data suggest protection from capping of filaments induced to polymerize by a Cdc42-dependent mechanism.
-
(1999)
Curr Biol
, vol.9
, pp. 979-982
-
-
Huang, M.1
Yang, C.2
Schafer, D.A.3
Cooper, J.A.4
Higgs, H.N.5
Zigmond, S.H.6
-
71
-
-
0033597934
-
Control of actin filament length and turnover by actin depolymerizing factor (ADF/cofilin) in the presence of capping proteins and ARP2/3 complex
-
Kinetic analysis of actin turnover demonstrates that Arp23 complex inhibits ADF/cofilin enhanced turnover but does not block it, suggesting that the Arp2/3 complex may be not a perfect pointed end capper
-
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. Kinetic analysis of actin turnover demonstrates that Arp23 complex inhibits ADF/cofilin enhanced turnover but does not block it, suggesting that the Arp2/3 complex may be not a perfect pointed end capper.
-
(1999)
J Biol Chem
, vol.274
, pp. 20970-20976
-
-
Ressad, F.1
Didry, D.2
Egile, C.3
Pantaloni, D.4
Carlier, M.-F.5
-
72
-
-
0025740949
-
Actin microfilament dynamics in locomoting cells
-
Theriot J.A., Mitchison T.J. Actin microfilament dynamics in locomoting cells. Nature. 352:1991;126-131.
-
(1991)
Nature
, vol.352
, pp. 126-131
-
-
Theriot, J.A.1
Mitchison, T.J.2
-
73
-
-
0033619258
-
Myosin VI is an actin-based motor that moves backwards
-
The title says it all. An astonishing result showing the first example of a member of the myosin superfamily that has a force polarity directed towards the pointed end
-
Wells A.L., Lin A.W., Chen L.Q., Safer D., Cain S.M., Hasson T., Carragher B.O., Milligan R.A., Sweeney H.L. Myosin VI is an actin-based motor that moves backwards. Nature. 401:1999;505-508. The title says it all. An astonishing result showing the first example of a member of the myosin superfamily that has a force polarity directed towards the pointed end.
-
(1999)
Nature
, vol.401
, pp. 505-508
-
-
Wells, A.L.1
Lin, A.W.2
Chen, L.Q.3
Safer, D.4
Cain, S.M.5
Hasson, T.6
Carragher, B.O.7
Milligan, R.A.8
Sweeney, H.L.9
-
74
-
-
0032254074
-
Subcellular tension fields and mechanical resistance of the lamella front related to the direction of locomotion
-
Bereiter-Hahn J., Luers H. Subcellular tension fields and mechanical resistance of the lamella front related to the direction of locomotion. Cell Biochem Biophys. 29:1998;243-262.
-
(1998)
Cell Biochem Biophys
, vol.29
, pp. 243-262
-
-
Bereiter-Hahn, J.1
Luers, H.2
|