-
1
-
-
0029775654
-
Cell motility driven by actin polymerization
-
of outstanding interest. The 'Brownian ratchet' model [54] is extended to include the elastic properties of actin filaments in generating propulsive force. The velocity of a polymerizing filament tip is calculated as a function of the load and of the angle of the filament to the load. The calculated value matches the measured rate of Listeria movement, assuming that the steady-state concentration of ATP·G-Actin is ≈10μM. The calculated value predicts a 'critical angle' of 48°, for fast rate of lamellipodium protusion, which is close to the observed orthogonal arrangements of filaments in lamellipodia [6].
-
Mogilner A, Oster G. Cell motility driven by actin polymerization. of outstanding interest Biophys J. 71:1996;3030-3045 The 'Brownian ratchet' model [54] is extended to include the elastic properties of actin filaments in generating propulsive force. The velocity of a polymerizing filament tip is calculated as a function of the load and of the angle of the filament to the load. The calculated value matches the measured rate of Listeria movement, assuming that the steady-state concentration of ATP·G-Actin is ≈10μM. The calculated value predicts a 'critical angle' of 48°, for fast rate of lamellipodium protusion, which is close to the observed orthogonal arrangements of filaments in lamellipodia [6].
-
(1996)
Biophys J
, vol.71
, pp. 3030-3045
-
-
Mogilner, A.1
Oster, G.2
-
2
-
-
0017176529
-
Head to tail polymerization of actin
-
Wegner A. Head to tail polymerization of actin. J Mol Biol. 108:1976;139-150.
-
(1976)
J Mol Biol
, vol.108
, pp. 139-150
-
-
Wegner, A.1
-
3
-
-
0022390903
-
Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
-
Wang Y. Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J Cell Biol. 101:1985;597-602.
-
(1985)
J Cell Biol
, vol.101
, pp. 597-602
-
-
Wang, Y.1
-
4
-
-
0024426297
-
Incorporation and turnover of biotinlabeled actin microinjected into fibroblastic cells: An immunoelectron microscopic study
-
Okabe S, Hirokawa N. Incorporation and turnover of biotinlabeled actin microinjected into fibroblastic cells: an immunoelectron microscopic study. J Cell Biol. 109:1989;1581-1595.
-
(1989)
J Cell Biol
, vol.109
, pp. 1581-1595
-
-
Okabe, S.1
Hirokawa, N.2
-
5
-
-
0025785552
-
Control of actin polymerization in live and permeabilized fibroblasts
-
Symons MH, Mitchison TJ. Control of actin polymerization in live and permeabilized fibroblasts. J Cell Biol. 114:1991;503-513.
-
(1991)
J Cell Biol
, vol.114
, pp. 503-513
-
-
Symons, M.H.1
Mitchison, T.J.2
-
6
-
-
0028797231
-
Getting the actin filaments straight: Nucleation-release or treadmilling
-
Small JV. 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
-
7
-
-
0030978526
-
High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
-
of outstanding interest. These authors are pioneering in showing that a nonmotile organism such as yeast has a dynamic actin cytoskeleton. Latrunculin-A, an actin-depolymerizing drug, causes rapid disassembly of the actin cytoskeleton. Interestingly, the drug enables the probing of cellular functions in which actin is involved, such as endocytosis, bud formation, cell polarity and polarized location of some regulatory proteins (Abp1p, cofilin, sec4p, sec8p and Smy1p).
-
Ayscough KR, Stryker J, Pokala N, Sanders M, Crews P, Drubin DG. High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. of outstanding interest J Cell Biol. 137:1997;399-416 These authors are pioneering in showing that a nonmotile organism such as yeast has a dynamic actin cytoskeleton. Latrunculin-A, an actin-depolymerizing drug, causes rapid disassembly of the actin cytoskeleton. Interestingly, the drug enables the probing of cellular functions in which actin is involved, such as endocytosis, bud formation, cell polarity and polarized location of some regulatory proteins (Abp1p, cofilin, sec4p, sec8p and Smy1p).
-
(1997)
J Cell Biol
, vol.137
, pp. 399-416
-
-
Ayscough, K.R.1
Stryker, J.2
Pokala, N.3
Sanders, M.4
Crews, P.5
Drubin, D.G.6
-
8
-
-
0025949804
-
Role of the N- And C-terminal actin-binding domains of gelsolin in barbed end capping
-
Weber A, Pring M, Lin SL, Bryan J. Role of the N- and C-terminal actin-binding domains of gelsolin in barbed end capping. Biochemistry. 30:1991;9327-9334.
-
(1991)
Biochemistry
, vol.30
, pp. 9327-9334
-
-
Weber, A.1
Pring, M.2
Lin, S.L.3
Bryan, J.4
-
10
-
-
0024632296
-
A Dityostelium mutant deficient in severin, an F-actin fragmenting protein, shows normal motility and chemotaxis
-
Andre E, Brink M, Gerisch G, Isenberg G, Noegel A, Schleicher M, Segall JE, Wallraff E. A Dityostelium mutant deficient in severin, an F-actin fragmenting protein, shows normal motility and chemotaxis. J Cell Biol. 108:1989;985-995.
-
(1989)
J Cell Biol
, vol.108
, pp. 985-995
-
-
Andre, E.1
Brink, M.2
Gerisch, G.3
Isenberg, G.4
Noegel, A.5
Schleicher, M.6
Segall, J.E.7
Wallraff, E.8
-
11
-
-
0028914814
-
Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
-
Witke W, Sharpe A, Hartwig J, Azuma T, Stossel T, Kwiatkowski D. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell. 81:1995;41-51.
-
(1995)
Cell
, vol.81
, pp. 41-51
-
-
Witke, W.1
Sharpe, A.2
Hartwig, J.3
Azuma, T.4
Stossel, T.5
Kwiatkowski, D.6
-
12
-
-
0030821155
-
Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails
-
of special interest. Immunodepletion of actin-depolymerizing factor (ADF)/cofilin from Xenopus egg extracts causes an increase in the length of actin tails at the rear of Listeria. Immunodepletion of gelsolin does not affect movement of Listeria. Adding back ADF, but not the Ser3→Glu ADF mutant, restores the control tail length. The authors conclude that ADF, but not gelsolin, increases the rate of depolymerization of actin filaments in the actin tails.
-
Rosenblatt J, Agnew BJ, Abe H, Bamburg JR, Mitchison TJ. Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails. of special interest J Cell Biol. 136:1997;1323-1332 Immunodepletion of actin-depolymerizing factor (ADF)/cofilin from Xenopus egg extracts causes an increase in the length of actin tails at the rear of Listeria. Immunodepletion of gelsolin does not affect movement of Listeria. Adding back ADF, but not the Ser3→Glu ADF mutant, restores the control tail length. The authors conclude that ADF, but not gelsolin, increases the rate of depolymerization of actin filaments in the actin tails.
-
(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
-
13
-
-
0029896597
-
Actin organization, bristle morphology, and viability are affected by actin capping protein mutations in Drosophila
-
of special interest. This is the first report that capping protein (CP) has an essential function in a multicellular organism. Reduced levels of CP in viable transheterozygous adults lead to defects in the organization of actin bundles in the bristles, causing abnormal morphology. The apparent increased amount of actin assembled in bundles may be consistent with a relatively low concentration of stady-state ATP·G-actin which results from incomplete capping.
-
Hopmann R, Cooper J, Miller K. Actin organization, bristle morphology, and viability are affected by actin capping protein mutations in Drosophila. of special interest J Cell Biol. 133:1996;1293-1305 This is the first report that capping protein (CP) has an essential function in a multicellular organism. Reduced levels of CP in viable transheterozygous adults lead to defects in the organization of actin bundles in the bristles, causing abnormal morphology. The apparent increased amount of actin assembled in bundles may be consistent with a relatively low concentration of stady-state ATP·G-actin which results from incomplete capping.
-
(1996)
J Cell Biol
, vol.133
, pp. 1293-1305
-
-
Hopmann, R.1
Cooper, J.2
Miller, K.3
-
14
-
-
0029065328
-
Capping protein levels influence actin assembly and cell motility in Dictyostelium
-
Hug C, Jay P, Reddy I, McNally J, Bridgman P, Elson E, Cooper J. Capping protein levels influence actin assembly and cell motility in Dictyostelium. Cell. 81:1995;591-600.
-
(1995)
Cell
, vol.81
, pp. 591-600
-
-
Hug, C.1
Jay, P.2
Reddy, I.3
McNally, J.4
Bridgman, P.5
Elson, E.6
Cooper, J.7
-
15
-
-
0025782925
-
Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin
-
Cunningham C, Stossel T, Kwiatkowski D. Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin. Science. 251:1991;1233-1236.
-
(1991)
Science
, vol.251
, pp. 1233-1236
-
-
Cunningham, C.1
Stossel, T.2
Kwiatkowski, D.3
-
16
-
-
0023780588
-
Predominant induction of gelsolin and actin-binding protein during myeloid differentiation
-
Kwiatkowski DJ. Predominant induction of gelsolin and actin-binding protein during myeloid differentiation. J Biol Chem. 263:1988;13857-13862.
-
(1988)
J Biol Chem
, vol.263
, pp. 13857-13862
-
-
Kwiatkowski, D.J.1
-
17
-
-
0029787092
-
Dependence of fibroblast migration on actin severing activity of gelsolin
-
Arora P, McCulloch C. Dependence of fibroblast migration on actin severing activity of gelsolin. J Biol Chem. 271:1996;20516-20523.
-
(1996)
J Biol Chem
, vol.271
, pp. 20516-20523
-
-
Arora, P.1
McCulloch, C.2
-
18
-
-
0028941257
-
Effects of CapG overexpression on agonist-induced motility and second messenger generation
-
Sun H, Kwiatkowska K, Wooten D, Yin H. Effects of CapG overexpression on agonist-induced motility and second messenger generation. J Cell Biol. 129:1995;147-156.
-
(1995)
J Cell Biol
, vol.129
, pp. 147-156
-
-
Sun, H.1
Kwiatkowska, K.2
Wooten, D.3
Yin, H.4
-
19
-
-
0029965630
-
How profilin/barbed-end synergy controls actin polymerization: A kinetic model of the ATP hydrolysis circuit
-
of special interest. This computer simulation study reveals the interesting point that if barbed ends are suddenly made available in a population of capped filaments, they grow at a fast rate.
-
Dufort PA, Lumsden CJ. How profilin/barbed-end synergy controls actin polymerization: a kinetic model of the ATP hydrolysis circuit. of special interest Cell Motil Cytoskeleton. 35:1996;309-330 This computer simulation study reveals the interesting point that if barbed ends are suddenly made available in a population of capped filaments, they grow at a fast rate.
-
(1996)
Cell Motil Cytoskeleton
, vol.35
, pp. 309-330
-
-
Dufort, P.A.1
Lumsden, C.J.2
-
20
-
-
0031580210
-
Control of actin dynamics in cell motility
-
of special interest. Shows how the treadmilling of actin filaments can be biased towards uncapped barbed ends by capping proteins and enhanced by actin-depolymerizing factor/cofilin, which act in a cumulative fashion to quantitatively account for the fast rates of barbed end growth observed in vivo in actin-based motility processes (lamellipodium protusion or Listeria movement).
-
Carlier MF, Pantaloni D. Control of actin dynamics in cell motility. of special interest J Mol Biol. 269:1997;459 Shows how the treadmilling of actin filaments can be biased towards uncapped barbed ends by capping proteins and enhanced by actin-depolymerizing factor/cofilin, which act in a cumulative fashion to quantitatively account for the fast rates of barbed end growth observed in vivo in actin-based motility processes (lamellipodium protusion or Listeria movement).
-
(1997)
J Mol Biol
, vol.269
, pp. 459
-
-
Carlier, M.F.1
Pantaloni, D.2
-
21
-
-
0029117595
-
Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
-
Hartwig J, Bokoch G, Carpenter C, Janmey P, Taylor L, Toker A, Stossel T. 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.1
Bokoch, G.2
Carpenter, C.3
Janmey, P.4
Taylor, L.5
Toker, A.6
Stossel, T.7
-
22
-
-
0029795850
-
Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphosphoinositides
-
of special interest. The kinetics of capping protein (CP) association with/dissociation from barbed actin filament ends in vitro are relatively slow. The interesting consequence is that the kinetics of association of CP with growing barbed ends may by themselves control the length of actin filaments in vivo. Phosphatidylinositol 4,5-bisophosphate efficiently and rapidly dissociates CP from barbed ends. Possible models for the regulation of capping/uncapping/nucleation in actin-based motility are discussed in this paper.
-
Schafer DA, Jennings PB, Cooper JA. Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides. of special interest J Cell Biol. 135:1996;169-179 The kinetics of capping protein (CP) association with/dissociation from barbed actin filament ends in vitro are relatively slow. The interesting consequence is that the kinetics of association of CP with growing barbed ends may by themselves control the length of actin filaments in vivo. Phosphatidylinositol 4,5-bisophosphate efficiently and rapidly dissociates CP from barbed ends. Possible models for the regulation of capping/uncapping/nucleation in actin-based motility are discussed in this paper.
-
(1996)
J Cell Biol
, vol.135
, pp. 169-179
-
-
Schafer, D.A.1
Jennings, P.B.2
Cooper, J.A.3
-
23
-
-
0029954225
-
Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
-
of special interest. The respective roles of gelsolin and capping protein (CP) in the regulation of actin assembly upon platelet stimulation are examined. CP is the major capping protein in platelets. The association of CP with the actin cytoskeleton increases upon platelet stimulation, which is unexpected in the context of the view that uncapping of barbed ends occurs following cell stimulation.
-
Barkalow K, Witke W, Kwiatkowski DJ, Hartwig JH. Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. of special interest J Cell Biol. 134:1996;389-399 The respective roles of gelsolin and capping protein (CP) in the regulation of actin assembly upon platelet stimulation are examined. CP is the major capping protein in platelets. The association of CP with the actin cytoskeleton increases upon platelet stimulation, which is unexpected in the context of the view that uncapping of barbed ends occurs following cell stimulation.
-
(1996)
J Cell Biol
, vol.134
, pp. 389-399
-
-
Barkalow, K.1
Witke, W.2
Kwiatkowski, D.J.3
Hartwig, J.H.4
-
24
-
-
0030849454
-
Regulation of actin polymerization in cell-free systems by GTPgammaS and Cdc42
-
of special interest. Actin polymerization is elicited by cdc42 in cell lysates of D. discoideum or neutrophils, and by GTPγ S-loaded cdc42 in supernatants resulting from high speed centrification of these lysates. These cell free systems are promising models for biochemical identification of the links between small G proteins and the response of actin.
-
Zigmond S, Joyce M, Borleis J, Bokoch G, Devreotes P. Regulation of actin polymerization in cell-free systems by GTPgammaS and Cdc42. of special interest J Cell Biol. 138:1997;363-374 Actin polymerization is elicited by cdc42 in cell lysates of D. discoideum or neutrophils, and by GTPγ S-loaded cdc42 in supernatants resulting from high speed centrification of these lysates. These cell free systems are promising models for biochemical identification of the links between small G proteins and the response of actin.
-
(1997)
J Cell Biol
, vol.138
, pp. 363-374
-
-
Zigmond, S.1
Joyce, M.2
Borleis, J.3
Bokoch, G.4
Devreotes, P.5
-
25
-
-
0030878997
-
Gelsolin binding to phosphatidylinositol 4,5-bisphosphate is modulated by calcium and pH
-
2's affinity for gelsolin and Cap G, leading to their dissociation from barbed actin filament ends (uncapping).
-
2's affinity for gelsolin and Cap G, leading to their dissociation from barbed actin filament ends (uncapping).
-
(1997)
J Biol Chem
, vol.272
, pp. 20443-20450
-
-
Lin, K.M.1
Wenegieme, E.2
Lu, P.J.3
Chen, C.S.4
Yin, H.L.5
-
26
-
-
0028839660
-
The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
-
Moon A, Drubin D. The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol Biol Cell. 6:1995;1423-1431.
-
(1995)
Mol Biol Cell
, vol.6
, pp. 1423-1431
-
-
Moon, A.1
Drubin, D.2
-
27
-
-
0030033237
-
Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium
-
Aizawa H, Sutoh K, Yahara I. Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium. J Cell Biol. 132:1996;335-344.
-
(1996)
J Cell Biol
, vol.132
, pp. 335-344
-
-
Aizawa, H.1
Sutoh, K.2
Yahara, I.3
-
28
-
-
0030843484
-
Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
-
of outstanding interest. Actin-depolymerizing factor (ADF) increases the rate of treadmilling of actin filaments in vitro by 25-fold. It does this by increasing the rate of filament disassembly from the pointed end specifically. ADF consistently increases the rate of Listeria propulsion in platelet extracts. Barbed end growth, which also powers lamellipodium protusion or filopodium extension, results from the ADF-regulated treadmilling of actin filaments.
-
Carlier MF, Laurent V, Santolini J, Melki R, Didry D, Xia GX, Hong Y, Chua NH, Pantaloni D. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. of outstanding interest J Cell Biol. 136:1997;1307-1322 Actin-depolymerizing factor (ADF) increases the rate of treadmilling of actin filaments in vitro by 25-fold. It does this by increasing the rate of filament disassembly from the pointed end specifically. ADF consistently increases the rate of Listeria propulsion in platelet extracts. Barbed end growth, which also powers lamellipodium protusion or filopodium extension, results from the ADF-regulated treadmilling of actin filaments.
-
(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
-
29
-
-
0030798735
-
Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton
-
Theriot JA. 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
-
30
-
-
0030797467
-
Cofilin promotes rapid actin filament turnover in vivo
-
of special interest. The function of cofilin in budding yeast is adressed by a genetic approach. Cofilin mutants display a slower rate of F-actin depolymerization by latrunculin-A, and harbor defects in endocytosis, while the motility of cortical actin patches is unaffected.
-
Lappalainen P, Drubin DG. Cofilin promotes rapid actin filament turnover in vivo. of special interest Nature. 388:1997;78-82 The function of cofilin in budding yeast is adressed by a genetic approach. Cofilin mutants display a slower rate of F-actin depolymerization by latrunculin-A, and harbor defects in endocytosis, while the motility of cortical actin patches is unaffected.
-
(1997)
Nature
, vol.388
, pp. 78-82
-
-
Lappalainen, P.1
Drubin, D.G.2
-
31
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-
0030820734
-
Cofilin changes the twist of F-actin. Implications for actin filament dynamics and cellular function
-
of special interest. Cryoelectron microscopic observations and image reconstructions show that, in binding to F-actin in a 1:1 ratio, cofilin makes contacts with two F-actin subunits along the long pitch helix, thereby increasing the twist of the filament. Interestingly, the cofilin-binding site overlaps with interfaces of myosin, profilin and gelsolin with actin, although the resulting structural features of the complexes are different.
-
McGough A, Pope B, Chiu W, Weeds A. Cofilin changes the twist of F-actin. Implications for actin filament dynamics and cellular function. of special interest J Cell Biol. 138:1997;771-781 Cryoelectron microscopic observations and image reconstructions show that, in binding to F-actin in a 1:1 ratio, cofilin makes contacts with two F-actin subunits along the long pitch helix, thereby increasing the twist of the filament. Interestingly, the cofilin-binding site overlaps with interfaces of myosin, profilin and gelsolin with actin, although the resulting structural features of the complexes are different.
-
(1997)
J Cell Biol
, vol.138
, pp. 771-781
-
-
McGough, A.1
Pope, B.2
Chiu, W.3
Weeds, A.4
-
32
-
-
0030880186
-
Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
-
of outstanding interest. This mutagenesis study delineates the regions of ADF that interact with both G- and F-actin, and demonstrates the existence of other regions more specifically involved in F-actin binding. The amino-terminal region of ADF, which contains the phosphorylatable serine residue, plays a role in actin binding. Despite the similar folds in ADF and gelsolin segment-1, the two proteins bind actin differently, consistent with their different functions.
-
Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. of outstanding interest EMBO J. 16:1997;5520-5530 This mutagenesis study delineates the regions of ADF that interact with both G- and F-actin, and demonstrates the existence of other regions more specifically involved in F-actin binding. The amino-terminal region of ADF, which contains the phosphorylatable serine residue, plays a role in actin binding. Despite the similar folds in ADF and gelsolin segment-1, the two proteins bind actin differently, consistent with their different functions.
-
(1997)
EMBO J
, vol.16
, pp. 5520-5530
-
-
Lappalainen, P.1
Fedorov, E.V.2
Fedorov, A.A.3
Almo, S.C.4
Drubin, D.G.5
-
33
-
-
0029859963
-
Dephosphorylation of serine 3 regulates nuclear translocation of cofilin
-
Nebl G, Meuer SC, Samstag Y. Dephosphorylation of serine 3 regulates nuclear translocation of cofilin. J Biol Chem. 271:1996;26276-26280.
-
(1996)
J Biol Chem
, vol.271
, pp. 26276-26280
-
-
Nebl, G.1
Meuer, S.C.2
Samstag, Y.3
-
34
-
-
0029736847
-
Dephosphorylation of cofilin in parotid acinar cells
-
Takuma T, Ichida T, Yokoyama N, Tamura S, Obinata T. Dephosphorylation of cofilin in parotid acinar cells. J Biochem (Tokyo). 120:1996;35-41.
-
(1996)
J Biochem (Tokyo)
, vol.120
, pp. 35-41
-
-
Takuma, T.1
Ichida, T.2
Yokoyama, N.3
Tamura, S.4
Obinata, T.5
-
35
-
-
0030601313
-
Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood
-
Okada K, Takano-Ohmuro H, Obinata T, Abe H. Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood. Exp Cell Res. 227:1996;116-122.
-
(1996)
Exp Cell Res
, vol.227
, pp. 116-122
-
-
Okada, K.1
Takano-Ohmuro, H.2
Obinata, T.3
Abe, H.4
-
36
-
-
0030908903
-
The isolated comet tail pseudopodium of Listeria monocytogenes: A tail of two actin filament populations, long and axial and short and random
-
of special interest. This is a very clear electron microscopic study of the organization of actin filaments in the actin tails of Listeria in cell protrusions. The study shows that long (over 2μm long) axial filaments forming the core of the tail are perpendicular to the bacterium surface, while peripheral shorter filaments (0.3 μm long) are arranged in randomly distributed oblique directions. A model more complex than the simple initial nucleation release model [55] needs to be elaborated to accommodate these new results.
-
Sechi AS, Wehland J, Small JV. The isolated comet tail pseudopodium of Listeria monocytogenes: a tail of two actin filament populations, long and axial and short and random. of special interest J Cell Biol. 137:1997;155-167 This is a very clear electron microscopic study of the organization of actin filaments in the actin tails of Listeria in cell protrusions. The study shows that long (over 2μm long) axial filaments forming the core of the tail are perpendicular to the bacterium surface, while peripheral shorter filaments (0.3 μm long) are arranged in randomly distributed oblique directions. A model more complex than the simple initial nucleation release model [55] needs to be elaborated to accommodate these new results.
-
(1997)
J Cell Biol
, vol.137
, pp. 155-167
-
-
Sechi, A.S.1
Wehland, J.2
Small, J.V.3
-
39
-
-
0030900504
-
Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes
-
of special interest. These authors make the interesting point that deletion of residues 21-97 in the amino-terminal region of Act A produces bacteria moving with periodic oscillatory changes in rate. Consistently, actin tails display a periodic density of actin filaments. This behavior has important implications for the mechanism of movement.
-
Lasa I, Gouin E, Goethals M, Vancompernolle K, David V, Vandekerckhove J, Cossart P. Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes. of special interest EMBO J. 16:1997;1531-1540 These authors make the interesting point that deletion of residues 21-97 in the amino-terminal region of Act A produces bacteria moving with periodic oscillatory changes in rate. Consistently, actin tails display a periodic density of actin filaments. This behavior has important implications for the mechanism of movement.
-
(1997)
EMBO J
, vol.16
, pp. 1531-1540
-
-
Lasa, I.1
Gouin, E.2
Goethals, M.3
Vancompernolle, K.4
David, V.5
Vandekerckhove, J.6
Cossart, P.7
-
40
-
-
0028933782
-
A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells
-
Chakraborty T, Ebel F, Domann E, Niebuhr K, Gerstel B, Pistor S, Temmgrove CJ, Jockusch BM, Reinhard M, Walters U, Wehland J. A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells. EMBO J. 14:1995;1314-1321.
-
(1995)
EMBO J
, vol.14
, pp. 1314-1321
-
-
Chakraborty, T.1
Ebel, F.2
Domann, E.3
Niebuhr, K.4
Gerstel, B.5
Pistor, S.6
Temmgrove, C.J.7
Jockusch, B.M.8
Reinhard, M.9
Walters, U.10
Wehland, J.11
-
41
-
-
0029807736
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The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin
-
Smith G, Theriot J, Portnoy D. The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin. J Cell Biol. 135:1996;647-660.
-
(1996)
J Cell Biol
, vol.135
, pp. 647-660
-
-
Smith, G.1
Theriot, J.2
Portnoy, D.3
-
42
-
-
0030592559
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Mena, a relative to VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics
-
of outstanding interest. Provides a novel perspective on the role of vasodilator-stimulated phosphoprotein (VASP), Enabled and mammalian Enabled (Mena) proteins as molecular linkers between signaling pathways and actin polymerization: The murine homolog of VASP, Mena, is recruited at the surface of Listeria in Listeria-infected PtK2 cells.
-
Gertler F, Niebuhr K, Reinhard M, Wehland J, Soriano P. Mena, a relative to VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. of outstanding interest Cell. 87:1996;227-239 Provides a novel perspective on the role of vasodilator-stimulated phosphoprotein (VASP), Enabled and mammalian Enabled (Mena) proteins as molecular linkers between signaling pathways and actin polymerization: The murine homolog of VASP, Mena, is recruited at the surface of Listeria in Listeria-infected PtK2 cells.
-
(1996)
Cell
, vol.87
, pp. 227-239
-
-
Gertler, F.1
Niebuhr, K.2
Reinhard, M.3
Wehland, J.4
Soriano, P.5
-
43
-
-
0030006284
-
Wiscott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
-
Symons M, Derry J, Karlak B, Jiang S, Lemahieu V, McCormick F, Francke U, Abo A. Wiscott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell. 84:1996;723-734.
-
(1996)
Cell
, vol.84
, pp. 723-734
-
-
Symons, M.1
Derry, J.2
Karlak, B.3
Jiang, S.4
Lemahieu, V.5
McCormick, F.6
Francke, U.7
Abo, A.8
-
44
-
-
0030851599
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Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): Implications for actin-based Listeria motility
-
Kang F, Laine R, Bubb M, Southwick F, Purich D. Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): implications for actin-based Listeria motility. Biochemistry. 36:1997;8384-8392.
-
(1997)
Biochemistry
, vol.36
, pp. 8384-8392
-
-
Kang, F.1
Laine, R.2
Bubb, M.3
Southwick, F.4
Purich, D.5
-
45
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-
0028981496
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Actin-based movement of Listeria monocytogenes: Actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface
-
Marchand JB, Moreau P, Paoletti A, Cossart P, Carlier MF, Pantaloni D. Actin-based movement of Listeria monocytogenes: actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface. J Cell Biol. 130:1995;331-343.
-
(1995)
J Cell Biol
, vol.130
, pp. 331-343
-
-
Marchand, J.B.1
Moreau, P.2
Paoletti, A.3
Cossart, P.4
Carlier, M.F.5
Pantaloni, D.6
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46
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0031021153
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Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
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of outstanding interest. The Arp2-Arp3 complex purified from platelet extracts initializes actin polymerization at the surface of Listeria in vitro. In vivo, Arp2-Arp3 is localized throughout the Listeria actin tails in infected cells, and in the lamellipodia of mobile cells, but not in actin bundles [47]. The challenging issue is to understand how Arp2-Arp3 can cycle between different cellular structures.
-
Welch M, Iwamatsu A, Mitchison T. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. of outstanding interest Nature. 385:1997;265-269 The Arp2-Arp3 complex purified from platelet extracts initializes actin polymerization at the surface of Listeria in vitro. In vivo, Arp2-Arp3 is localized throughout the Listeria actin tails in infected cells, and in the lamellipodia of mobile cells, but not in actin bundles [47]. The challenging issue is to understand how Arp2-Arp3 can cycle between different cellular structures.
-
(1997)
Nature
, vol.385
, pp. 265-269
-
-
Welch, M.1
Iwamatsu, A.2
Mitchison, T.3
-
47
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0030802671
-
The human Arp2/3 complex is composed of evolutionary conserved subunits and is localized to cellular regions of dynamic actin filament assembly
-
Welch M, DePace A, Verma S, Iwamatsu A, Mitchison T. The human Arp2/3 complex is composed of evolutionary conserved subunits and is localized to cellular regions of dynamic actin filament assembly. J Cell Biol. 138:1997;375-384.
-
(1997)
J Cell Biol
, vol.138
, pp. 375-384
-
-
Welch, M.1
Depace, A.2
Verma, S.3
Iwamatsu, A.4
Mitchison, T.5
-
48
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0031051993
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Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba
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of special interest. This paper reports the physical properties of the Arp2-Arp3 complex purified from Acanthamoeba and shows that it binds to F-actin with a relatively low affinity. The pure complex has no effect on nucleation, nor does it possess any property of the known actin-binding proteins.
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Mullins RD, Stafford WF, Pollard TD. Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba. of special interest J Cell Biol. 136:1997;331-343 This paper reports the physical properties of the Arp2-Arp3 complex purified from Acanthamoeba and shows that it binds to F-actin with a relatively low affinity. The pure complex has no effect on nucleation, nor does it possess any property of the known actin-binding proteins.
-
(1997)
J Cell Biol
, vol.136
, pp. 331-343
-
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Mullins, R.D.1
Stafford, W.F.2
Pollard, T.D.3
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49
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0029849062
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The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin
-
McCollum D, Feoktistova A, Morphew M, Balasubramanian M, Gould KL. The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin. EMBO J. 15:1996;6438-6446.
-
(1996)
EMBO J
, vol.15
, pp. 6438-6446
-
-
McCollum, D.1
Feoktistova, A.2
Morphew, M.3
Balasubramanian, M.4
Gould, K.L.5
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50
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0031193920
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The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches
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of special interest. This is a genetic and biochemical characterization of S. cerevisiae Arp2-Arp3, providing the sequences of the polypeptides of the complex and showing its function in morphogenesis and actin patch movement.
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Winter D, Podtelejnikov A, Mann M, Li R. The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches. of special interest Curr Biol. 7:1997;519-529 This is a genetic and biochemical characterization of S. cerevisiae Arp2-Arp3, providing the sequences of the polypeptides of the complex and showing its function in morphogenesis and actin patch movement.
-
(1997)
Curr Biol
, vol.7
, pp. 519-529
-
-
Winter, D.1
Podtelejnikov, A.2
Mann, M.3
Li, R.4
-
51
-
-
0029959468
-
The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton
-
Moreau V, Madania A, Martin R, Winson B. The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J Cell Biol. 134:1996;117-132.
-
(1996)
J Cell Biol
, vol.134
, pp. 117-132
-
-
Moreau, V.1
Madania, A.2
Martin, R.3
Winson, B.4
-
52
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0030852059
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In vitro reconstitution of cortical actin assembly sites in budding yeast
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of outstanding interest. This is an original in vitro reconstitution assay of actin assembly in pre-inactivated permeabilized yeast cells, used to identify and purify components of the actin assembly machinery in cortical patches. Elegantly designed experiments show evidence for Bee-1 and pca-1 binding sequentially to the sites of actin assembly in permeabilized cells.
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Lechler T, Li R. In vitro reconstitution of cortical actin assembly sites in budding yeast. of outstanding interest J Cell Biol. 138:1997;95-103 This is an original in vitro reconstitution assay of actin assembly in pre-inactivated permeabilized yeast cells, used to identify and purify components of the actin assembly machinery in cortical patches. Elegantly designed experiments show evidence for Bee-1 and pca-1 binding sequentially to the sites of actin assembly in permeabilized cells.
-
(1997)
J Cell Biol
, vol.138
, pp. 95-103
-
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Lechler, T.1
Li, R.2
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53
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0031045512
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Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton
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of special interest. The identification of Beelp, a homolog of Wiscott - Aldrich syndrome protein in yeast, its localization in cortical actin patches and its interaction with sla1p and actin point to this protein as playing a crucial role in the organization of the molecular scaffold which links the actin cytoskeleton to the signaling pathway involved in the control of cell growth and exocytosis.
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Li R. Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. of special interest J Cell Biol. 136:1997;649-658 The identification of Beelp, a homolog of Wiscott - Aldrich syndrome protein in yeast, its localization in cortical actin patches and its interaction with sla1p and actin point to this protein as playing a crucial role in the organization of the molecular scaffold which links the actin cytoskeleton to the signaling pathway involved in the control of cell growth and exocytosis.
-
(1997)
J Cell Biol
, vol.136
, pp. 649-658
-
-
Li, R.1
-
54
-
-
0027194759
-
Cellular motions and thermal fluctuations: The Brownian ratchet
-
Peskin C, Oster G. Cellular motions and thermal fluctuations: the Brownian ratchet. Biophys J. 65:1993;316-324.
-
(1993)
Biophys J
, vol.65
, pp. 316-324
-
-
Peskin, C.1
Oster, G.2
-
55
-
-
0025740949
-
Actin microfilament dynamics in locomoting cells
-
Theriot JA, Michison TJ. Actin microfilament dynamics in locomoting cells. Nature. 352:1991;126-131.
-
(1991)
Nature
, vol.352
, pp. 126-131
-
-
Theriot, J.A.1
Michison, T.J.2
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