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Volumn 43, Issue 6, 1998, Pages 813-822

Assembly of tropomyosin isoforms into the cytoskeleton of avian muscle cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MYOSIN; TROPOMYOSIN;

EID: 0031801755     PISSN: 00313998     EISSN: None     Source Type: Journal    
DOI: 10.1203/00006450-199806000-00016     Document Type: Article
Times cited : (6)

References (54)
  • 1
    • 0028938790 scopus 로고
    • The cytoskeleton and morphogenesis of the early Drosophila embryo
    • Sullivan W, Theurkauf WE 1995 The cytoskeleton and morphogenesis of the early Drosophila embryo. Curr Opin Cell Biol 7:18-22
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 18-22
    • Sullivan, W.1    Theurkauf, W.E.2
  • 2
    • 0029055622 scopus 로고
    • The role of the cytoskeleton in renal development
    • Baccalo R 1995 The role of the cytoskeleton in renal development. Semin Nephrol 14:285-290
    • (1995) Semin Nephrol , vol.14 , pp. 285-290
    • Baccalo, R.1
  • 3
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen D 1995 Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science 14:247-251
    • (1995) Science , vol.14 , pp. 247-251
    • Mochly-Rosen, D.1
  • 4
    • 0027358356 scopus 로고
    • Axonal transport and the cytoskeleton
    • Hirokawa N 1993 Axonal transport and the cytoskeleton. Curr Opin Neurobiol 3:724-731
    • (1993) Curr Opin Neurobiol , vol.3 , pp. 724-731
    • Hirokawa, N.1
  • 5
    • 0031050451 scopus 로고    scopus 로고
    • Cell anchorage and the cytoskeleton as partners in growth factor dependent cell cycle progression
    • Assoian RK, Zhu X 1997 Cell anchorage and the cytoskeleton as partners in growth factor dependent cell cycle progression. Curr Opin Cell Biol 9:93-98
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 93-98
    • Assoian, R.K.1    Zhu, X.2
  • 6
    • 0029240366 scopus 로고
    • Signaling, mitogenesis, and the cytoskeleton: Where the action is
    • Carraway KL, Carraway CA 1995 Signaling, mitogenesis, and the cytoskeleton: where the action is. Bioessays 17:171-175
    • (1995) Bioessays , vol.17 , pp. 171-175
    • Carraway, K.L.1    Carraway, C.A.2
  • 7
    • 0030272844 scopus 로고    scopus 로고
    • The compartmentalization of protein synthesis: Importance of cytoskeleton and role in mRNA targeting
    • Hovland R 1996 The compartmentalization of protein synthesis: importance of cytoskeleton and role in mRNA targeting. Int J Biochem Cell Biol 28:1089-1105
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 1089-1105
    • Hovland, R.1
  • 8
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman LS 1996 Thin filament-mediated regulation of cardiac contraction. Annu Rev Physiol 58:447-481
    • (1996) Annu Rev Physiol , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 9
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller JP, Helfman DM 1991 The molecular basis for tropomyosin isoform diversity. Bioessays 13:429-437
    • (1991) Bioessays , vol.13 , pp. 429-437
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 10
    • 0018762433 scopus 로고
    • Structure and function of tropomyosin from muscle and non-muscle sources
    • Smillie LB 1979 Structure and function of tropomyosin from muscle and non-muscle sources. Trends Biochem Sci 4:151-155
    • (1979) Trends Biochem Sci , vol.4 , pp. 151-155
    • Smillie, L.B.1
  • 11
    • 0018881743 scopus 로고
    • Regulation and kinetics of the actin-myosin ATP interaction
    • Adelstein RS, Eisenberg E 1980 Regulation and kinetics of the actin-myosin ATP interaction. Annu Rev Biochem 49:921-956
    • (1980) Annu Rev Biochem , vol.49 , pp. 921-956
    • Adelstein, R.S.1    Eisenberg, E.2
  • 12
    • 0022930024 scopus 로고
    • Low Mr tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin-binding properties
    • Broschat KO, Burgess WR 1986 Low Mr tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin-binding properties. J Biol Chem 261:13350-13359
    • (1986) J Biol Chem , vol.261 , pp. 13350-13359
    • Broschat, K.O.1    Burgess, W.R.2
  • 13
    • 0025613855 scopus 로고
    • Tropomyosin prevents depolymerization of actin filaments from the pointed end
    • Broschat KO 1990 Tropomyosin prevents depolymerization of actin filaments from the pointed end. J Biol Chem 265:21323-21329
    • (1990) J Biol Chem , vol.265 , pp. 21323-21329
    • Broschat, K.O.1
  • 14
    • 0025293491 scopus 로고
    • Striated muscle tropomyosin-enriched microfilaments of developing muscles of chicken embryos
    • Wang S-M, Wang S-H, Lin JL-C, Lin JJ-C 1990 Striated muscle tropomyosin-enriched microfilaments of developing muscles of chicken embryos. J Muscle Res Cell Motil 11:191-202
    • (1990) J Muscle Res Cell Motil , vol.11 , pp. 191-202
    • Wang, S.-M.1    Wang, S.-H.2    Lin, J.L.-C.3    Lin, J.J.-C.4
  • 15
    • 0023032307 scopus 로고
    • Assembly of different isoforms of actin and tropomyosin into the skeletal tropomyosin-enriched microfilaments during differentiation of muscle cells in vitro
    • Lin JJ-C, Lin JL-C 1986 Assembly of different isoforms of actin and tropomyosin into the skeletal tropomyosin-enriched microfilaments during differentiation of muscle cells in vitro. J Cell Biol 103:2173-2183
    • (1986) J Cell Biol , vol.103 , pp. 2173-2183
    • Lin, J.J.-C.1    Lin, J.L.-C.2
  • 16
    • 0025881243 scopus 로고
    • Thin filament changes during in vivo rat heart development
    • L'Ecuyer TJ, Schulte D, Lin JJ-C 1991 Thin filament changes during in vivo rat heart development. Pediatr Res 30:232-238
    • (1991) Pediatr Res , vol.30 , pp. 232-238
    • L'Ecuyer, T.J.1    Schulte, D.2    Lin, J.J.-C.3
  • 17
    • 0026339891 scopus 로고
    • Rate and mechanism of assembly of tropomyosin with actin filaments
    • Weight C, Wegner A, Koch MHJ 1991 Rate and mechanism of assembly of tropomyosin with actin filaments. Biochemistry 30:10700-10707
    • (1991) Biochemistry , vol.30 , pp. 10700-10707
    • Weight, C.1    Wegner, A.2    Koch, M.H.J.3
  • 18
    • 0018324977 scopus 로고
    • Equilibrium of the actin-tropomyosin interaction
    • Wegner A 1979 Equilibrium of the actin-tropomyosin interaction. J Mol Biol 131:839-853
    • (1979) J Mol Biol , vol.131 , pp. 839-853
    • Wegner, A.1
  • 19
    • 0025105127 scopus 로고
    • The amino terminus of muscle tropomyosin is a major determinant for function
    • Cho Y-J, Liu J, Hitchcock-DeGregori SE 1990 The amino terminus of muscle tropomyosin is a major determinant for function. J Biol Chem 265:538-545
    • (1990) J Biol Chem , vol.265 , pp. 538-545
    • Cho, Y.-J.1    Liu, J.2    Hitchcock-DeGregori, S.E.3
  • 20
    • 0027513917 scopus 로고
    • Incorporation of microinjected mutant and wild type recombinant tropomyosins into stress fibers in fibroblasts
    • Ranucci D, Yamakita Y, Matsamura F, Hitchcock-DeGregori SE 1993 Incorporation of microinjected mutant and wild type recombinant tropomyosins into stress fibers in fibroblasts. Cell Motil Cytoskel 24:119-128
    • (1993) Cell Motil Cytoskel , vol.24 , pp. 119-128
    • Ranucci, D.1    Yamakita, Y.2    Matsamura, F.3    Hitchcock-DeGregori, S.E.4
  • 22
    • 0024453411 scopus 로고
    • Biosynthesis of titin in cultured skeletal muscle cells
    • Isaacs WB, Kim IS, Struve A, Fulton AB 1989 Biosynthesis of titin in cultured skeletal muscle cells. J Cell Biol 109:2189-2195
    • (1989) J Cell Biol , vol.109 , pp. 2189-2195
    • Isaacs, W.B.1    Kim, I.S.2    Struve, A.3    Fulton, A.B.4
  • 23
    • 0023414711 scopus 로고
    • Cotranslational assembly of myosin heavy chain in developing skeletal muscle
    • Isaacs WB, Fulton AB 1987 Cotranslational assembly of myosin heavy chain in developing skeletal muscle. Proc Natl Acad Sci USA 84:6174-6178
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6174-6178
    • Isaacs, W.B.1    Fulton, A.B.2
  • 24
    • 84989620678 scopus 로고
    • Assembly of the cytoskcleton in cultured muscle cells
    • Isaacs WB, Fulton AB 1989 Assembly of the cytoskcleton in cultured muscle cells. UCLA Symp Mol Cell Biol 93:137-146
    • (1989) UCLA Symp Mol Cell Biol , vol.93 , pp. 137-146
    • Isaacs, W.B.1    Fulton, A.B.2
  • 25
  • 26
    • 0022349490 scopus 로고
    • Monoclonal antibodies against chicken tropomyosin isoforms: Production, characterization, and application
    • Lin JJ-C, Chou C-S, Lin JJ-C 1985 Monoclonal antibodies against chicken tropomyosin isoforms: Production, characterization, and application. Hybridoma 4:223-242
    • (1985) Hybridoma , vol.4 , pp. 223-242
    • Lin, J.J.-C.1    Chou, C.-S.2    Lin, J.J.-C.3
  • 27
    • 0018177457 scopus 로고
    • Biogenesis of peroxisomes: Intracellular site of synthesis of catalase and urease
    • Goldman BM, Blobel G 1978 Biogenesis of peroxisomes: intracellular site of synthesis of catalase and urease. Proc Natl Acad Sci USA 75:5066-5070
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5066-5070
    • Goldman, B.M.1    Blobel, G.2
  • 28
    • 0027403429 scopus 로고
    • Comparison of magnetic separation with Staph A for the immunoprecipitation of tropomyosin and other cytoskeletal proteins
    • L'Ecuyer TJ, Fulton AB 1993 Comparison of magnetic separation with Staph A for the immunoprecipitation of tropomyosin and other cytoskeletal proteins. BioTechniques 14:436-441
    • (1993) BioTechniques , vol.14 , pp. 436-441
    • L'Ecuyer, T.J.1    Fulton, A.B.2
  • 29
    • 0020538452 scopus 로고
    • Isolation and characterization of tropomyosin-containing microfilaments from cultured cells
    • Matsumura F, Yamashiro-Matsumura S, Lin JJ-C 1983 Isolation and characterization of tropomyosin-containing microfilaments from cultured cells. J Biol Chem 258:6636-6644
    • (1983) J Biol Chem , vol.258 , pp. 6636-6644
    • Matsumura, F.1    Yamashiro-Matsumura, S.2    Lin, J.J.-C.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK 1970 Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J 1979 Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 32
    • 0022978973 scopus 로고
    • Newly synthesized Na, K ATP-ase α-subunit has no cytosolic intermediate in MDCK cells
    • Caplan MJ, Palade GE, Jamieson JD 1986 Newly synthesized Na, K ATP-ase α-subunit has no cytosolic intermediate in MDCK cells. J Biol Chem 261:2860-2865
    • (1986) J Biol Chem , vol.261 , pp. 2860-2865
    • Caplan, M.J.1    Palade, G.E.2    Jamieson, J.D.3
  • 33
    • 0014409499 scopus 로고
    • Inhibitors of protein biosynthesis
    • Grollman AP 1968 Inhibitors of protein biosynthesis. J Biol Chem 243:4089-4094
    • (1968) J Biol Chem , vol.243 , pp. 4089-4094
    • Grollman, A.P.1
  • 34
    • 0020576833 scopus 로고
    • Many cytoskeletal proteins associate with the HeLa cytoskeleton during translation in vitro
    • Fulton AB, Wan KM 1983 Many cytoskeletal proteins associate with the HeLa cytoskeleton during translation in vitro. Cell 32:619-625
    • (1983) Cell , vol.32 , pp. 619-625
    • Fulton, A.B.1    Wan, K.M.2
  • 35
    • 0027184957 scopus 로고
    • Cotranslational assembly of some cytoskeletal proteins: Implications and prospects
    • Fulton AB, L'Ecuyer TJ 1993 Cotranslational assembly of some cytoskeletal proteins: implications and prospects. J Cell Sci 105:867-871
    • (1993) J Cell Sci , vol.105 , pp. 867-871
    • Fulton, A.B.1    L'Ecuyer, T.J.2
  • 36
    • 0018831514 scopus 로고
    • The spatial distribution of polyribosomes in 3T3 cells and the associated assembly of proteins into the skeletal framework
    • Fulton AB, Wan KM, Penman S 1980 The spatial distribution of polyribosomes in 3T3 cells and the associated assembly of proteins into the skeletal framework. Cell 20:849-857
    • (1980) Cell , vol.20 , pp. 849-857
    • Fulton, A.B.1    Wan, K.M.2    Penman, S.3
  • 37
    • 0020512134 scopus 로고
    • Vimentin filaments are assembled from a soluble precursor in avian erythroid cells
    • Blikstad I, Lazarides E 1983 Vimentin filaments are assembled from a soluble precursor in avian erythroid cells. J Cell Biol 96:1803-1808
    • (1983) J Cell Biol , vol.96 , pp. 1803-1808
    • Blikstad, I.1    Lazarides, E.2
  • 38
    • 0014219466 scopus 로고
    • Catalysis of peptide bond formation by 50s ribosomal subunits from Escherichia coli
    • Munro RE 1967 Catalysis of peptide bond formation by 50s ribosomal subunits from Escherichia coli. J Mol Biol 26:147-151
    • (1967) J Mol Biol , vol.26 , pp. 147-151
    • Munro, R.E.1
  • 39
    • 0025691520 scopus 로고
    • Construction, expression, and unexpected regulatory properties of a tropomyosin mutant with a 31-residue deletion at the C-terminus
    • Bartegi A, Ferraz C, Fattoum A, Sri Widada J, Heitz F, Kassab R, Liautard JP 1990 Construction, expression, and unexpected regulatory properties of a tropomyosin mutant with a 31-residue deletion at the C-terminus. Eur J Biochem 194:845-852
    • (1990) Eur J Biochem , vol.194 , pp. 845-852
    • Bartegi, A.1    Ferraz, C.2    Fattoum, A.3    Sri Widada, J.4    Heitz, F.5    Kassab, R.6    Liautard, J.P.7
  • 40
    • 84985735713 scopus 로고
    • Excluded volume as a determinant of macromolecular structure and reactivity
    • Minton AP 1981 Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers 20:2093-2120
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 41
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences
    • Minton AP 1983 The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences. Mol Cell Biochem 55:119-140
    • (1983) Mol Cell Biochem , vol.55 , pp. 119-140
    • Minton, A.P.1
  • 42
    • 0023764056 scopus 로고
    • Posttranslational incorporation of contractile proteins into myofibrils in a cell-free system
    • Bouche M, Goldfine SM, Fischman DA 1988 Posttranslational incorporation of contractile proteins into myofibrils in a cell-free system. J Cell Biol 107:587-596
    • (1988) J Cell Biol , vol.107 , pp. 587-596
    • Bouche, M.1    Goldfine, S.M.2    Fischman, D.A.3
  • 44
    • 0027403002 scopus 로고
    • Vimentin mRNA location changes during muscle development
    • Cripe L, Morris E, Fulton AB 1993 Vimentin mRNA location changes during muscle development. Proc Natl Acad Sci USA 90:2724-2728
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2724-2728
    • Cripe, L.1    Morris, E.2    Fulton, A.B.3
  • 45
    • 0026047846 scopus 로고
    • Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model
    • Krasheninnikov IA, Komar AA, Adzhubei IA 1991 Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model. J Protein Chem 10:445-453
    • (1991) J Protein Chem , vol.10 , pp. 445-453
    • Krasheninnikov, I.A.1    Komar, A.A.2    Adzhubei, I.A.3
  • 46
    • 0026619867 scopus 로고
    • Folding on the ribosome of Escherichia coli tryptophan synthase β subunit nascent chains probed with a conformation-dependent monoclonal antibody
    • Federov AN, Friguet B, Djavadi-Ohaniance L, Alakhov YB, Goldberg ME 1992 Folding on the ribosome of Escherichia coli tryptophan synthase β subunit nascent chains probed with a conformation-dependent monoclonal antibody. J Mol Biol 228:351-358
    • (1992) J Mol Biol , vol.228 , pp. 351-358
    • Federov, A.N.1    Friguet, B.2    Djavadi-Ohaniance, L.3    Alakhov, Y.B.4    Goldberg, M.E.5
  • 47
    • 0026459383 scopus 로고
    • Protein folding within the cell is influenced by controlled rates of polypeptide elongation
    • Crombie T, Swaffield JC, Brown AJ 1992 Protein folding within the cell is influenced by controlled rates of polypeptide elongation. J Mol Biol 228:7-12
    • (1992) J Mol Biol , vol.228 , pp. 7-12
    • Crombie, T.1    Swaffield, J.C.2    Brown, A.J.3
  • 48
    • 0026611165 scopus 로고
    • 2+ regulation of mechanical properties of striated muscle: Mechanistics studies using extraction and replacement of regulatory proteins
    • 2+ regulation of mechanical properties of striated muscle: mechanistics studies using extraction and replacement of regulatory proteins Circ Res 70:865-884
    • (1992) Circ Res , vol.70 , pp. 865-884
    • Moss, R.L.1
  • 49
    • 0028439115 scopus 로고
    • Translation and the cystoskeleton: A mechanism for targeted protein synthesis
    • Hesketh J 1994 Translation and the cystoskeleton: a mechanism for targeted protein synthesis. Mol Biol Rep 19:233-243
    • (1994) Mol Biol Rep , vol.19 , pp. 233-243
    • Hesketh, J.1
  • 50
    • 0029844404 scopus 로고    scopus 로고
    • Alterations in fligth muscle ultrastructure and function m Drosophila tropomyosin mutants
    • Kreuz AJ, Simcox A, Maughan D 1996 Alterations in fligth muscle ultrastructure and function m Drosophila tropomyosin mutants. J Cell Biol 135:673-687
    • (1996) J Cell Biol , vol.135 , pp. 673-687
    • Kreuz, A.J.1    Simcox, A.2    Maughan, D.3
  • 53
    • 0028927032 scopus 로고
    • Molecular genetics of hypertrophic cardiomyopathy
    • Marian AJ, Roberts R 1995 Molecular genetics of hypertrophic cardiomyopathy. Annu Rev Med 46:213-222
    • (1995) Annu Rev Med , vol.46 , pp. 213-222
    • Marian, A.J.1    Roberts, R.2


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