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Volumn 7, Issue 1, 1996, Pages 113-127

Modulation of myosin filament organization by C-protein family members

Author keywords

[No Author keywords available]

Indexed keywords

MUSCLE PROTEIN; MYOSIN HEAVY CHAIN; PROTEIN C;

EID: 0030027029     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.7.1.113     Document Type: Article
Times cited : (51)

References (50)
  • 1
    • 0022384881 scopus 로고
    • Novel thick filament protein of chicken pectoralis muscle: The 86 kd protein. I Purification and characterization
    • Bahler, M., Eppenberger, H.M., and Walliman, T. (1985a). Novel thick filament protein of chicken pectoralis muscle: the 86 kd protein. I Purification and characterization. J. Mol. Biol. 186, 381-391.
    • (1985) J. Mol. Biol. , vol.186 , pp. 381-391
    • Bahler, M.1    Eppenberger, H.M.2    Walliman, T.3
  • 2
    • 0022380096 scopus 로고
    • Novel thick filament protein of chicken pectoralis muscle: The 86 kd protein. II. Distribution and localization
    • Bahler, M.H., Eppenberger, M., and Walliman, T. (1985b). Novel thick filament protein of chicken pectoralis muscle: the 86 kd protein. II. Distribution and localization. J. Mol. Biol. 186, 393-401.
    • (1985) J. Mol. Biol. , vol.186 , pp. 393-401
    • Bahler, M.H.1    Eppenberger, M.2    Walliman, T.3
  • 3
    • 0022899276 scopus 로고
    • The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle
    • Bennett, P., Craig, R., Starr, R., and Offer, G. (1986). The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle. J. Muscle Res. Cell Motil. 7, 550-567.
    • (1986) J. Muscle Res. Cell Motil. , vol.7 , pp. 550-567
    • Bennett, P.1    Craig, R.2    Starr, R.3    Offer, G.4
  • 4
    • 0002490362 scopus 로고
    • Differentiating skeletal muscle cells initially express a ventricular myosin heavy chain
    • Bourke, D.L., Wylie, S.R., Wick, M., and Bandman, E. (1991). Differentiating skeletal muscle cells initially express a ventricular myosin heavy chain. Basic Appl. Myol. 1, 13-21.
    • (1991) Basic Appl. Myol. , vol.1 , pp. 13-21
    • Bourke, D.L.1    Wylie, S.R.2    Wick, M.3    Bandman, E.4
  • 5
    • 0019566636 scopus 로고
    • C-protein from rabbit soleus (red) muscle
    • Callaway, J.E., and Bechtel, P.J. (1981). C-protein from rabbit soleus (red) muscle. Biochem. J. 195, 463-469.
    • (1981) Biochem. J. , vol.195 , pp. 463-469
    • Callaway, J.E.1    Bechtel, P.J.2
  • 6
    • 0017362413 scopus 로고
    • Structure of A-segments from frog and rabbit skeletal muscle
    • Craig, R. (1977). Structure of A-segments from frog and rabbit skeletal muscle. J. Mol. Biol. 109, 69-81.
    • (1977) J. Mol. Biol. , vol.109 , pp. 69-81
    • Craig, R.1
  • 7
    • 0023993251 scopus 로고
    • Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle
    • Davis, J.S. (1988). Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle. J. Muscle Res. Cell Motil. 9, 174-183.
    • (1988) J. Muscle Res. Cell Motil. , vol.9 , pp. 174-183
    • Davis, J.S.1
  • 8
    • 0021259458 scopus 로고
    • Localization of C-protein isoforms in chicken skeletal muscle: Ultrastructural detection using monoclonal antibodies
    • Dennis, J.E., Shimizu, T , Reinach, F.C., and Fischman, D.A. (1984). Localization of C-protein isoforms in chicken skeletal muscle: ultrastructural detection using monoclonal antibodies. J. Cell Biol. 98, 1514-1522.
    • (1984) J. Cell Biol. , vol.98 , pp. 1514-1522
    • Dennis, J.E.1    Shimizu, T.2    Reinach, F.C.3    Fischman, D.A.4
  • 9
    • 0025246301 scopus 로고
    • Isolation and characterization of a cDNA clone encoding avian skeletal C-protein: An intracellular member of the immunoglobulin superfarnily
    • Einheber, S., and Fischman, D A. (1990). Isolation and characterization of a cDNA clone encoding avian skeletal C-protein: an intracellular member of the immunoglobulin superfarnily. Proc. Natl. Acad. Sci. USA 87, 2157-2161.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2157-2161
    • Einheber, S.1    Fischman, D.A.2
  • 10
    • 0024513698 scopus 로고
    • Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain
    • Feghali, R., and Leinwand, L.A. (1989). Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain. J. Cell Biol. 108, 1791-1797.
    • (1989) J. Cell Biol. , vol.108 , pp. 1791-1797
    • Feghali, R.1    Leinwand, L.A.2
  • 12
    • 0026800671 scopus 로고
    • X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 a resolution
    • Holden, H.M., Ito, M., Hartshorne, D.J., and Rayment, I. (1992). X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution. J. Mol. Biol. 227, 840-851.
    • (1992) J. Mol. Biol. , vol.227 , pp. 840-851
    • Holden, H.M.1    Ito, M.2    Hartshorne, D.J.3    Rayment, I.4
  • 13
    • 85012414651 scopus 로고
    • Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle
    • Huxley, H.E. (1963). Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol. 7, 281-308.
    • (1963) J. Mol. Biol. , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 14
    • 0019216704 scopus 로고
    • r 150,000 in perfused rat heart, and the tentative identification of this as C-protein
    • r 150,000 in perfused rat heart, and the tentative identification of this as C-protein. FEBS Lett. 122, 129-132.
    • (1980) FEBS Lett. , vol.122 , pp. 129-132
    • Jeacocke, S.A.1    England, P.J.2
  • 15
    • 0025327985 scopus 로고
    • Generation of a full-length human perinatal myosin heavy-chain-encoding cDNA
    • Karsch-Mizrachi, I., Feghali, R , Shows, T.B , and Leinwand, L.A. (1990). Generation of a full-length human perinatal myosin heavy-chain-encoding cDNA. Gene 59, 289-294.
    • (1990) Gene , vol.59 , pp. 289-294
    • Karsch-Mizrachi, I.1    Feghali, R.2    Shows, T.B.3    Leinwand, L.A.4
  • 16
    • 0024582782 scopus 로고
    • The phosphorylation state of eucaryotic initiation factor 2 alters translational efficiency of specific mRNAs
    • Kaufman, R.J., Davies, M.V., Pathak, V.K., and Hershey, J.W.B. (1989). The phosphorylation state of eucaryotic initiation factor 2 alters translational efficiency of specific mRNAs. Mol. Cell. Biol. 9, 946-958.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 946-958
    • Kaufman, R.J.1    Davies, M.V.2    Pathak, V.K.3    Hershey, J.W.B.4
  • 17
    • 0018674244 scopus 로고
    • Effects of C-protein on synthetic myosin filament structure
    • Koretz, J.F. (1979). Effects of C-protein on synthetic myosin filament structure. Biophys. J. 27, 433-446.
    • (1979) Biophys. J. , vol.27 , pp. 433-446
    • Koretz, J.F.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 237, 680-685.
    • (1970) Nature , vol.237 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0025812961 scopus 로고
    • Mutagenesis of the putative fusion domain of Semliki virus spike protein
    • Levy-Mintz, P., and Kielian, M. (1992). Mutagenesis of the putative fusion domain of Semliki virus spike protein. J. Virol. 65, 4292-4300.
    • (1992) J. Virol. , vol.65 , pp. 4292-4300
    • Levy-Mintz, P.1    Kielian, M.2
  • 20
    • 41549105310 scopus 로고
    • Improvements in epoxy resin embedding methods
    • Luft, J.H. (1961). Improvements in epoxy resin embedding methods. J. Biophys. Biochem. Cytol. 9, 409-414.
    • (1961) J. Biophys. Biochem. Cytol. , vol.9 , pp. 409-414
    • Luft, J.H.1
  • 21
    • 0024311374 scopus 로고
    • Evolutionary conserved sequences of striated muscle myosin heavy chain isoforms: Epitope mapping by cDNA expression
    • Miller, J.B., Teal, S.B., and Stockdale, F.E. (1989). Evolutionary conserved sequences of striated muscle myosin heavy chain isoforms: epitope mapping by cDNA expression. J. Biol. Chem. 264, 13122-13130.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13122-13130
    • Miller, J.B.1    Teal, S.B.2    Stockdale, F.E.3
  • 22
    • 0027527672 scopus 로고
    • Segregated assembly of muscle myosin expressed in non-muscle cells
    • Moncman, C.L., Rindt, H., Robbins, J., and Winkelmann, D.A. (1993). Segregated assembly of muscle myosin expressed in non-muscle cells. Mol. Biol. Cell 4, 1051-1067.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1051-1067
    • Moncman, C.L.1    Rindt, H.2    Robbins, J.3    Winkelmann, D.A.4
  • 23
    • 0019723545 scopus 로고
    • Fluorescence microscope study of the binding of added C protein to skeletal muscle myofibrils
    • Moos, C. (1981). Fluorescence microscope study of the binding of added C protein to skeletal muscle myofibrils. J. Cell Biol. 90, 25-31.
    • (1981) J. Cell Biol. , vol.90 , pp. 25-31
    • Moos, C.1
  • 24
    • 0019068808 scopus 로고
    • Effect of C-protein on actomyosin ATPase
    • Moos, C., and Feng, I.-N.M. (1980). Effect of C-protein on actomyosin ATPase. Biochim. Biophys. Acta 632, 141-149.
    • (1980) Biochim. Biophys. Acta , vol.632 , pp. 141-149
    • Moos, C.1    Feng, I.-N.M.2
  • 25
    • 0018126953 scopus 로고
    • The binding of skeletal muscle C-protien to F-actin, and its relation to the interaction of actin with myosin subfragment-1
    • Moos, C., Mason, C.M., Besterman, J.M., Feng, I.-N.M., and Dubin, J.H (1978). The binding of skeletal muscle C-protien to F-actin, and its relation to the interaction of actin with myosin subfragment-1. J. Mol. Biol. 124, 571-586.
    • (1978) J. Mol. Biol. , vol.124 , pp. 571-586
    • Moos, C.1    Mason, C.M.2    Besterman, J.M.3    Feng, I.-N.M.4    Dubin, J.H.5
  • 26
    • 0016818769 scopus 로고
    • Interaction of C-protein with myosin, myosin rod and light meromyosm
    • Moos, C., Offer, G., Starr, R., and Bennett, P. (1975). Interaction of C-protein with myosin, myosin rod and light meromyosm. J. Mol. Biol. 97, 1-9.
    • (1975) J. Mol. Biol. , vol.97 , pp. 1-9
    • Moos, C.1    Offer, G.2    Starr, R.3    Bennett, P.4
  • 27
    • 0021225376 scopus 로고
    • Co-existence of fast-type and slow-type C-proteins in neonatal chicken breast muscle
    • Obinata, T., Kitani, S., Masaki, T., and Fischman, D. (1984). Co-existence of fast-type and slow-type C-proteins in neonatal chicken breast muscle. Dev. Biol. 105, 253-256.
    • (1984) Dev. Biol. , vol.105 , pp. 253-256
    • Obinata, T.1    Kitani, S.2    Masaki, T.3    Fischman, D.4
  • 28
    • 0015924821 scopus 로고
    • A new protein of the thick filament of vertebrate skeletal myofibrils
    • Offer, G., Moos, C., and Starr, R. (1973). A new protein of the thick filament of vertebrate skeletal myofibrils. J. Mol. Biol. 74, 653-676.
    • (1973) J. Mol. Biol. , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 29
    • 0027515217 scopus 로고
    • The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal, immunoglobulin C2 repeat
    • Okagaki, T., Weber, F.E., Fischman, D.A., Vaughan, K.T., Mikawa, T., and Reinach, F.C. (1993). The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal, immunoglobulin C2 repeat. J. Cell Biol 123, 619-626.
    • (1993) J. Cell Biol , vol.123 , pp. 619-626
    • Okagaki, T.1    Weber, F.E.2    Fischman, D.A.3    Vaughan, K.T.4    Mikawa, T.5    Reinach, F.C.6
  • 31
    • 0020650583 scopus 로고
    • Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: Heterogeneity within a single sarcomere
    • Reinach, F.C., Masaki, T., and Fischman, D.A. (1983). Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere. J. Cell Biol. 96, 297-300.
    • (1983) J. Cell Biol. , vol.96 , pp. 297-300
    • Reinach, F.C.1    Masaki, T.2    Fischman, D.A.3
  • 32
    • 0020350969 scopus 로고
    • Isoforms of C-protein in adult chicken skeletal muscle: Detection with monoclonal antibodies
    • Reinach, F.C., Masaki, T , Shafiq, S., Obinata, T., and Fischman, D.A. (1982) Isoforms of C-protein in adult chicken skeletal muscle: detection with monoclonal antibodies. J. Cell Biol. 95, 78-84.
    • (1982) J. Cell Biol. , vol.95 , pp. 78-84
    • Reinach, F.C.1    Masaki, T.2    Shafiq, S.3    Obinata, T.4    Fischman, D.A.5
  • 33
    • 0028278854 scopus 로고
    • The premyofibril: Evidence for its role in myogenesis
    • Rhee, D., Sanger, J.M., and Sanger, J.W. (1994). The premyofibril: evidence for its role in myogenesis. Cell Motil. Cytoskeleton 28, 1-24.
    • (1994) Cell Motil. Cytoskeleton , vol.28 , pp. 1-24
    • Rhee, D.1    Sanger, J.M.2    Sanger, J.W.3
  • 34
    • 1942506926 scopus 로고
    • Cytochemistry and electron microscopy: The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation
    • Sabatini, D.D , Bensch, K., and Barrnett, R.J. (1963). Cytochemistry and electron microscopy: the preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. J. Cell Biol. 17, 19-58.
    • (1963) J. Cell Biol. , vol.17 , pp. 19-58
    • Sabatini, D.D.1    Bensch, K.2    Barrnett, R.J.3
  • 35
    • 0022981355 scopus 로고
    • Developmental progression of myosin gene expression in cultured muscle cells
    • Silberstein, L., Webster, S.G., Travis, M., and Blau, H.M. (1986). Developmental progression of myosin gene expression in cultured muscle cells. Cell 46, 1075-1081.
    • (1986) Cell , vol.46 , pp. 1075-1081
    • Silberstein, L.1    Webster, S.G.2    Travis, M.3    Blau, H.M.4
  • 36
    • 0021843049 scopus 로고
    • Location of C-protein, H-protein and X-protein in rabbit skeletal muscle fibre types
    • Starr, R., Almond, R., and Offer, G. (1985). Location of C-protein, H-protein and X-protein in rabbit skeletal muscle fibre types. J Muscle Res. Cell Motil. 6, 227-256.
    • (1985) J Muscle Res. Cell Motil. , vol.6 , pp. 227-256
    • Starr, R.1    Almond, R.2    Offer, G.3
  • 37
    • 0002854866 scopus 로고
    • Polypeptide chains of intermediate molecular weight in myosin preparations
    • Starr, R., and Offer, G. (1971). Polypeptide chains of intermediate molecular weight in myosin preparations. FEBS Lett. 15, 40-14.
    • (1971) FEBS Lett. , vol.15 , pp. 40-114
    • Starr, R.1    Offer, G.2
  • 38
    • 0017826080 scopus 로고
    • The interaction of C-protein with heavy meromyosin and subfragment 2
    • Starr, R., and Offer, G. (1978). The interaction of C-protein with heavy meromyosin and subfragment 2. Biochem. J. 171, 813-816.
    • (1978) Biochem. J. , vol.171 , pp. 813-816
    • Starr, R.1    Offer, G.2
  • 39
    • 0021069784 scopus 로고
    • H-protein and X-protein: Two new components of the thick filaments of vertebrate skeletal muscle
    • Starr, R., and Offer, G. (1983). H-protein and X-protein: two new components of the thick filaments of vertebrate skeletal muscle. J. Mol. Biol. 170, 675-698.
    • (1983) J. Mol. Biol. , vol.170 , pp. 675-698
    • Starr, R.1    Offer, G.2
  • 40
    • 0024740978 scopus 로고
    • Size and charge heterogeneity of C-protein isoforms in avian skeletal muscle: Expression of six different isoforms in chicken muscle
    • Takano-Ohmuro, H., Goldfine, S.M., Kojima, T., Obinata, T., and Fischman, D.A. (1989). Size and charge heterogeneity of C-protein isoforms in avian skeletal muscle: expression of six different isoforms in chicken muscle J. Muscle Res. Cell. Motil. 10, 369-378.
    • (1989) J. Muscle Res. Cell. Motil. , vol.10 , pp. 369-378
    • Takano-Ohmuro, H.1    Goldfine, S.M.2    Kojima, T.3    Obinata, T.4    Fischman, D.A.5
  • 41
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Nat Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Nat Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 42
    • 0027407773 scopus 로고
    • Molecular cloning of chicken myosin-binding protein (MyBP) H (86-kDA protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs
    • Vaughan, K.T., Weber, F.E., Einheber, S., and Fischman, D.A. (1993a). Molecular cloning of chicken myosin-binding protein (MyBP) H (86-kDA protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs. J. Biol. Chem. 268, 3670-3676.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3670-3676
    • Vaughan, K.T.1    Weber, F.E.2    Einheber, S.3    Fischman, D.A.4
  • 43
    • 0027083562 scopus 로고
    • cDNA cloning and sequence comparisons of human and chicken muscle C-protein and 86kD protein
    • Vaughan, K.T., Weber, F.E., and Fischman, D.A. (1992). cDNA cloning and sequence comparisons of human and chicken muscle C-protein and 86kD protein. Symp. Soc. Exp. Biol. 46, 167-177.
    • (1992) Symp. Soc. Exp. Biol. , vol.46 , pp. 167-177
    • Vaughan, K.T.1    Weber, F.E.2    Fischman, D.A.3
  • 44
    • 0027285758 scopus 로고
    • Human myosin binding protein H (MyBP-H): Complete primary sequence, genomic organization, and chromosomal location
    • Vaughan, K.T., Weber, F.E., Reid, T., Ward, D.C., Reinach, F.C., and Fischman, D.A. (1993b) Human myosin binding protein H (MyBP-H): complete primary sequence, genomic organization, and chromosomal location. Genomics 16, 34-40.
    • (1993) Genomics , vol.16 , pp. 34-40
    • Vaughan, K.T.1    Weber, F.E.2    Reid, T.3    Ward, D.C.4    Reinach, F.C.5    Fischman, D.A.6
  • 45
    • 0027436343 scopus 로고
    • Sarcomeric myosin heavy chain expressed in nonmuscle cells forms thick filaments in the presence of substoichiometric amounts of light chains
    • Vikstrom, K.L., Rovner, A.S , Saez, C.G., Bravo-Zehnder, M., Straceski, A.J , and Leinwand, L.A. (1993). Sarcomeric myosin heavy chain expressed in nonmuscle cells forms thick filaments in the presence of substoichiometric amounts of light chains. Cell Motil. Cytoskeleton 26, 192-204.
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 192-204
    • Vikstrom, K.L.1    Rovner, A.S.2    Saez, C.G.3    Bravo-Zehnder, M.4    Straceski, A.J.5    Leinwand, L.A.6
  • 46
    • 0002738505 scopus 로고
    • A year in the life of the immunoglobulin superfamily
    • Williams, A.F. (1987). A year in the life of the immunoglobulin superfamily Immunol. Today 8, 298-303.
    • (1987) Immunol. Today , vol.8 , pp. 298-303
    • Williams, A.F.1
  • 47
    • 0027168759 scopus 로고
    • Complete sequence of human fast-type and slow-type muscle myosin binding protein C (MyBP-C): Differential expression, conserved domain structure and chromosome assignment
    • Weber, F.E., Vaughan, K.T., Reinach, F.C., and Fischman, D.A. (1993). Complete sequence of human fast-type and slow-type muscle myosin binding protein C (MyBP-C): differential expression, conserved domain structure and chromosome assignment. Euro. J. Biochem 226, 661-669.
    • (1993) Euro. J. Biochem , vol.226 , pp. 661-669
    • Weber, F.E.1    Vaughan, K.T.2    Reinach, F.C.3    Fischman, D.A.4
  • 48
    • 0021194773 scopus 로고
    • Characterization of H-protein, a component of skeletal muscle myofibrils
    • Yamamoto, K. (1984). Characterization of H-protein, a component of skeletal muscle myofibrils. J. Biol. Chem. 259, 7163-7168.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7163-7168
    • Yamamoto, K.1
  • 49
    • 0023029653 scopus 로고
    • The binding of skeletal muscle C-protein to regulated actin
    • Yamamoto, K. (1986). The binding of skeletal muscle C-protein to regulated actin. FEBS Lett. 208, 123-127.
    • (1986) FEBS Lett. , vol.208 , pp. 123-127
    • Yamamoto, K.1
  • 50
    • 0023838427 scopus 로고
    • Effect of H-protein on the formation of myosin filaments and light meromyosin paracrystals
    • Yamamoto, K. (1988). Effect of H-protein on the formation of myosin filaments and light meromyosin paracrystals. J. Biochem. 303, 274-280.
    • (1988) J. Biochem. , vol.303 , pp. 274-280
    • Yamamoto, K.1


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