메뉴 건너뛰기




Volumn 190, Issue 1-2, 1999, Pages 67-74

Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms

Author keywords

Actin; Actin depolymerizing factor; Actin monomer pool; Actin monomer sequestration; Atp hydrolysis; Capping proteins; Cofilin; Coordinated calcium regulation; Critical concentration changes; Depolymerization rate constant; Ebashi; Elongation rates; Lamellipodia; Leucocytes; Listeria monocytogenes; Myosin heads; Platelets; Profilin; Thymosin 4; Thyone acrosome; Treadmilling; Tropomodulin; Troponin

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ADENOSINE TRIPHOSPHATE; COFILIN; TROPOMODULIN;

EID: 0032971134     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-1-4615-5543-8_8     Document Type: Article
Times cited : (48)

References (31)
  • 2
    • 0025970527 scopus 로고
    • Actin: Protein structure and filament dynamics
    • Carlier M-F: Actin: Protein structure and filament dynamics. J Biol Chem 266: 1-4, 1991
    • (1991) J Biol Chem , vol.266 , pp. 1-4
    • Carlier, M.-F.1
  • 3
    • 0022555884 scopus 로고
    • Actin and actin binding proteins. a critical evaluation of mechanisms and functions
    • Pollard TD, Cooper JA: Actin and actin binding proteins. A critical evaluation of mechanisms and functions. Ann Rev Biochem 55: 987-103, 1986
    • (1986) Ann Rev Biochem , vol.55 , pp. 987-1103
    • Pollard, T.D.1    Cooper, J.A.2
  • 4
    • 0020484210 scopus 로고
    • Treadmilling of actin at physiological salt solutions
    • Wegner A: Treadmilling of actin at physiological salt solutions. J Mol Biol 161: 607-615, 1982
    • (1982) J Mol Biol , vol.161 , pp. 607-615
    • Wegner, A.1
  • 5
    • 0025239493 scopus 로고
    • Kinetics of the interaction of a 41 - kilodalton macrophage capping protein with actin: Promotion of nucleation during prolongation of the lag period
    • Young CL, Southwick FS, Weber A: Kinetics of the interaction of a 41 - kilodalton macrophage capping protein with actin: Promotion of nucleation during prolongation of the lag period. Biochemistry 29: 2232-2240, 1990
    • (1990) Biochemistry , vol.29 , pp. 2232-2240
    • Young, C.L.1    Southwick, F.S.2    Weber, A.3
  • 6
    • 0029612323 scopus 로고
    • Control of actin assembly at filament ends
    • Schafer DA, Cooper JA: Control of actin assembly at filament ends. Ann Rev Cell Dev Biol 11: 497-514, 1995
    • (1995) Ann Rev Cell Dev Biol , vol.11 , pp. 497-514
    • Schafer, D.A.1    Cooper, J.A.2
  • 8
    • 0023272783 scopus 로고
    • r 43,000 tropomyosin binding protein from human erythrocyte membranes
    • r 43,000 tropomyosin binding protein from human erythrocyte membranes. J Biol Chem 262: 12792-12800, 1987
    • (1987) J Biol Chem , vol.262 , pp. 12792-12800
    • Fowler, V.M.1
  • 9
    • 0030021105 scopus 로고    scopus 로고
    • Regulation of actin filament length in erythrocytes and muscle
    • Fowler VM: Regulation of actin filament length in erythrocytes and muscle. Curr Opin Cell Biol 8: 86-96, 1996
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 86-96
    • Fowler, V.M.1
  • 10
    • 0019853076 scopus 로고
    • 7-chloro-4-nitrobenzeno-2-oxa-1,3-diazole actin as a probe for actin polymerization
    • Detmers P, Weber A, Elzinga M, Stephens RE: 7-chloro-4-nitrobenzeno-2-oxa-1,3-diazole actin as a probe for actin polymerization. J Biol Chem 256: 99-105, 1981
    • (1981) J Biol Chem , vol.256 , pp. 99-105
    • Detmers, P.1    Weber, A.2    Elzinga, M.3    Stephens, R.E.4
  • 11
  • 14
    • 0027446345 scopus 로고
    • Cofilin is an essential component of the yeast cortical cytoskeleton
    • Moon AL, Janmey PA, Louie KA, Drubin DG: Cofilin is an essential component of the yeast cortical cytoskeleton. J Cell Biol 120: 421-435, 1993
    • (1993) J Cell Biol , vol.120 , pp. 421-435
    • Moon, A.L.1    Janmey, P.A.2    Louie, K.A.3    Drubin, D.G.4
  • 16
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot JA, Mitchison TJ: Actin microfilament dynamics in locomoting cells. Nature 352: 126-131, 1991
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 17
    • 0027293382 scopus 로고
    • Recent quantitative studies of actin filament turnover during cell locomotion
    • Zigmond SH: Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil Cytoskeleton 25: 309-316, 1993
    • (1993) Cell Motil Cytoskeleton , vol.25 , pp. 309-316
    • Zigmond, S.H.1
  • 18
    • 0029351519 scopus 로고
    • Actin cytoskeleton. Missing link for intracellular bacterial motility
    • Pollard TD: Actin cytoskeleton. Missing link for intracellular bacterial motility. Curr Biol 5: 837-840, 1995
    • (1995) Curr Biol , vol.5 , pp. 837-840
    • Pollard, T.D.1
  • 19
    • 0030821155 scopus 로고    scopus 로고
    • Xenopos actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails
    • Rosenblatt J, Agnew BJ, Abe H, Bamburg JR, Mitchison TJ: Xenopos actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails. J Cell Biol 136: 1323-1332, 1997
    • (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
  • 20
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew BJ, Minamide LS, Bamburg JR: Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem 270: 17582-17587, 1995
    • (1995) J Biol Chem , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 21
    • 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: Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium. J Cell Biol 132: 335-344, 1996
    • (1996) J Cell Biol , vol.132 , pp. 335-344
    • Aizawa, H.1    Sutoh, K.2    Yahara, I.3
  • 22
    • 0028464361 scopus 로고
    • At the crossroads of signal transduction and the actin cytoskeleton
    • Sohn RH, Goldschmidt-Clemont PJ: At the crossroads of signal transduction and the actin cytoskeleton. Bioassays 16: 465-472, 1994
    • (1994) Bioassays , vol.16 , pp. 465-472
    • Sohn, R.H.1    Goldschmidt-Clemont, P.J.2
  • 24
    • 0026589150 scopus 로고
    • Profilin-actin complexes directly elongate actin filaments at the barbed end
    • Pring M, Weber A, Bubb MR: Profilin-actin complexes directly elongate actin filaments at the barbed end. Biochemistry 31: 1827-1836, 1992
    • (1992) Biochemistry , vol.31 , pp. 1827-1836
    • Pring, M.1    Weber, A.2    Bubb, M.R.3
  • 25
    • 0021914954 scopus 로고
    • Acrosomal reaction of Thione sperm III. the relationship between actin assembly and water influx during extension of the acrosomal process
    • Tilney LC, Inoue S: Acrosomal reaction of Thione sperm III. The relationship between actin assembly and water influx during extension of the acrosomal process. J Cell Biol 100: 1273-1283, 1985
    • (1985) J Cell Biol , vol.100 , pp. 1273-1283
    • Tilney, L.C.1    Inoue, S.2
  • 26
    • 0020147351 scopus 로고
    • Acrosomal reaction of Thione sperm II. The kinetics and possible mechanism of acrosomal process elongation
    • Tilney LC, Inoue S: Acrosomal reaction of Thione sperm II. The kinetics and possible mechanism of acrosomal process elongation. J Cell Biol 91: 820-827, 1982
    • (1982) J Cell Biol , vol.91 , pp. 820-827
    • Tilney, L.C.1    Inoue, S.2
  • 27
    • 0020790453 scopus 로고
    • Actin from Thyone sperm assembles on only one end of an actin filament: A behaviour regulated by profilin
    • Tilney LC, Bonder EM, Coluccio LM, Mooseker MS: Actin from Thyone sperm assembles on only one end of an actin filament: A behaviour regulated by profilin. J Cell Biol 97: 112-124, 1983
    • (1983) J Cell Biol , vol.97 , pp. 112-124
    • Tilney, L.C.1    Bonder, E.M.2    Coluccio, L.M.3    Mooseker, M.S.4
  • 28
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • Pollard TD, Cooper JA: Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 23: 6631-6641, 1984
    • (1984) Biochemistry , vol.23 , pp. 6631-6641
    • Pollard, T.D.1    Cooper, J.A.2
  • 29
    • 0022621479 scopus 로고
    • Purification and characterization of two isoforms of acantharroeba profilin
    • Kaiser DA, Sato M, Ebert RF, Pollard TD: Purification and characterization of two isoforms of acantharroeba profilin. J Cell Biol 102: 221-226, 1986
    • (1986) J Cell Biol , vol.102 , pp. 221-226
    • Kaiser, D.A.1    Sato, M.2    Ebert, R.F.3    Pollard, T.D.4
  • 30
    • 0026747879 scopus 로고
    • Chicadee encodes a profilin required for intercellular cytoplasm transport during Drosophila oogenesis
    • Cooley L, Verheyen E, Ayers K: Chicadee encodes a profilin required for intercellular cytoplasm transport during Drosophila oogenesis. Cell: 69: 173-184, 1992
    • (1992) Cell , vol.69 , pp. 173-184
    • Cooley, L.1    Verheyen, E.2    Ayers, K.3
  • 31
    • 0025008805 scopus 로고
    • Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells
    • Haarer BK, Lillie SH, Adams AEM, Magdolen V, Bandlow W, Brown SS: Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells. J Cell Biol 110: 105-114, 1989
    • (1989) J Cell Biol , vol.110 , pp. 105-114
    • Haarer, B.K.1    Lillie, S.H.2    Adams, A.E.M.3    Magdolen, V.4    Bandlow, W.5    Brown, S.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.