메뉴 건너뛰기




Volumn 10, Issue 5, 1999, Pages 1297-1308

Different domains of the M-band protein myomesin are involved in myosin binding and M-band targeting

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; CONNECTIN; GREEN FLUORESCENT PROTEIN; MYOMESIN; MYOSIN; RECOMBINANT PROTEIN;

EID: 0032945590     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.5.1297     Document Type: Article
Times cited : (63)

References (52)
  • 1
    • 0022380096 scopus 로고
    • Novel thick filament protein of chicken pectoralis muscle: The 86 kd protein. II. Distribution and localization
    • Bähler, M., Eppenberger, H.M., and Wallimann, T. (1985). 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
    • Bähler, M.1    Eppenberger, H.M.2    Wallimann, T.3
  • 3
    • 0023102940 scopus 로고
    • Diversification of the myofibrillar M band in rat skeletal muscle during postnatal development
    • Carlsson, E., and Thornell, L.E. (1987). Diversification of the myofibrillar M band in rat skeletal muscle during postnatal development. Cell Tissue Res. 248, 169-180.
    • (1987) Cell Tissue Res. , vol.248 , pp. 169-180
    • Carlsson, E.1    Thornell, L.E.2
  • 4
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W.W., and Prasher, D.C. (1994). Green fluorescent protein as a marker for gene expression. Science 263, 802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 5
    • 0017234893 scopus 로고
    • The location of C-protein in rabbit skeletal muscle
    • Craig, R., and Offer, G. (1976). The location of C-protein in rabbit skeletal muscle. Proc. R. Soc. Lond. B Biol. Sci. 192, 325-332.
    • (1976) Proc. R. Soc. Lond. B Biol. Sci. , vol.192 , pp. 325-332
    • Craig, R.1    Offer, G.2
  • 6
    • 0025246301 scopus 로고
    • Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: An intracellular member of the immunoglobulin superfamily
    • Einheber, S., and Fischman, D.A. (1990). Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: an intracellular member of the immunoglobulin superfamily. 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
  • 7
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interactions between titin and myosin-binding protein C: Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg, A., and Gautel, M. (1996). A molecular map of the interactions between titin and myosin-binding protein C: implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem. 235, 317-323.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 8
    • 0029006530 scopus 로고
    • The anatomy of molecular giant: How the sarcomere cytoskeleton is assembled from immunoglobulin superfamily molecules
    • Fürst, D.O., and Gautel, M. (1995). The anatomy of molecular giant: how the sarcomere cytoskeleton is assembled from immunoglobulin superfamily molecules. J. Mol. Cell. Cardiol. 27, 951-959.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 951-959
    • Fürst, D.O.1    Gautel, M.2
  • 9
    • 0024348057 scopus 로고
    • Myogenesis in the mouse embryo: Differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly
    • Fürst, D.O., Osborn, M., and Weber, K. (1989). Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly. J. Cell Biol. 109, 517-527.
    • (1989) J. Cell Biol. , vol.109 , pp. 517-527
    • Fürst, D.O.1    Osborn, M.2    Weber, K.3
  • 10
    • 0021795178 scopus 로고
    • A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
    • Gallione, C.J., and Rose, J.K. (1985). A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. J. Virol. 54, 374-382.
    • (1985) J. Virol. , vol.54 , pp. 374-382
    • Gallione, C.J.1    Rose, J.K.2
  • 11
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/ connectin elasticity reveals two different mechanisms acting in series
    • Gautel, M., and Goulding, D. (1996). A molecular map of titin/ connectin elasticity reveals two different mechanisms acting in series. FEBS Lett. 385, 11-14.
    • (1996) FEBS Lett. , vol.385 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 12
    • 0030030825 scopus 로고    scopus 로고
    • The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle
    • Gilbert, R., Kelly, M.G., Mikawa, T., and Fischman, D.A. (1996). The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle. J. Cell Sci. 109, 101-111.
    • (1996) J. Cell Sci. , vol.109 , pp. 101-111
    • Gilbert, R.1    Kelly, M.G.2    Mikawa, T.3    Fischman, D.A.4
  • 13
    • 0022344532 scopus 로고
    • Myomesin and M-protein: Expression of two M-band proteins in pectoral muscle and heart during development
    • Grove, B.K., Cerny, L., Perriard, J.-C., and Eppenberger, H.M. (1985). Myomesin and M-protein: expression of two M-band proteins in pectoral muscle and heart during development. J. Cell Biol. 101, 1413-1421.
    • (1985) J. Cell Biol. , vol.101 , pp. 1413-1421
    • Grove, B.K.1    Cerny, L.2    Perriard, J.-C.3    Eppenberger, H.M.4
  • 17
    • 0023047016 scopus 로고
    • A physiological role for titin and nebulin in skeletal muscle
    • Horowits, R., Kempner, E.S., Bisher, M.E., and Podolsky, R.J. (1986). A physiological role for titin and nebulin in skeletal muscle. Nature 23, 160-164.
    • (1986) Nature , vol.23 , pp. 160-164
    • Horowits, R.1    Kempner, E.S.2    Bisher, M.E.3    Podolsky, R.J.4
  • 18
    • 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
  • 19
    • 0029837673 scopus 로고    scopus 로고
    • The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition
    • Komiyama, M., Soldati, T., von Arx, P., and Perriard, J.-C. (1996). The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition. J. Cell Sci. 109, 2089-2099.
    • (1996) J. Cell Sci. , vol.109 , pp. 2089-2099
    • Komiyama, M.1    Soldati, T.2    Von Arx, P.3    Perriard, J.-C.4
  • 20
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M. (1989). The scanning model for translation: an update. J. Cell Biol. 108, 229-241.
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 21
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S., and Kolmerer, B. (1995). Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270, 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 22
    • 0018121212 scopus 로고
    • Interaction studies of the 165,000 dalton protein component of the M-line with the S2 subfragment of myosin
    • Mani, R.S., and Kay, CM. (1978). Interaction studies of the 165,000 dalton protein component of the M-line with the S2 subfragment of myosin. Biochim. Biophys. Acta 536, 134-141.
    • (1978) Biochim. Biophys. Acta , vol.536 , pp. 134-141
    • Mani, R.S.1    Kay, C.M.2
  • 24
    • 0018133199 scopus 로고
    • SDS microslab linear gradient PAGE
    • Matsudaira, P., and Burgess, D.R. (1978). SDS microslab linear gradient PAGE. Anal. Biochem. 87, 386-396.
    • (1978) Anal. Biochem. , vol.87 , pp. 386-396
    • Matsudaira, P.1    Burgess, D.R.2
  • 26
    • 0027364752 scopus 로고
    • Three-dimensional visualization of multi-channel volume data: The amSFP algorithm
    • Messerli J.M., van der Voort, H.T.M., Rungger-Brändle, E., and Perriard, J.-C. (1993b). Three-dimensional visualization of multi-channel volume data: the amSFP algorithm. Cytometry 14, 725-735.
    • (1993) Cytometry , vol.14 , pp. 725-735
    • Messerli, J.M.1    Van Der Voort, H.T.M.2    Rungger-Brändle, E.3    Perriard, J.-C.4
  • 27
    • 0024440423 scopus 로고
    • Visualization of the polarity of isolated titin molecules: A single globular head on a long thin rod as the M band anchoring domain?
    • Nave, R., Fürst, D.O., and Weber, K. (1989). Visualization of the polarity of isolated titin molecules: a single globular head on a long thin rod as the M band anchoring domain? J. Cell Biol. 209, 2177-2187.
    • (1989) J. Cell Biol. , vol.209 , pp. 2177-2187
    • Nave, R.1    Fürst, D.O.2    Weber, K.3
  • 28
    • 0026668036 scopus 로고
    • Complete primary structure and tissue specific expression of chicken pectoralis M-protein
    • Noguchi, J., Yanagisawa, M., Imamura, M., Kasuiya, Y., Sakurai, T., Tanaka, T., and Masaki, T. (1992). Complete primary structure and tissue specific expression of chicken pectoralis M-protein. J. Biol. Chem. 267, 20302-20310.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20302-20310
    • Noguchi, J.1    Yanagisawa, M.2    Imamura, M.3    Kasuiya, Y.4    Sakurai, T.5    Tanaka, T.6    Masaki, T.7
  • 29
    • 0031034775 scopus 로고    scopus 로고
    • Molecular structure of the M band: Mapping of titin- and myosin-binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin
    • Obermann, W.M., Gautel, M., Weber, K., and Fürst, D.O. (1997). Molecular structure of the M band: mapping of titin- and myosin-binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin. EMBO J. 16, 211-220.
    • (1997) EMBO J. , vol.16 , pp. 211-220
    • Obermann, W.M.1    Gautel, M.2    Weber, K.3    Fürst, D.O.4
  • 30
    • 0028838439 scopus 로고
    • Purification and biochemical characterization of myomesin, a myosin- and titin-binding protein, from bovine skeletal muscle
    • Obermann, W.M., Plessmann, U., Weber, K., and Fürst, D.O. (1995). Purification and biochemical characterization of myomesin, a myosin- and titin-binding protein, from bovine skeletal muscle. Eur. J. Biochem. 233, 110-115.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 110-115
    • Obermann, W.M.1    Plessmann, U.2    Weber, K.3    Fürst, D.O.4
  • 31
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: Localization of defined domains of myomesin, M-protein and the 250-kDa carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann, W.M.J., Gautel, M., Steiner, F., van der Veen, P.F.M., Weber, K., and Fürst, D.O. (1996). The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein and the 250-kDa carboxy-terminal region of titin by immunoelectron microscopy. J. Cell Biol. 134, 1441-1453.
    • (1996) J. Cell Biol. , vol.134 , pp. 1441-1453
    • Obermann, W.M.J.1    Gautel, M.2    Steiner, F.3    Van Der Veen, P.F.M.4    Weber, K.5    Fürst, D.O.6
  • 32
    • 0031897698 scopus 로고    scopus 로고
    • Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band
    • Obermann, W.M.J., van der Ven, P.F.M., Steiner, F., Weber, K., and Fürst, D.O. (1998). Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band. Mol. Biol. Cell 9, 829-840.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 829-840
    • Obermann, W.M.J.1    Van Der Ven, P.F.M.2    Steiner, F.3    Weber, K.4    Fürst, D.O.5
  • 33
    • 0015924821 scopus 로고
    • A new protein of the thick filaments of vertebrate skeletal myofibrils. Extraction, purification and characterization
    • Offer, G., Moos, C., and Starr, R. (1973). A new protein of the thick filaments of vertebrate skeletal myofibrils. Extraction, purification and characterization. J. Mol. Biol. 74, 653-676.
    • (1973) J. Mol. Biol. , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 34
    • 0027515217 scopus 로고
    • The major myosin-binding domain of skeletal muscle MyPB-C (C-protein) resides in the COOH-terminal, immunoglobulin C2 motif
    • 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 MyPB-C (C-protein) resides in the COOH-terminal, immunoglobulin C2 motif. 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
  • 35
    • 0028586108 scopus 로고
    • M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles
    • Pask, H.T., Jones, K.L., Luther, P.K., and Squire, J.M. (1994). M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles. J. Muscle Res. Cell Motil. 35, 633-645.
    • (1994) J. Muscle Res. Cell Motil. , vol.35 , pp. 633-645
    • Pask, H.T.1    Jones, K.L.2    Luther, P.K.3    Squire, J.M.4
  • 36
    • 0028058747 scopus 로고
    • Immunoglobulin-type domains of titin are stabilized by amino-terminal extension
    • Politou, A.S., Gautel, M., Joseph, C., and Pastore, A. (1994). Immunoglobulin-type domains of titin are stabilized by amino-terminal extension. FEBS Lett. 352, 27-31.
    • (1994) FEBS Lett. , vol.352 , pp. 27-31
    • Politou, A.S.1    Gautel, M.2    Joseph, C.3    Pastore, A.4
  • 37
    • 0023227133 scopus 로고
    • Skelemins: Cytoskeletal proteins located at the periphery of M-discs in mammalian striated muscle
    • Price, M.G. (1987). Skelemins: cytoskeletal proteins located at the periphery of M-discs in mammalian striated muscle. J. Cell Biol. 104, 1325-1336.
    • (1987) J. Cell Biol. , vol.104 , pp. 1325-1336
    • Price, M.G.1
  • 39
    • 0023895438 scopus 로고
    • Intracellular targeting of isoproteins in muscle cytoarchitecture
    • Schäfer, B.W., and Perriard, J.-C. (1988). Intracellular targeting of isoproteins in muscle cytoarchitecture. J. Cell Biol. 106, 1161-1170.
    • (1988) J. Cell Biol. , vol.106 , pp. 1161-1170
    • Schäfer, B.W.1    Perriard, J.-C.2
  • 41
    • 0024232653 scopus 로고
    • Terminally differentiated neonatal rat myocardial cells proliferate and maintain specific differentiated functions following expression of SV40 large T antigen
    • Sen, A., Dunnmon, P., Henderson, S.A., Gerard, R.D., and Chien, K.R. (1988). Terminally differentiated neonatal rat myocardial cells proliferate and maintain specific differentiated functions following expression of SV40 large T antigen. J. Biol. Chem. 263, 19132-19136.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19132-19136
    • Sen, A.1    Dunnmon, P.2    Henderson, S.A.3    Gerard, R.D.4    Chien, K.R.5
  • 42
  • 43
    • 0025917462 scopus 로고
    • Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging
    • Soldati, T., and Perriard, J.C. (1991). Intracompartmental sorting of essential myosin light chains: molecular dissection and in vivo monitoring by epitope tagging. Cell 66, 277-289.
    • (1991) Cell , vol.66 , pp. 277-289
    • Soldati, T.1    Perriard, J.C.2
  • 44
    • 0021843049 scopus 로고
    • Location of C-protein, H-protein and X-protein in rabbit skeletal muscle fiber types
    • Starr, R., Almond, R., and Offer, G. (1985). Location of C-protein, H-protein and X-protein in rabbit skeletal muscle fiber 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
  • 45
    • 0031781884 scopus 로고    scopus 로고
    • Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: Allocation of N-terminal binding epitope in MM-CK and BB-CK
    • Stolz, M., and Wallimann, T. (1998). Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: allocation of N-terminal binding epitope in MM-CK and BB-CK. J. Cell Sci. 111, 1207-1216.
    • (1998) J. Cell Sci. , vol.111 , pp. 1207-1216
    • Stolz, M.1    Wallimann, T.2
  • 46
    • 0025877737 scopus 로고
    • Elastic filaments and giant proteins in muscle
    • Trinick, J. (1991). Elastic filaments and giant proteins in muscle. Curr. Opin. Cell Biol. 3, 112-119.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 112-119
    • Trinick, J.1
  • 47
    • 0028091960 scopus 로고
    • Titin and nebulin: Protein rulers in muscle?
    • Trinick, J. (1994). Titin and nebulin: protein rulers in muscle? Trends Biochem. Sci. 19, 405-409.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 405-409
    • Trinick, J.1
  • 48
    • 0015598038 scopus 로고
    • A protein that binds specifically to the M-line of skeletal muscle is identified as the muscle form of creatine kinase
    • Turner, D.C., Wallimann, T., and Eppenberger, H.M. (1973). A protein that binds specifically to the M-line of skeletal muscle is identified as the muscle form of creatine kinase. Proc. Natl. Acad. Sci. USA 70, 702-705.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 702-705
    • Turner, D.C.1    Wallimann, T.2    Eppenberger, H.M.3
  • 49
    • 1842334510 scopus 로고    scopus 로고
    • Assembly of titin, myomesin and M-protein into the sarcomeric M band in differentiating human skeletal muscle cells in vitro
    • van der Ven, P.F., and Fürst, D.O. (1997). Assembly of titin, myomesin and M-protein into the sarcomeric M band in differentiating human skeletal muscle cells in vitro. Cell Struct. Funct. 22, 163-171.
    • (1997) Cell Struct. Funct. , vol.22 , pp. 163-171
    • Van Der Ven, P.F.1    Fürst, D.O.2
  • 50
    • 0027374159 scopus 로고
    • The globular head domain of titin extends into the center of the sarcomeric M band
    • Vinkemeier, U., Obermann, W., Weber, K., and Fürst, D.O. (1993). The globular head domain of titin extends into the center of the sarcomeric M band. J. Cell Sci. 106, 319-330.
    • (1993) J. Cell Sci. , vol.106 , pp. 319-330
    • Vinkemeier, U.1    Obermann, W.2    Weber, K.3    Fürst, D.O.4
  • 51
    • 0020805791 scopus 로고
    • Isoenzyme specific localization of M-line-bound creatine kinase in myogenic cells
    • Wallimann, T., Moser, H., and Eppenberger, H.M. (1983). Isoenzyme specific localization of M-line-bound creatine kinase in myogenic cells. J. Muscle Res. Cell Motil. 4, 429-441.
    • (1983) J. Muscle Res. Cell Motil. , vol.4 , pp. 429-441
    • Wallimann, T.1    Moser, H.2    Eppenberger, H.M.3
  • 52
    • 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. Eur. J. Biochem. 226, 661-669.
    • (1993) Eur. J. Biochem. , vol.226 , pp. 661-669
    • Weber, F.E.1    Vaughan, K.T.2    Reinach, F.C.3    Fischman, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.