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Volumn 44, Issue 12, 2005, Pages 4905-4910

Structural requirements of tropomodulin for tropomyosin binding and actin filament capping

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; FLUORESCENCE; GELS; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; MONOMERS; POLYMERIZATION;

EID: 15444377428     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047468p     Document Type: Article
Times cited : (52)

References (45)
  • 1
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D., and Borisy, G. G. (2003) Cellular motility driven by assembly and disassembly of actin filaments, Cell 112, 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 2
    • 3943052117 scopus 로고    scopus 로고
    • Crawling toward a unified model of cell mobility: Spatial and temporal regulation of actin dynamics
    • Rafelski, S. M., and Theriot, J. A. (2004) Crawling toward a unified model of cell mobility: spatial and temporal regulation of actin dynamics, Annu. Rev. Biochem. 73, 209-239.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 209-239
    • Rafelski, S.M.1    Theriot, J.A.2
  • 3
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier, M. F., and Pantaloni, D. (1997) Control of actin dynamics in cell motility, J. Mol. Biol. 269, 459-467.
    • (1997) J. Mol. Biol. , vol.269 , pp. 459-467
    • Carlier, M.F.1    Pantaloni, D.2
  • 4
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: Distribution, properties and function
    • Perry, S. V. (2001) Vertebrate tropomyosin: distribution, properties and function, J. Muscle Res. Cell Motil. 22, 5-49.
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 5-49
    • Perry, S.V.1
  • 5
    • 0142157493 scopus 로고    scopus 로고
    • Tropomodulins: Life at the slow end
    • Fischer, R. S., and Fowler, V. M. (2003) Tropomodulins: life at the slow end, Trends Cell Biol. 13, 593-601.
    • (2003) Trends Cell Biol. , vol.13 , pp. 593-601
    • Fischer, R.S.1    Fowler, V.M.2
  • 6
    • 4043147895 scopus 로고    scopus 로고
    • Capping protein: New insights into mechanism and regulation
    • Wear, M. A., and Cooper, J. A. (2004) Capping protein: new insights into mechanism and regulation, Trends Biochem. Sci. 29, 418-428.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 418-428
    • Wear, M.A.1    Cooper, J.A.2
  • 7
    • 0029612323 scopus 로고
    • Control of actin assembly at filament ends
    • Schafer, D. A., and Cooper, J. A. (1995) Control of actin assembly at filament ends, Annu. Rev. Cell Dev. Biol. 11, 497-518.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 497-518
    • Schafer, D.A.1    Cooper, J.A.2
  • 8
    • 0032971134 scopus 로고    scopus 로고
    • Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms
    • Weber, A. (1999) Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms, Mol. Cell Biochem. 190, 67-74.
    • (1999) Mol. Cell Biochem. , vol.190 , pp. 67-74
    • Weber, A.1
  • 9
    • 0023272783 scopus 로고
    • Identification and purification of a novel Mr 43,000 tropomyosin- binding protein from human erythrocyte membranes
    • Fowler, V. M. (1987) Identification and purification of a novel Mr 43,000 tropomyosin- binding protein from human erythrocyte membranes, J. Biol. Chem. 262, 12792-12800.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12792-12800
    • Fowler, V.M.1
  • 10
    • 0029838840 scopus 로고    scopus 로고
    • N-tropomodulin: A novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin
    • Watakabe, A., Kobayashi, R., and Helfman, D. M. (1996) N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin, J. Cell Sci. 109, 2299-2310.
    • (1996) J. Cell Sci. , vol.109 , pp. 2299-2310
    • Watakabe, A.1    Kobayashi, R.2    Helfman, D.M.3
  • 11
    • 0032948760 scopus 로고    scopus 로고
    • Tropomodulin assembles early in myofibrillogenesis in chick skeletal muscle: Evidence that thin filaments rearrange to form striated myofibrils
    • Almenar-Queralt, A., Gregorio, C. C., and Fowler, V. M. (1999) Tropomodulin assembles early in myofibrillogenesis in chick skeletal muscle: evidence that thin filaments rearrange to form striated myofibrils, J. Cell Sci. 112, 1111-1123.
    • (1999) J. Cell Sci. , vol.112 , pp. 1111-1123
    • Almenar-Queralt, A.1    Gregorio, C.C.2    Fowler, V.M.3
  • 12
    • 0035870762 scopus 로고    scopus 로고
    • Leiomodins: Larger members of the tropomodulin (tmod) gene family
    • Conley, C. A., Fritz-Six, K. L., Almenar-Queralt, A., and Fowler, V. M. (2001) Leiomodins: larger members of the tropomodulin (tmod) gene family, Genomics 73, 127-139.
    • (2001) Genomics , vol.73 , pp. 127-139
    • Conley, C.A.1    Fritz-Six, K.L.2    Almenar-Queralt, A.3    Fowler, V.M.4
  • 13
    • 0036232091 scopus 로고    scopus 로고
    • Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin
    • Greenfield, N. J., and Fowler, V. M. (2002) Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin, Biophys. J. 82, 2580-2591.
    • (2002) Biophys. J. , vol.82 , pp. 2580-2591
    • Greenfield, N.J.1    Fowler, V.M.2
  • 14
    • 0027535632 scopus 로고
    • Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle
    • Fowler, V. M., Sussmann, M. A., Miller, P. G., Flucher, B. E., and Daniels, M. P. (1993) Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle, J. Cell Biol. 120, 411-420.
    • (1993) J. Cell Biol. , vol.120 , pp. 411-420
    • Fowler, V.M.1    Sussmann, M.A.2    Miller, P.G.3    Flucher, B.E.4    Daniels, M.P.5
  • 15
    • 0038070120 scopus 로고    scopus 로고
    • Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility
    • Fischer, R. S., Fritz-Six, K. L., and Fowler, V. M. (2003) Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility, J. Cell Biol. 161, 371-380.
    • (2003) J. Cell Biol. , vol.161 , pp. 371-380
    • Fischer, R.S.1    Fritz-Six, K.L.2    Fowler, V.M.3
  • 16
    • 0028914944 scopus 로고
    • Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: Tropomodulin requires tropomyosin for assembly
    • Gregorio, C. C., and Fowler, V. M. (1995) Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: tropomodulin requires tropomyosin for assembly, J. Cell Biol. 129, 683-695.
    • (1995) J. Cell Biol. , vol.129 , pp. 683-695
    • Gregorio, C.C.1    Fowler, V.M.2
  • 17
    • 0141545016 scopus 로고    scopus 로고
    • The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes
    • Mudry, R. E., Perry, C. N., Richards, M., Fowler, V. M., and Gregorio, C. C. (2003) The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes, J. Cell Biol. 162, 1057-1068.
    • (2003) J. Cell Biol. , vol.162 , pp. 1057-1068
    • Mudry, R.E.1    Perry, C.N.2    Richards, M.3    Fowler, V.M.4    Gregorio, C.C.5
  • 18
    • 0035371379 scopus 로고    scopus 로고
    • The shapes and sizes of two domains of tropomodulin, the P-end-capping protein of actin-tropomyosin
    • Fujisawa, T., Kostyukova, A., and Maeda, Y. (2001) The shapes and sizes of two domains of tropomodulin, the P-end-capping protein of actin-tropomyosin, FEBS Lett. 498, 67-71.
    • (2001) FEBS Lett. , vol.498 , pp. 67-71
    • Fujisawa, T.1    Kostyukova, A.2    Maeda, Y.3
  • 19
    • 0036841312 scopus 로고    scopus 로고
    • Crystal structure of tropomodulin C-terminal half and structural basis of actin filament pointed-end capping
    • Krieger, I., Kostyukova, A., Yamashita, A., Nitanai, Y., and Maeda, Y. (2002) Crystal structure of tropomodulin C-terminal half and structural basis of actin filament pointed-end capping, Biophys. J. 83, 2716-2725.
    • (2002) Biophys. J. , vol.83 , pp. 2716-2725
    • Krieger, I.1    Kostyukova, A.2    Yamashita, A.3    Nitanai, Y.4    Maeda, Y.5
  • 20
    • 0141809370 scopus 로고    scopus 로고
    • Tropomodulin contains two actin filament pointed end-capping domains
    • Fowler, V. M., Greenfield, N. J., and Moyer, J. (2003) Tropomodulin contains two actin filament pointed end-capping domains, J. Biol. Chem. 278, 40000-40009.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40000-40009
    • Fowler, V.M.1    Greenfield, N.J.2    Moyer, J.3
  • 21
    • 0033756332 scopus 로고    scopus 로고
    • Domain structure of tropomodulin: Distinct properties of the N-terminal and C-terminal halves
    • Kostyukova, A., Yamauchi, E., Maeda, K., Krieger, I., and Maeda, Y. (2000) Domain structure of tropomodulin: distinct properties of the N-terminal and C-terminal halves, Eur. J. Biochem. 267, 6470-6475.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6470-6475
    • Kostyukova, A.1    Yamauchi, E.2    Maeda, K.3    Krieger, I.4    Maeda, Y.5
  • 22
    • 0034950529 scopus 로고    scopus 로고
    • Folding properties of functional domains of tropomodulin
    • Kostyukova, A. S., Tiktopulo, E. I., and Maeda, Y. (2001) Folding properties of functional domains of tropomodulin, Biophys. J. 81, 345-351.
    • (2001) Biophys. J. , vol.81 , pp. 345-351
    • Kostyukova, A.S.1    Tiktopulo, E.I.2    Maeda, Y.3
  • 23
    • 1242294519 scopus 로고    scopus 로고
    • Effect of the structure of the N terminus of tropomyosin on tropomodulin function
    • Kostyukova, A. S., and Hitchcock-DeGregori, S. E. (2004) Effect of the structure of the N terminus of tropomyosin on tropomodulin function, J. Biol. Chem. 279, 5066-5071.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5066-5071
    • Kostyukova, A.S.1    Hitchcock-DeGregori, S.E.2
  • 24
    • 11244323829 scopus 로고    scopus 로고
    • Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1
    • Greenfield, N. J., Kostyukova, A. S., and Hitchcock-Degregori, S. E. (2005) Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1, Biophys. J. 88, 372-383.
    • (2005) Biophys. J. , vol.88 , pp. 372-383
    • Greenfield, N.J.1    Kostyukova, A.S.2    Hitchcock-Degregori, S.E.3
  • 25
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and Watt, S. (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin, J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 26
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
    • MacLean-Fletcher, S., and Pollard, T. D. (1980) Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association, Biochem. Biophys. Res. Commun. 96, 18-27.
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 18-27
    • MacLean-Fletcher, S.1    Pollard, T.D.2
  • 27
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama, T., and Mihashi, K. (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin, Eur. J. Biochem. 114, 33-38.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 28
    • 0020533805 scopus 로고
    • Pyrene actin: Documentation of the validity of a sensitive assay for actin polymerization
    • Cooper, J. A., Walker, S. B., and Pollard, T. D. (1983) Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization, J. Muscle Res. Cell Motil. 4, 253-262.
    • (1983) J. Muscle Res. Cell Motil. , vol.4 , pp. 253-262
    • Cooper, J.A.1    Walker, S.B.2    Pollard, T.D.3
  • 29
    • 0033619726 scopus 로고    scopus 로고
    • The ends of tropomyosin are major determinants of actin affinity and myosin subfragment 1-induced binding to F-actin in the open state
    • Moraczewska, J., Nicholson-Flynn, K., and Hitchcock-DeGregori, S. E. (1999) The ends of tropomyosin are major determinants of actin affinity and myosin subfragment 1-induced binding to F-actin in the open state, Biochemistry 38, 15885-15892.
    • (1999) Biochemistry , vol.38 , pp. 15885-15892
    • Moraczewska, J.1    Nicholson-Flynn, K.2    Hitchcock-DeGregori, S.E.3
  • 30
    • 0035965135 scopus 로고    scopus 로고
    • Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein
    • Greenfield, N. J., Huang, Y. J., Palm, T., Swapna, G. V., Monleon, D., Montelione, G. T., and Hitchcock-DeGregori, S. E. (2001) Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein, J. Mol. Biol. 312, 833-847.
    • (2001) J. Mol. Biol. , vol.312 , pp. 833-847
    • Greenfield, N.J.1    Huang, Y.J.2    Palm, T.3    Swapna, G.V.4    Monleon, D.5    Montelione, G.T.6    Hitchcock-DeGregori, S.E.7
  • 31
    • 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 227, 680-685.
    • (1970) Nature , Issue.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins, Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 34
    • 0029591294 scopus 로고
    • The stability of tropomyosin, a two-stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface
    • Greenfield, N. J., and Hitchcock-DeGregori, S. E. (1995) The stability of tropomyosin, a two-stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface, Biochemistry 34, 16797-16805.
    • (1995) Biochemistry , vol.34 , pp. 16797-16805
    • Greenfield, N.J.1    Hitchcock-DeGregori, S.E.2
  • 35
    • 0032568543 scopus 로고    scopus 로고
    • The structure of the N-terminus of striated muscle alpha-tropomyosin in a chimeric peptide: Nuclear magnetic resonance structure and circular dichroism studies
    • Greenfield, N. J., Montelione, G. T., Farid, R. S., and Hitchcock-DeGregori, S. E. (1998) The structure of the N-terminus of striated muscle alpha-tropomyosin in a chimeric peptide: nuclear magnetic resonance structure and circular dichroism studies, Biochemistry 37, 7834-7843.
    • (1998) Biochemistry , vol.37 , pp. 7834-7843
    • Greenfield, N.J.1    Montelione, G.T.2    Farid, R.S.3    Hitchcock-DeGregori, S.E.4
  • 36
    • 3242713435 scopus 로고    scopus 로고
    • Circular dichroism analysis for protein-protein interactions
    • Greenfield, N. J. (2004) Circular dichroism analysis for protein-protein interactions, Methods Mol. Biol. 261, 55-78.
    • (2004) Methods Mol. Biol. , vol.261 , pp. 55-78
    • Greenfield, N.J.1
  • 37
    • 0027995873 scopus 로고
    • α-helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix
    • Zhou, N. E., Monera, O. D., Kay, C. M., and Hodges, R. S. (1994) α-helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix, Protein Pept. Lett. 1, 114-119.
    • (1994) Protein Pept. Lett. , vol.1 , pp. 114-119
    • Zhou, N.E.1    Monera, O.D.2    Kay, C.M.3    Hodges, R.S.4
  • 38
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K. T., and DeGrado, W. F. (1990) A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids, Science 250, 646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 39
    • 6444234180 scopus 로고    scopus 로고
    • The helical alanine controversy: An (Ala)6 insertion dramatically increases helicity
    • Lin, J. C., Barua, B., and Andersen, N. H. (2004) The helical alanine controversy: an (Ala)6 insertion dramatically increases helicity, J. Am. Chem. Soc. 126, 13679-13684.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 13679-13684
    • Lin, J.C.1    Barua, B.2    Andersen, N.H.3
  • 40
    • 0041989754 scopus 로고    scopus 로고
    • A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex
    • Panchal, S. C., Kaiser, D. A., Torres, E., Pollard, T. D., and Rosen, M. K. (2003) A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex, Nat. Struct. Biol. 10, 591-598.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 591-598
    • Panchal, S.C.1    Kaiser, D.A.2    Torres, E.3    Pollard, T.D.4    Rosen, M.K.5
  • 42
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou, P. Y., and Fasman, G. D. (1978) Empirical predictions of protein conformation, Annu. Rev. Biochem. 47, 251-276.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 44
    • 0035808418 scopus 로고    scopus 로고
    • The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments
    • McElhinny, A. S., Kolmerer, B., Fowler, V. M., Labeit, S., and Gregorio, C. C. (2001) The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments, J. Biol. Chem. 276, 583-592.
    • (2001) J. Biol. Chem. , vol.276 , pp. 583-592
    • McElhinny, A.S.1    Kolmerer, B.2    Fowler, V.M.3    Labeit, S.4    Gregorio, C.C.5
  • 45
    • 1642450634 scopus 로고    scopus 로고
    • The interaction between E-tropomodulin and thymosin beta-10 rescues tumor cells from thymosin beta-10 mediated apoptosis by restoring actin architecture
    • Rho, S. B., Chun, T., Lee, S. H., Park, K., and Lee, J. H. (2004) The interaction between E-tropomodulin and thymosin beta-10 rescues tumor cells from thymosin beta-10 mediated apoptosis by restoring actin architecture, FEBS Lett. 557, 57-63.
    • (2004) FEBS Lett. , vol.557 , pp. 57-63
    • Rho, S.B.1    Chun, T.2    Lee, S.H.3    Park, K.4    Lee, J.H.5


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