메뉴 건너뛰기




Volumn 823, Issue 1-2, 1999, Pages 129-140

A quantitative analysis of G-actin binding proteins and the G-actin pool in developing chick brain

Author keywords

thymosin; ADF; Cofilin; Developing chick brain; G actin; Profilin

Indexed keywords

ACTIN BINDING PROTEIN; ACTIN DEPOLYMERIZING FACTOR; BRAIN EXTRACT; CELL PROTEIN; COFILIN; G ACTIN; PROFILIN; THYMOSIN BETA4;

EID: 0033608731     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(99)01147-6     Document Type: Article
Times cited : (44)

References (56)
  • 1
    • 0024468554 scopus 로고
    • A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle
    • Tokyo
    • H. Abe, S. Ohshima, T. Obinata, A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle, J. Biochem. (Tokyo) 106 (1989) 696-702.
    • (1989) J. Biochem. , vol.106 , pp. 696-702
    • Abe, H.1    Ohshima, S.2    Obinata, T.3
  • 2
    • 0025108764 scopus 로고
    • Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: Two functionally distinct actin-regulatory proteins exhibit structural homology
    • H. Abe, T. Endo, K. Yamamoto, T. Obinata, Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: two functionally distinct actin-regulatory proteins exhibit structural homology, Biochemistry 29 (1990) 7420-7425.
    • (1990) Biochemistry , vol.29 , pp. 7420-7425
    • Abe, H.1    Endo, T.2    Yamamoto, K.3    Obinata, T.4
  • 3
    • 0025050666 scopus 로고
    • Nucleotide sequence and expression of a cDNa encoding chick brain actin depolymerizing factor
    • M.E. Adams, L.S. Minamide, G. Duester, J.R. Bamburg, Nucleotide sequence and expression of a cDNA encoding chick brain actin depolymerizing factor, Biochemistry 29 (1990) 7414-7420.
    • (1990) Biochemistry , vol.29 , pp. 7414-7420
    • Adams, M.E.1    Minamide, L.S.2    Duester, G.3    Bamburg, J.R.4
  • 4
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • B.J. Agnew, L.S. Minamide, J.R. Bamburg, Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site, J. Biol. Chem. 270 (1995) 17582-17587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 5
    • 0019170917 scopus 로고
    • Partial purification and characterization of an actin depolymerizing factor from brain
    • J.R. Bamburg, J.E. Harris, A.G. Weeds, Partial purification and characterization of an actin depolymerizing factor from brain, FEBS Lett. 121 (1980) 178-182.
    • (1980) FEBS Lett. , vol.121 , pp. 178-182
    • Bamburg, J.R.1    Harris, J.E.2    Weeds, A.G.3
  • 6
    • 0023571668 scopus 로고
    • Distribution and cellular localization of actin depolymerizing factor
    • J.R. Bamburg, D. Bray, Distribution and cellular localization of actin depolymerizing factor, J. Cell Biol. 105 (1987) 2817-2825.
    • (1987) J. Cell Biol. , vol.105 , pp. 2817-2825
    • Bamburg, J.R.1    Bray, D.2
  • 7
    • 0025763462 scopus 로고
    • Purification and characterization of low-molecular weight actin-depolymerizing proteins from brain and cultured cells
    • J.R. Bamburg, L.S. Minamide, T.E. Morgan, S.M. Hayden, K.A. Giuliano, A. Koffer, Purification and characterization of low-molecular weight actin-depolymerizing proteins from brain and cultured cells, Methods Enzymol. 196 (1991) 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
  • 8
    • 0027332655 scopus 로고
    • Alterations in actin-binding beta thymosin expression accompany neuronal differentiation and migration in rat cerebellum
    • B.G. Border, S.-C. Lin, S.T. Griffin, S. Pardue, M. Morrison-Bogorad, Alterations in actin-binding beta thymosin expression accompany neuronal differentiation and migration in rat cerebellum, J. Neurochem. 61 (1993) 2104-2114.
    • (1993) J. Neurochem. , vol.61 , pp. 2104-2114
    • Border, B.G.1    Lin, S.-C.2    Griffin, S.T.3    Pardue, S.4    Morrison-Bogorad, M.5
  • 9
    • 0017065560 scopus 로고
    • Unpolymerized Actin in Fibroblasts and Brain
    • D. Bray, C. Thomas, Unpolymerized actin in fibroblasts and brain, J. Mol. Biol. 105 (1976) 527-544.
    • (1976) J. Mol. Biol. , vol.105 , pp. 527-544
    • Bray, D.1    Thomas, C.2
  • 11
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in nonmuscle cells
    • L. Carlsson, L.-E. Nystrom, Il. Sundkvist, F. Markey, U. Lindberg, Actin polymerizability is influenced by profilin, a low molecular weight protein in nonmuscle cells, J. Mol. Biol. 115 (1977) 465-468.
    • (1977) J. Mol. Biol. , vol.115 , pp. 465-468
    • Carlsson, L.1    Nystrom, L.-E.2    Sundkvist, Il.3    Markey, F.4    Lindberg, U.5
  • 13
    • 26544475606 scopus 로고    scopus 로고
    • Nature of the actin-bound nucleotide differentially influences the binding of ADF and cofilin to G-actin
    • H. Chen, S. Kelly, A. Tang, J.R. Bamburg, Nature of the actin-bound nucleotide differentially influences the binding of ADF and cofilin to G-actin, FASEB J. 11 (1997) A985.
    • (1997) FASEB J. , vol.11
    • Chen, H.1    Kelly, S.2    Tang, A.3    Bamburg, J.R.4
  • 14
    • 0022619258 scopus 로고
    • Purification and characterization of actophorin, a new 15,000-Da actin-binding protein from Acanthamoeba castellanii
    • J.A. Cooper, J.D. Blum, R.C. Williams Jr., T.D. Pollard, Purification and characterization of actophorin, a new 15,000-Da actin-binding protein from Acanthamoeba castellanii, J. Biol. Chem. 261 (1986) 477-485.
    • (1986) J. Biol. Chem. , vol.261 , pp. 477-485
    • Cooper, J.A.1    Blum, J.D.2    Williams R.C., Jr.3    Pollard, T.D.4
  • 16
    • 0022451827 scopus 로고
    • 4-like peptides by high-pressure liquid chromatography
    • 4-like peptides by high-pressure liquid chromatography, Anal. Biochem. 156 (1986) 390-396.
    • (1986) Anal. Biochem. , vol.156 , pp. 390-396
    • Hannappel, E.1
  • 17
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- And F-actin
    • S.M. Hayden, P.S. Miller, A. Brauweiler, J.R. Bamburg, Analysis of the interactions of actin depolymerizing factor with G- and F-actin, Biochemistry 32 (1993) 9994-10004.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 18
    • 0026724890 scopus 로고
    • Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin
    • P.A. Janmey, J. Lamb, P.G. Allen, P.T. Matsudaira, Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin, J. Biol. Chem. 267 (1992) 11818-11823.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11818-11823
    • Janmey, P.A.1    Lamb, J.2    Allen, P.G.3    Matsudaira, P.T.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0023037420 scopus 로고
    • Purification and characterization of actobindin, a new actin monomer-binding protein from Acanthamoeba
    • P.K. Lambooy, E.D. Korn, Purification and characterization of actobindin, a new actin monomer-binding protein from Acanthamoeba, J. Biol. Chem. 261 (1986) 17150-17155.
    • (1986) J. Biol. Chem. , vol.261 , pp. 17150-17155
    • Lambooy, P.K.1    Korn, E.D.2
  • 21
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin
    • I. Lassing, U. Lindberg, Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin, Nature 314 (1985) 472-474.
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 22
    • 0025653344 scopus 로고
    • Developmental expression of mRNAs encoding thymosins beta four and beta ten in rat brain and other tissues
    • S.C. Lin, M. Morrison-Bogorad, Developmental expression of mRNAs encoding thymosins beta four and beta ten in rat brain and other tissues, J. Mol. Neurosci. 2 (1990) 35-44.
    • (1990) J. Mol. Neurosci. , vol.2 , pp. 35-44
    • Lin, S.C.1    Morrison-Bogorad, M.2
  • 23
    • 0024289542 scopus 로고
    • The use of poly(L-proline)-Sepharose in the isolation of profilin and profilactin complexes
    • U. Lindberg, C.E. Schutt, E. Hellsten, A.-C. Tjaeder, T. Huit, The use of poly(L-proline)-Sepharose in the isolation of profilin and profilactin complexes, Biochim. Biophys. Acta 967 (1988) 391-400.
    • (1988) Biochim. Biophys. Acta , vol.967 , pp. 391-400
    • Lindberg, U.1    Schutt, C.E.2    Hellsten, E.3    Tjaeder, A.-C.4    Huit, T.5
  • 25
    • 0028981496 scopus 로고
    • Actin-based movement of Listeria monocytogenes: Actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface
    • J.-B. Marchand, P. Moreau, A. Paoletti, P. Cossart, M.-F. Carlier, D. Pantaloni, 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
  • 26
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing 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 depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension, J. Cell Motil. Cytoskel. 39 (1998) 172-190.
    • (1998) J. Cell Motil. Cytoskel. , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 27
    • 0029799252 scopus 로고    scopus 로고
    • Slow axonal transport of soluble actin with actin depolymerizing factor, cofilin and profilin suggests actin moves in an unassembled form
    • R.G. Mills, L.S. Minamide, A. Yuan, J.R. Bamburg, J.J. Bray, Slow axonal transport of soluble actin with actin depolymerizing factor, cofilin and profilin suggests actin moves in an unassembled form, J. Neurochem. 67 (1996) 1225-1234.
    • (1996) J. Neurochem. , vol.67 , pp. 1225-1234
    • Mills, R.G.1    Minamide, L.S.2    Yuan, A.3    Bamburg, J.R.4    Bray, J.J.5
  • 28
    • 0024994046 scopus 로고
    • A filter paper dye-binding assay for quantitative determination of protein without interference from reducing agents or detergents
    • L.S. Minamide, J.R. Bamburg, A filter paper dye-binding assay for quantitative determination of protein without interference from reducing agents or detergents, Anal. Biochem. 190 (1990) 66-70.
    • (1990) Anal. Biochem. , vol.190 , pp. 66-70
    • Minamide, L.S.1    Bamburg, J.R.2
  • 30
    • 0025213355 scopus 로고
    • Destrin, a mammalian actin-depolymerizing protein, is closely related to cofilin. Cloning and expression of porcine brain destrin cDNA
    • K. Moriyama, E. Nishida, N. Yonezawa, H. Sakai, S. Matsumoto, K. Iida, I. Yahara, Destrin, a mammalian actin-depolymerizing protein, is closely related to cofilin. Cloning and expression of porcine brain destrin cDNA, J. Biol. Chem. 265 (1990) 5768-5773.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5768-5773
    • Moriyama, K.1    Nishida, E.2    Yonezawa, N.3    Sakai, H.4    Matsumoto, S.5    Iida, K.6    Yahara, I.7
  • 31
    • 0025840384 scopus 로고
    • Vinculin in relation to stress fibers in spread platelets
    • V.T. Nachmias, R. Golla, Vinculin in relation to stress fibers in spread platelets, Cell Motil. Cytoskel. 20 (1991) 190-202.
    • (1991) Cell Motil. Cytoskel. , vol.20 , pp. 190-202
    • Nachmias, V.T.1    Golla, R.2
  • 32
    • 0026501647 scopus 로고
    • G-actin pool and actin messenger RNA during development of the apical processes of the retinal pigment epithelial cells of the chick
    • V.T. Nachmias, N. Philp, Y. Momoyama, J.K. Choi, G-actin pool and actin messenger RNA during development of the apical processes of the retinal pigment epithelial cells of the chick, Dev. Biol. 149 (1992) 239-246.
    • (1992) Dev. Biol. , vol.149 , pp. 239-246
    • Nachmias, V.T.1    Philp, N.2    Momoyama, Y.3    Choi, J.K.4
  • 34
    • 0030023293 scopus 로고    scopus 로고
    • Cap Z, a calcium insensitive capping protein in resting and activated platelets
    • V.T. Nachmias, R. Golla, J.F. Casella, E. Barron-Casella, Cap Z, a calcium insensitive capping protein in resting and activated platelets, FEBS Lett. 378 (1996) 258-262.
    • (1996) FEBS Lett. , vol.378 , pp. 258-262
    • Nachmias, V.T.1    Golla, R.2    Casella, J.F.3    Barron-Casella, E.4
  • 35
    • 0029829409 scopus 로고    scopus 로고
    • Quantitative analysis of low molecular weight G-actin binding proteins, cofilin, ADF and profilin, expressed in developing and degenerating chicken skeletal muscles
    • R. Nagaoka, N. Minami, K. Hayakawa, H. Abe, T. Obinata, Quantitative analysis of low molecular weight G-actin binding proteins, cofilin, ADF and profilin, expressed in developing and degenerating chicken skeletal muscles, J. Muscle Res. Cell Motil. 17 (1996) 463-473.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 463-473
    • Nagaoka, R.1    Minami, N.2    Hayakawa, K.3    Abe, H.4    Obinata, T.5
  • 36
    • 0021749110 scopus 로고
    • Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • E. Nishida, S. Maekawa, H. Sakai, Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin, Biochemistry 23 (1984) 5307-5313.
    • (1984) Biochemistry , vol.23 , pp. 5307-5313
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 37
    • 0022410877 scopus 로고
    • An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin
    • E. Nishida, E. Muneyuki, S. Maekawa, Y. Ohta, H. Sakai, An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin, Biochemistry 24 (1985) 6624-6630.
    • (1985) Biochemistry , vol.24 , pp. 6624-6630
    • Nishida, E.1    Muneyuki, E.2    Maekawa, S.3    Ohta, Y.4    Sakai, H.5
  • 39
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • P.H. O'Farrell, High resolution two-dimensional electrophoresis of proteins, J. Biol. Chem. 250 (1975) 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 40
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta four
    • D. Pantaloni, M.F. Carlier, How profilin promotes actin filament assembly in the presence of thymosin beta four, Cell 75 (1993) 1007-1014.
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 41
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP and ADP-actin with the ends of actin filaments
    • T.D. Pollard, Rate constants for the reactions of ATP and ADP-actin with the ends of actin filaments, J. Cell Biol. 103 (1986) 2747-2754.
    • (1986) J. Cell Biol. , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 42
    • 0024543601 scopus 로고
    • An electrophoretic procedure for detecting proteins that bind actin monomers
    • D. Safer, An electrophoretic procedure for detecting proteins that bind actin monomers, Anal. Biochem. 178 (1989) 32-37.
    • (1989) Anal. Biochem. , vol.178 , pp. 32-37
    • Safer, D.1
  • 43
    • 0025355476 scopus 로고
    • Isolation of a 5-kDa actin-sequestering peptide from human blood platelets
    • D. Safer, R. Golla, V.T. Nachmias, Isolation of a 5-kDa actin-sequestering peptide from human blood platelets, Proc. Natl. Acad. Sci. USA 87 (1990) 2536-2540.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2536-2540
    • Safer, D.1    Golla, R.2    Nachmias, V.T.3
  • 44
    • 0025856003 scopus 로고
    • 4 and Fx, an actin-sequestering peptide, are indistinguishable
    • 4 and Fx, an actin-sequestering peptide, are indistinguishable, J. Biol. Chem. 266 (1991) 4029-4032.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4029-4032
    • Safer, D.1    Elzinga, M.2    Nachmias, V.T.3
  • 45
    • 0005789093 scopus 로고
    • G-actin and thymosin beta four in chick embryo fibroblasts
    • D. Safer, N. Devineni, G-actin and thymosin beta four in chick embryo fibroblasts, Mol. Biol. Cell 4 (1993) 383a.
    • (1993) Mol. Biol. Cell , vol.4
    • Safer, D.1    Devineni, N.2
  • 46
    • 0028465425 scopus 로고
    • Beta thymosins as actin binding peptides
    • D. Safer, V.T. Nachmias, Beta thymosins as actin binding peptides, BioEssays 16 (1994) 473-479.
    • (1994) BioEssays , vol.16 , pp. 473-479
    • Safer, D.1    Nachmias, V.T.2
  • 48
    • 0025340881 scopus 로고
    • The actin released from profilin-actin complexes is insufficient to account for the increase in F-actin in chemoattractant-stimulated polymorphonuclear leukocytes
    • F.S. Southwick, C.L. Young, The actin released from profilin-actin complexes is insufficient to account for the increase in F-actin in chemoattractant-stimulated polymorphonuclear leukocytes, J. Cell Biol. 110 (1990) 1965-1973.
    • (1990) J. Cell Biol. , vol.110 , pp. 1965-1973
    • Southwick, F.S.1    Young, C.L.2
  • 50
    • 0026708551 scopus 로고
    • 4 with muscle and platelet actin: Implications for actin sequestration in resting platelets
    • 4 with muscle and platelet actin: implications for actin sequestration in resting platelets, Biochem. 31 (1992) 6179-6185.
    • (1992) Biochem. , vol.31 , pp. 6179-6185
    • Weber, A.1    Nachmias, V.T.2    Pennise, C.R.3    Pring, M.4    Safer, D.5
  • 51
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • D. Wessel, U.I. Fļgge, A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids, Anal. Biochem. 138 (1984) 141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Fļgge, U.I.2
  • 52
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • N. Yonezawa, E. Nishida, H. Sakai, pH control of actin polymerization by cofilin, J. Biol. Chem. 260 (1985) 14410-14412.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14410-14412
    • Yonezawa, N.1    Nishida, E.2    Sakai, H.3
  • 53
    • 0023428481 scopus 로고
    • Distribution among tissues and intracellular localization of cofilin, a 21 kDa actin-binding protein
    • N. Yonezawa, E. Nishida, S. Koyasu, S. Maekawa, Y. Ohta, I. Yahara, H. Sakai, Distribution among tissues and intracellular localization of cofilin, a 21 kDa actin-binding protein, Cell Struct. Funct. 12 (1987) 443-452.
    • (1987) Cell Struct. Funct. , vol.12 , pp. 443-452
    • Yonezawa, N.1    Nishida, E.2    Koyasu, S.3    Maekawa, S.4    Ohta, Y.5    Yahara, I.6    Sakai, H.7
  • 54
    • 0025277362 scopus 로고
    • Inhibition of the interactions of cofilin, destrin and deoxyribonuclease I with actin by phosphoinositides
    • N. Yonezawa, E. Nishida, K. Iida, I. Yahara, H. Sakai, Inhibition of the interactions of cofilin, destrin and deoxyribonuclease I with actin by phosphoinositides, J. Biol. Chem. 265 (1990) 8336-8382.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8336-8382
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.