메뉴 건너뛰기




Volumn 45, Issue 4, 2000, Pages 293-306

Actin filaments are severed by both native and recombinant Dictyostelium cofilin but to different extents

Author keywords

Actin; ADF; Chemotaxis; Cofilin; Cytoskeleton; Motility

Indexed keywords

COFILIN; F ACTIN;

EID: 0034113924     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(200004)45:4<293::AID-CM5>3.0.CO;2-1     Document Type: Article
Times cited : (79)

References (45)
  • 1
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated ADF and identification of the regulatory site
    • Agnew B, Minamide L, Bamburg J. 1995. Reactivation of phosphorylated ADF and identification of the regulatory site. J Biol Chem 270:17582-17587.
    • (1995) J Biol Chem , vol.270 , pp. 17582-17587
    • Agnew, B.1    Minamide, L.2    Bamburg, J.3
  • 2
    • 0028921277 scopus 로고
    • Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum
    • Aizawa H, Sutoh K, Tsubuki S, Kawashima S, Ishii A, Yahara I. 1995. Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum. J Biol Chem 270:10923-10932.
    • (1995) J Biol Chem , vol.270 , pp. 10923-10932
    • Aizawa, H.1    Sutoh, K.2    Tsubuki, S.3    Kawashima, S.4    Ishii, A.5    Yahara, I.6
  • 3
    • 0030033237 scopus 로고    scopus 로고
    • Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium
    • Aizawa H, Sutoh K, Yahara I. 1996. Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium. J Cell Biol 132:335-344.
    • (1996) J Cell Biol , vol.132 , pp. 335-344
    • Aizawa, H.1    Sutoh, K.2    Yahara, I.3
  • 4
    • 0344299281 scopus 로고    scopus 로고
    • Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation
    • Bailly M, Macaluso F, Cammer M. Chan A, Segall JE, Condeelis JS. 1999. 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 145:331-345
    • (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
  • 5
    • 0025763462 scopus 로고
    • Purification and characterization of low-molecular-weight actin-depolymerizing proteins from brain and cultured cells
    • Bamburg JR, Minamide LS, Morgan TE, Hayden SM, Giuliano KA, Koffer A. 1991. Purification and characterization of low-molecular-weight actin-depolymerizing proteins from brain and cultured cells. Methods Enzymol 196:125-140.
    • (1991) Methods Enzymol , vol.196 , pp. 125-140
    • Bamburg, J.R.1    Minamide, L.S.2    Morgan, T.E.3    Hayden, S.M.4    Giuliano, K.A.5    Koffer, A.6
  • 6
    • 0033198879 scopus 로고    scopus 로고
    • Putting a new twist on actin: ADF/cofilins modulate actin dynamics
    • Bamburg JR, McGough A, Ono S. 1999. Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol 9:364-70
    • (1999) Trends Cell Biol , vol.9 , pp. 364-370
    • Bamburg, J.R.1    McGough, A.2    Ono, S.3
  • 7
    • 0029954225 scopus 로고    scopus 로고
    • Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
    • Barkalow K, Witke W, Kwiatkowski DJ, Hartwig JH. 1996. Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J Cell Biol 134:389-399.
    • (1996) J Cell Biol , vol.134 , pp. 389-399
    • Barkalow, K.1    Witke, W.2    Kwiatkowski, D.J.3    Hartwig, J.H.4
  • 8
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • Blanchoin L, Pollard T. 1998. Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. J Biol Chem 273:25106-25111.
    • (1998) J Biol Chem , vol.273 , pp. 25106-25111
    • Blanchoin, L.1    Pollard, T.2
  • 9
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments
    • Blanchoin L, Pollard T. 1999. Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J Biol Chem 274:15538-155546.
    • (1999) J Biol Chem , vol.274 , pp. 15538-155546
    • Blanchoin, L.1    Pollard, T.2
  • 10
    • 0025764368 scopus 로고
    • Isolation of actin-binding proteins from Dictyostelium discoideum
    • Bresnick AR, Condeelis J. 1991. Isolation of actin-binding proteins from Dictyostelium discoideum. Methods Enzymol 196:70-83.
    • (1991) Methods Enzymol , vol.196 , pp. 70-83
    • Bresnick, A.R.1    Condeelis, J.2
  • 11
    • 0026045382 scopus 로고
    • Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution
    • Cano M, Lauffenburger D, Zigmond S. 1991. Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution. J Cell Biol 115:677-687.
    • (1991) J Cell Biol , vol.115 , pp. 677-687
    • Cano, M.1    Lauffenburger, D.2    Zigmond, S.3
  • 12
    • 0024527982 scopus 로고
    • Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules
    • Carlier M. 1989. Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules. Int Rev Cytol 115:139-170.
    • (1989) Int Rev Cytol , vol.115 , pp. 139-170
    • Carlier, M.1
  • 13
    • 0032006817 scopus 로고    scopus 로고
    • Control of actin dynamics
    • Carlier M. 1998. Control of actin dynamics. Curr Opin Cell Biol 10:45-51
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 45-51
    • Carlier, M.1
  • 14
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier M, Laurent V, Santolini J, Melki R, Didry D, Xia G, Hong Y, Chua N, Pantaloni D. 1997. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J Cell Biol 136:1307-1323.
    • (1997) J Cell Biol , vol.136 , pp. 1307-1323
    • Carlier, M.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.6    Hong, Y.7    Chua, N.8    Pantaloni, D.9
  • 15
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier M, Pantaloni D. 1997. Control of actin dynamics in cell motility. J Mol Biol 269:459-467.
    • (1997) J Mol Biol , vol.269 , pp. 459-467
    • Carlier, M.1    Pantaloni, D.2
  • 16
    • 0031908252 scopus 로고    scopus 로고
    • EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells
    • Chan AY, Raft S, Bailly M, Wyckoff JB, Segall JE, Condeelis JS. 1998. EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells. J Cell Sci 111:199-211.
    • (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
  • 17
    • 0022619258 scopus 로고
    • Purification and characterization of actophorin, a new 15,000-Dalton actin-binding protein from Acanthamoeba castellanii
    • Cooper JA, Blum JD, Williams RC, Pollard TD. 1986. Purification and characterization of actophorin, a new 15,000-Dalton actin-binding protein from Acanthamoeba castellanii. J Biol Chem 261: 477-485.
    • (1986) J Biol Chem , vol.261 , pp. 477-485
    • Cooper, J.A.1    Blum, J.D.2    Williams, R.C.3    Pollard, T.D.4
  • 18
    • 0020533805 scopus 로고
    • Pyrene actin: Documentation of the validity of a sensitive assay for actin polymerization
    • Cooper JA, Walker SB, Pollard TD. 1983. Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J Muscle Res Cell Motil 4:253-262.
    • (1983) J Muscle Res Cell Motil , vol.4 , pp. 253-262
    • Cooper, J.A.1    Walker, S.B.2    Pollard, T.D.3
  • 19
    • 0022993466 scopus 로고
    • Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules
    • Drenckhahn D, Pollard TD. 1986. Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J Biol Chem 261:12754-12758.
    • (1986) J Biol Chem , vol.261 , pp. 12754-12758
    • Drenckhahn, D.1    Pollard, T.D.2
  • 20
    • 0032558437 scopus 로고    scopus 로고
    • Kinetic studies on the effect of yeast cofilin on yeast actin polymerization
    • Du J, Frieden C. 1998. Kinetic studies on the effect of yeast cofilin on yeast actin polymerization.Biochemistry 37:13276-13284.
    • (1998) Biochemistry , vol.37 , pp. 13276-13284
    • Du, J.1    Frieden, C.2
  • 21
    • 0030728491 scopus 로고    scopus 로고
    • Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium
    • Eddy RJ, Han J, Condeelis JS. 1997. Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium. J Cell Biol 139:1243-1253.
    • (1997) J Cell Biol , vol.139 , pp. 1243-1253
    • Eddy, R.J.1    Han, J.2    Condeelis, J.S.3
  • 22
    • 0029020353 scopus 로고
    • pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1α
    • Edmonds BT, Murray J, Condeelis J. 1995. pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1α. J Biol Chem 270:15222-15230.
    • (1995) J Biol Chem , vol.270 , pp. 15222-15230
    • Edmonds, B.T.1    Murray, J.2    Condeelis, J.3
  • 24
    • 0024044667 scopus 로고
    • Relationship of pseudopod extension to chemotactic hormone-induced actin polymerization in amoeboid cells
    • Hall AL, Schlein A, Condeelis J. 1988. Relationship of pseudopod extension to chemotactic hormone-induced actin polymerization in amoeboid cells. J Cell Biochem 37:285-299.
    • (1988) J Cell Biochem , vol.37 , pp. 285-299
    • Hall, A.L.1    Schlein, A.2    Condeelis, J.3
  • 25
    • 0024351030 scopus 로고
    • Transduction of the chemotactic signal to the actin cytoskeleton of Dictyostelium discoideum
    • Hall AL, Warren V, Condeelis J. 1989. Transduction of the chemotactic signal to the actin cytoskeleton of Dictyostelium discoideum. Dev Biol 136:517-525.
    • (1989) Dev Biol , vol.136 , pp. 517-525
    • Hall, A.L.1    Warren, V.2    Condeelis, J.3
  • 26
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins M, Pope B, Maciver SK, Weeds AG. 1993. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 32:9985-9993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 27
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor (ADF) with G- and F-actin
    • Hayden SM, Miller PS, Brauweiler A, Bamburg JR. 1993. Analysis of the interactions of actin depolymerizing factor (ADF) with G- and F-actin. Biochemistry 32:9994-10004.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 28
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron SJ, Spudich JA. 1986. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc Natl Acad Sci USA 83:6272-6276.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 29
    • 0025782977 scopus 로고
    • Assays for actin sliding movement over myosin-coated surfaces. Molecular motors and the cytoskeleton
    • Kron SJ, Toyoshima YY, Uyeda TQP, Spudich JA. 1991. Assays for actin sliding movement over myosin-coated surfaces. Molecular motors and the cytoskeleton. Methods Enzymol 196:399-416.
    • (1991) Methods Enzymol , vol.196 , pp. 399-416
    • Kron, S.J.1    Toyoshima, Y.Y.2    Uyeda, T.Q.P.3    Spudich, J.A.4
  • 30
    • 0030880186 scopus 로고    scopus 로고
    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG. 1997. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis EMBO J 16:5520-5530
    • (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
  • 31
    • 0031887131 scopus 로고    scopus 로고
    • How ADF/cofilin depolymerizes actin filaments
    • Maciver SK. 1998. How ADF/cofilin depolymerizes actin filaments. Curr Opin Cell Biol 10:140-144.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 140-144
    • Maciver, S.K.1
  • 32
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin from Acanthamoeba castellani
    • Maciver SK, Zot HG, Pollard TD. 1991. Characterization of actin filament severing by actophorin from Acanthamoeba castellani. J Cell Biol 115:1611-1620.
    • (1991) J Cell Biol , vol.115 , pp. 1611-1620
    • Maciver, S.K.1    Zot, H.G.2    Pollard, T.D.3
  • 33
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough A, Pope B, Chiu W, Weeds A. 1997. Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function. J Cell Biol 138:771-781.
    • (1997) J Cell Biol , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 34
    • 0028839660 scopus 로고
    • The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
    • Moon A, Drubin D. 1995. The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol Biol Cell 6:1423-1431.
    • (1995) Mol Biol Cell , vol.6 , pp. 1423-1431
    • Moon, A.1    Drubin, D.2
  • 35
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high-affinity pointed-end capping and formation of branching networks of filaments
    • Mullins RD, Heuser JA, Pollard TD. 1998. 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 95:6181-6186.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 36
    • 0023789421 scopus 로고
    • Direct demonstration of actin filament annealing in vitro
    • Murphy DB, Gray RO, Grasser WA, Pollard TD. 1988. Direct demonstration of actin filament annealing in vitro. J Cell Biol 106:1947-1954.
    • (1988) J Cell Biol , vol.106 , pp. 1947-1954
    • Murphy, D.B.1    Gray, R.O.2    Grasser, W.A.3    Pollard, T.D.4
  • 37
    • 0025099508 scopus 로고
    • Length distribution of F-actin in Dictyostelium discoideum
    • Podolski J, Steck T. 1990. Length distribution of F-actin in Dictyostelium discoideum. J Biol Chem 265:1312-1318.
    • (1990) J Biol Chem , vol.265 , pp. 1312-1318
    • Podolski, J.1    Steck, T.2
  • 38
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard TD. 1986. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J Cell Biol 103: 2747-2754.
    • (1986) J Cell Biol , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 39
    • 0033597934 scopus 로고    scopus 로고
    • Control of actin filament length and turnover by actin depolymerizing factor (ADF/cofilin) in the presence of capping proteins and ARP2/3 complex
    • Ressad F, Didry D, Egile C, Pantaloni D, Carlier M. 1999. 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 274:20970-20976.
    • (1999) J Biol Chem , vol.274 , pp. 20970-20976
    • Ressad, F.1    Didry, D.2    Egile, C.3    Pantaloni, D.4    Carlier, M.5
  • 42
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-toroponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-toroponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246:4866-4871.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 43
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina TM, Borisy GG. 1999. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J Cell Biol 145:1009-1026
    • (1999) J Cell Biol , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 44
    • 0030798735 scopus 로고    scopus 로고
    • Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton
    • Theriot JA. 1997. Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton. J Cell Biol 136:1165-1168.
    • (1997) J Cell Biol , vol.136 , pp. 1165-1168
    • Theriot, J.A.1
  • 45
    • 0027293382 scopus 로고
    • Recent quantitative studies of actin filament turnover during cell locomotion
    • Zigmond SH. 1993. Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil Cytoskeleton 25: 309-316.
    • (1993) Cell Motil Cytoskeleton , vol.25 , pp. 309-316
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.