메뉴 건너뛰기




Volumn 84, Issue 4, 2005, Pages 503-515

Activated cofilin colocalises with Arp2/3 complex in apoptotic blebs during programmed cell death

Author keywords

A431 cells; ADF cofilin; Apoptosis; Arp2 3 complex; Blebs

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; COFILIN; ENHANCED GREEN FLUORESCENT PROTEIN; ETOPOSIDE; PROTEIN ANTIBODY;

EID: 16244370745     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2004.11.008     Document Type: Article
Times cited : (37)

References (49)
  • 2
    • 0034536444 scopus 로고    scopus 로고
    • The serine phosphatases PP1 and PP2A associate with and activate actin-binding protein cofilin in human T-lymphocytes
    • A. Ambach J. Saunus M. Konstandin S. Wesselborg S.C. Meuer Y. Samstag The serine phosphatases PP1 and PP2A associate with and activate actin-binding protein cofilin in human T-lymphocytes Eur. J. Immunol. 30 2000 3422-3431
    • (2000) Eur. J. Immunol. , vol.30 , pp. 3422-3431
    • Ambach, A.1    Saunus, J.2    Konstandin, M.3    Wesselborg, S.4    Meuer, S.C.5    Samstag, Y.6
  • 4
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • J.R. Bamburg Proteins of the ADF/cofilin family: Essential regulators of actin dynamics Annu. Rev. Cell Dev. Biol. 15 1999 185-230
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0032517817 scopus 로고    scopus 로고
    • The localisation of myosin VI at the Golgi complex and leading edges of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation
    • F. Buss J. Kendrick-Jones C. Lionne A. Knight G. Coté P. Luzio The localisation of myosin VI at the Golgi complex and leading edges of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation J. Cell Biol. 143 1998 1535-1545
    • (1998) J. Cell Biol. , vol.143 , pp. 1535-1545
    • Buss, F.1    Kendrick-Jones, J.2    Lionne, C.3    Knight, A.4    Coté, G.5    Luzio, P.6
  • 8
    • 0344668558 scopus 로고    scopus 로고
    • Mitochondrial translocation of cofilin is an early step in apoptosis induction
    • B.T. Chua C. Volbracht K.O. Tan R. Li V.C. Yu L. Peng Mitochondrial translocation of cofilin is an early step in apoptosis induction Nat. Cell Biol. 5 2003 1083-1089
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1083-1089
    • Chua, B.T.1    Volbracht, C.2    Tan, K.O.3    Li, R.4    Yu, V.C.5    Peng, L.6
  • 9
    • 0035072953 scopus 로고    scopus 로고
    • Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I
    • M.L. Coleman E.A. Sahai M. Yeo M. Bosch A. Dear M.F. Olson Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I Nat. Cell Biol. 3 2001 339-345
    • (2001) Nat. Cell Biol. , vol.3 , pp. 339-345
    • Coleman, M.L.1    Sahai, E.A.2    Yeo, M.3    Bosch, M.4    Dear, A.5    Olson, M.F.6
  • 10
    • 4344674527 scopus 로고    scopus 로고
    • Cortactin signalling and dynamic actin networks
    • R.J. Daly Cortactin signalling and dynamic actin networks Biochem. J. 15 2004 13-25
    • (2004) Biochem. J. , vol.15 , pp. 13-25
    • Daly, R.J.1
  • 11
    • 0343341218 scopus 로고    scopus 로고
    • Staurosporine-induced neuronal death: Multiple mechanisms and methodological implications
    • M. Deshmukh E.M. Johnson Jr. Staurosporine-induced neuronal death: multiple mechanisms and methodological implications Cell Death Differ. 7 2000 250-261
    • (2000) Cell Death Differ. , vol.7 , pp. 250-261
    • Deshmukh, M.1    Johnson, E.M.2
  • 12
    • 4444339659 scopus 로고    scopus 로고
    • Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension
    • V. DesMarais F. Macaluso J. Condeelis M. Bailly Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension J. Cell Sci. 117 2004 3499-3510
    • (2004) J. Cell Sci. , vol.117 , pp. 3499-3510
    • DesMarais, V.1    Macaluso, F.2    Condeelis, J.3    Bailly, M.4
  • 13
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates and functions during apoptosis
    • W.C. Earnshaw L.M. Martins S.H. Kaufmann Mammalian caspases: Structure, activation, substrates and functions during apoptosis Annu. Rev. Biochem. 68 1999 383-424
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 14
    • 0037389872 scopus 로고    scopus 로고
    • Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin
    • M. Endo K. Ohashi Y. Sasaki Y. Goshima R. Niwa T. Uemura K. Mizuno Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin J. Neurosci. 23 2003 2527-2537
    • (2003) J. Neurosci. , vol.23 , pp. 2527-2537
    • Endo, M.1    Ohashi, K.2    Sasaki, Y.3    Goshima, Y.4    Niwa, R.5    Uemura, T.6    Mizuno, K.7
  • 15
    • 0030756377 scopus 로고    scopus 로고
    • Cofilin undergoes rapid dephosphorylation in stimulated neutrophils and translocates to ruffled membranes enriched in products of the NADPH oxidase complex. Evidence for a novel cycle of phosphorylation and dephosphorylation
    • P.G. Heyworth J.M. Robinson J. Ding B.A. Ellis J.A. Badwey Cofilin undergoes rapid dephosphorylation in stimulated neutrophils and translocates to ruffled membranes enriched in products of the NADPH oxidase complex. Evidence for a novel cycle of phosphorylation and dephosphorylation Histochem. Cell Biol. 108 1997 221-233
    • (1997) Histochem. Cell Biol. , vol.108 , pp. 221-233
    • Heyworth, P.G.1    Robinson, J.M.2    Ding, J.3    Ellis, B.A.4    Badwey, J.A.5
  • 16
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • J.F.R. Kerr A.H. Wyllie A.R. Currie Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics Br. J. Cancer 26 1972 239-257
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 18
    • 15144352303 scopus 로고    scopus 로고
    • The effect of two actin depolymerising factors (ADF/cofilin) on actin filament turnover: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin
    • S.K. Maciver B.J. Pope S. Whytock A.G. Weeds The effect of two actin depolymerising factors (ADF/cofilin) on actin filament turnover: PH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin Eur. J. Biochem. 256 1998 388-397
    • (1998) Eur. J. Biochem. , vol.256 , pp. 388-397
    • Maciver, S.K.1    Pope, B.J.2    Whytock, S.3    Weeds, A.G.4
  • 20
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • A. McGough B. Pope W. Chiu A.G. Weeds Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function J. Cell Biol. 138 1997 771-781
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.G.4
  • 21
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerising factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • P.J. Meberg S. Ono L.S. Minamide M. Takahashi J.R. Bamburg Actin depolymerising factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension Cell Motil. Cytoskeleton 39 1998 172-190
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 22
    • 0032498625 scopus 로고    scopus 로고
    • Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation
    • J.C. Mills N.L. Stone J. Erhardt R.N. Pittman Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation J. Cell Biol. 140 1998 627-636
    • (1998) J. Cell Biol. , vol.140 , pp. 627-636
    • Mills, J.C.1    Stone, N.L.2    Erhardt, J.3    Pittman, R.N.4
  • 23
    • 0019800463 scopus 로고
    • Silver-stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • J.H. Morrissey Silver-stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity Anal. Biochem. 117 1981 307-310
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 26
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganisation by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • R. Niwa K. Nagata-Ohashi M. Takeichi K. Mizuno T. Uemura Control of actin reorganisation by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin Cell 108 2002 233-246
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 27
    • 0031822941 scopus 로고    scopus 로고
    • Mycoplasma nucleases able to induce internucleosomal DNA degradation in cultured cells possess many characteristics of eukaryotic apoptotic nucleases
    • R. Paddenberg A. Weber S. Wulf H.G. Mannherz Mycoplasma nucleases able to induce internucleosomal DNA degradation in cultured cells possess many characteristics of eukaryotic apoptotic nucleases Cell Death Differ. 5 1998 517-528
    • (1998) Cell Death Differ. , vol.5 , pp. 517-528
    • Paddenberg, R.1    Weber, A.2    Wulf, S.3    Mannherz, H.G.4
  • 28
    • 0034986733 scopus 로고    scopus 로고
    • Serum withdrawal induces a redistribution of intracellular gelsolin towards F-actin in NIH 3T3 fibroblasts preceding apoptotic cell death
    • R. Paddenberg S. Loos H.-J. Schöneberger S. Wulf A. Müller M. Iwig H.G. Mannherz Serum withdrawal induces a redistribution of intracellular gelsolin towards F-actin in NIH 3T3 fibroblasts preceding apoptotic cell death Eur. J. Cell Biol. 80 2001 366-378
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 366-378
    • Paddenberg, R.1    Loos, S.2    Schöneberger, H.-J.3    Wulf, S.4    Müller, A.5    Iwig, M.6    Mannherz, H.G.7
  • 29
    • 0028057478 scopus 로고
    • The apoptotis endonucleases: Cleaning up after cell death
    • M.C. Peitsch H.G. Mannherz J. Tschopp The apoptotis endonucleases: cleaning up after cell death Trends Cell Biol. 4 1994 37-41
    • (1994) Trends Cell Biol. , vol.4 , pp. 37-41
    • Peitsch, M.C.1    Mannherz, H.G.2    Tschopp, J.3
  • 30
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • T.D. Pollard G.G. Borisy Cellular motility driven by assembly and disassembly of actin filaments Cell 112 2003 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 31
    • 0028342410 scopus 로고
    • Distribution of deoxyribonuclease I in rat tissues and its correlation to cellular turnover and apoptosis (programmed cell death)
    • B. Polzar S. Zanotti H. Stephan F. Rauch M. Peitsch M. Irmler J. Tschopp H.G. Mannherz Distribution of deoxyribonuclease I in rat tissues and its correlation to cellular turnover and apoptosis (programmed cell death) Eur. J. Cell Biol. 64 1994 200-210
    • (1994) Eur. J. Cell Biol. , vol.64 , pp. 200-210
    • Polzar, B.1    Zanotti, S.2    Stephan, H.3    Rauch, F.4    Peitsch, M.5    Irmler, M.6    Tschopp, J.7    Mannherz, H.G.8
  • 32
    • 0034640134 scopus 로고    scopus 로고
    • Uncoupling filament fragmentation by cofilin from increased subunit turnover
    • B. Pope S.M. Gonsior S. Yeoh A. McGough A.G. Weeds Uncoupling filament fragmentation by cofilin from increased subunit turnover J. Mol. Biol. 298 2000 649-661
    • (2000) J. Mol. Biol. , vol.298 , pp. 649-661
    • Pope, B.1    Gonsior, S.M.2    Yeoh, S.3    McGough, A.4    Weeds, A.G.5
  • 33
    • 0008727013 scopus 로고    scopus 로고
    • Alterations of the actin polymerisation status as an apoptotic morphological effector in HL-60 cells
    • J.Y. Rao Y.S. Jin Q. Zheng J. Cheng J. Tai G.P. Hemstreet Alterations of the actin polymerisation status as an apoptotic morphological effector in HL-60 cells J. Cell. Biochem. 75 1999 686-697
    • (1999) J. Cell. Biochem. , vol.75 , pp. 686-697
    • Rao, J.Y.1    Jin, Y.S.2    Zheng, Q.3    Cheng, J.4    Tai, J.5    Hemstreet, G.P.6
  • 36
    • 0035075597 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing
    • M. Sebbagh C. Renvoizé J. Hamelin N. Riché J. Bertoglio J. Bréard Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing Nat. Cell Biol. 3 2001 346-350
    • (2001) Nat. Cell Biol. , vol.3 , pp. 346-350
    • Sebbagh, M.1    Renvoizé, C.2    Hamelin, J.3    Riché, N.4    Bertoglio, J.5    Bréard, J.6
  • 37
    • 0035826163 scopus 로고    scopus 로고
    • Staurosporine and conventional anticancer drugs induce overlapping, yet distinct pathways of apoptosis and caspase activation
    • A. Stepczynska K. Lauber I.H. Engels O. Janssen D. Kabelitz S. Wesselborg K. Schulze-Osthoff Staurosporine and conventional anticancer drugs induce overlapping, yet distinct pathways of apoptosis and caspase activation Oncogene 20 2001 1193-1202
    • (2001) Oncogene , vol.20 , pp. 1193-1202
    • Stepczynska, A.1    Lauber, K.2    Engels, I.H.3    Janssen, O.4    Kabelitz, D.5    Wesselborg, S.6    Schulze-Osthoff, K.7
  • 38
    • 0033852098 scopus 로고    scopus 로고
    • Different sublines of Jurkat cells respond with varying susceptibility of internucleosomal DNA degradation to different mediators of apoptosis
    • I. Stolzenberg S. Wulf H.G. Mannherz R. Paddenberg Different sublines of Jurkat cells respond with varying susceptibility of internucleosomal DNA degradation to different mediators of apoptosis Cell Tissue Res. 301 2000 273-382
    • (2000) Cell Tissue Res. , vol.301 , pp. 273-382
    • Stolzenberg, I.1    Wulf, S.2    Mannherz, H.G.3    Paddenberg, R.4
  • 39
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerisation factor/cofilin in dendritic organisation and treadmilling of actin filament array in lamellipodia
    • T.M. Svitkina G.G. Borisy Arp2/3 complex and actin depolymerisation factor/cofilin in dendritic organisation and treadmilling of actin filament array in lamellipodia J. Cell Biol. 145 1999 1009-1026
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 40
    • 0037081289 scopus 로고    scopus 로고
    • Impaired spermatogenic ability of testicular germ cells in mice deficient in the LIM-kinase 2 gene
    • H. Takahashi U. Koshimizu J. Miyazaki T. Nakamura Impaired spermatogenic ability of testicular germ cells in mice deficient in the LIM-kinase 2 gene Dev. Biol. 241 2002 259-272
    • (2002) Dev. Biol. , vol.241 , pp. 259-272
    • Takahashi, H.1    Koshimizu, U.2    Miyazaki, J.3    Nakamura, T.4
  • 41
    • 3042858915 scopus 로고    scopus 로고
    • Caspase-mediated cleavage and activation of LIM-kinase 1 and its role in apoptotic membrane blebbing
    • G. Tomiyoshi Y. Horita M. Nishita K. Ohashi K. Mizuno Caspase-mediated cleavage and activation of LIM-kinase 1 and its role in apoptotic membrane blebbing Genes Cells 9 2004 591-600
    • (2004) Genes Cells , vol.9 , pp. 591-600
    • Tomiyoshi, G.1    Horita, Y.2    Nishita, M.3    Ohashi, K.4    Mizuno, K.5
  • 42
    • 0032901710 scopus 로고    scopus 로고
    • Self-polarisation and directional motility of cytoplasm
    • A.B. Verkhovsky T.M. Svitkina G.G. Borisy Self-polarisation and directional motility of cytoplasm Curr. Biol. 9 1999 11-20
    • (1999) Curr. Biol. , vol.9 , pp. 11-20
    • Verkhovsky, A.B.1    Svitkina, T.M.2    Borisy, G.G.3
  • 43
    • 0000212480 scopus 로고
    • Die nachembryonale Entwicklung der Musciden nach Beobachtungen an Musca vomitoria und Sarcophaga carnaria
    • A. Weismann Die nachembryonale Entwicklung der Musciden nach Beobachtungen an Musca vomitoria und Sarcophaga carnaria Z. Wiss. Zool. 14 1864 187-336
    • (1864) Z. Wiss. Zool. , vol.14 , pp. 187-336
    • Weismann, A.1
  • 45
    • 0033839622 scopus 로고    scopus 로고
    • Protein expression patterns of identified neurons and of sprouting cells from leech central nervous system
    • X. Wu B. Ritter J.H. Schlattjan V. Lessmann R. Heumann I.D. Dietzel Protein expression patterns of identified neurons and of sprouting cells from leech central nervous system J. Neurobiol. 44 2000 320-332
    • (2000) J. Neurobiol. , vol.44 , pp. 320-332
    • Wu, X.1    Ritter, B.2    Schlattjan, J.H.3    Lessmann, V.4    Heumann, R.5    Dietzel, I.D.6
  • 46
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • A.H. Wyllie Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation Nature 284 1980 555-556
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 48
    • 1842783552 scopus 로고    scopus 로고
    • Overexpression of LIM kinase 1 renders resistance to apoptosis in PC12 cells by inhibition of caspase activation
    • E. Yang H. Kim J. Lee J.-S. Shin H. Yoon S.-J. Kim I.-H. Choi Overexpression of LIM kinase 1 renders resistance to apoptosis in PC12 cells by inhibition of caspase activation Cell. Mol. Neurol. 24 2004 181-192
    • (2004) Cell. Mol. Neurol. , vol.24 , pp. 181-192
    • Yang, E.1    Kim, H.2    Lee, J.3    Shin, J.-S.4    Yoon, H.5    Kim, S.-J.6    Choi, I.-H.7
  • 49
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • S. Yeoh B. Pope H.G. Mannherz A. Weeds Determining the differences in actin binding by human ADF and cofilin J. Mol. Biol. 315 2002 911-925
    • (2002) J. Mol. Biol. , vol.315 , pp. 911-925
    • Yeoh, S.1    Pope, B.2    Mannherz, H.G.3    Weeds, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.