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Volumn 1794, Issue 2, 2009, Pages 237-243

Effect of actin C-terminal modification on tropomyosin isoforms binding and thin filament regulation

Author keywords

Actin; Non muscle; Regulation; Smooth muscle; Tropomyosin; Truncated actin

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; ISOPROTEIN; MYOSIN; PROTEIN SUBUNIT; REGULATOR PROTEIN; TROPOMYOSIN;

EID: 58149186451     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.10.014     Document Type: Article
Times cited : (19)

References (44)
  • 2
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller J.P., and Helfman D.M. The molecular basis for tropomyosin isoform diversity. Bioessays 13 (1991) 429-437
    • (1991) Bioessays , vol.13 , pp. 429-437
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 3
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: distribution, properties and function
    • Perry S.V. Vertebrate tropomyosin: distribution, properties and function. J. Muscle Res. Cell Motil. 22 (2001) 5-49
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 5-49
    • Perry, S.V.1
  • 4
    • 20444398071 scopus 로고    scopus 로고
    • Tropomyosin isoforms: divining rods for actin cytoskeleton function
    • Gunning P.W., Schevzov G., Kee A.J., and Hardeman E.C. Tropomyosin isoforms: divining rods for actin cytoskeleton function. Trends Cell Biol. 15 (2005) 333-341
    • (2005) Trends Cell Biol. , vol.15 , pp. 333-341
    • Gunning, P.W.1    Schevzov, G.2    Kee, A.J.3    Hardeman, E.C.4
  • 5
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosin-based regulation of the actin cytoskeleton in time and space
    • Gunning P.W., O'Neill G., and Hardeman E. Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol. Rev. 88 (2008) 1-35
    • (2008) Physiol. Rev. , vol.88 , pp. 1-35
    • Gunning, P.W.1    O'Neill, G.2    Hardeman, E.3
  • 6
    • 33645774707 scopus 로고    scopus 로고
    • Differential interaction of cardiac, skeletal muscle, and yeast tropomyosins with fluorescent (pyrene235) yeast actin
    • Chen W., Wen K.K., Sens A.E., and Rubenstein P.A. Differential interaction of cardiac, skeletal muscle, and yeast tropomyosins with fluorescent (pyrene235) yeast actin. Biophys. J. 90 (2006) 1308-1318
    • (2006) Biophys. J. , vol.90 , pp. 1308-1318
    • Chen, W.1    Wen, K.K.2    Sens, A.E.3    Rubenstein, P.A.4
  • 7
    • 0033581012 scopus 로고    scopus 로고
    • Role of residues 311/312 in actin-tropomyosin interaction. In vitro motility study using yeast actin mutant e311a/r312a
    • Gerson J.H., Bobkova E., Homsher E., and Reisler E. Role of residues 311/312 in actin-tropomyosin interaction. In vitro motility study using yeast actin mutant e311a/r312a. J. Biol. Chem. 274 (1999) 17545-17550
    • (1999) J. Biol. Chem. , vol.274 , pp. 17545-17550
    • Gerson, J.H.1    Bobkova, E.2    Homsher, E.3    Reisler, E.4
  • 8
    • 0033529663 scopus 로고    scopus 로고
    • Mutations in actin subdomain 3 that impair thin filament regulation by troponin and tropomyosin
    • Korman V.L., and Tobacman L.S. Mutations in actin subdomain 3 that impair thin filament regulation by troponin and tropomyosin. J. Biol. Chem. 274 (1999) 22191-22196
    • (1999) J. Biol. Chem. , vol.274 , pp. 22191-22196
    • Korman, V.L.1    Tobacman, L.S.2
  • 9
    • 0034726706 scopus 로고    scopus 로고
    • Role of residues 230 and 236 of actin in myosin-ATPase activation by actin-tropomyosin
    • Saeki K., Yasunaga T., Matsuura Y., and Wakabayashi T. Role of residues 230 and 236 of actin in myosin-ATPase activation by actin-tropomyosin. Biochem. Biophys. Res. Commun. 275 (2000) 428-433
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 428-433
    • Saeki, K.1    Yasunaga, T.2    Matsuura, Y.3    Wakabayashi, T.4
  • 10
  • 11
    • 0019163447 scopus 로고
    • Effect of the state of oxidation of cysteine 190 of tropomyosin on the assembly of the actin-tropomyosin complex
    • Walsh T.P., and Wegner A. Effect of the state of oxidation of cysteine 190 of tropomyosin on the assembly of the actin-tropomyosin complex. Biochim. Biophys. Acta 626 (1980) 79-87
    • (1980) Biochim. Biophys. Acta , vol.626 , pp. 79-87
    • Walsh, T.P.1    Wegner, A.2
  • 12
    • 0019318268 scopus 로고
    • The interaction of alpha, alpha- and alpha, beta-tropomyosin with actin filaments
    • Wegner A. The interaction of alpha, alpha- and alpha, beta-tropomyosin with actin filaments,. FEBS Lett. 119 (1980) 245-248
    • (1980) FEBS Lett. , vol.119 , pp. 245-248
    • Wegner, A.1
  • 13
    • 0025105127 scopus 로고
    • The amino terminus of muscle tropomyosin is a major determinant for function
    • Cho Y.J., Liu J., and Hitchcock-DeGregori S. The amino terminus of muscle tropomyosin is a major determinant for function. J. Biol. Chem. 265 (1990) 538-545
    • (1990) J. Biol. Chem. , vol.265 , pp. 538-545
    • Cho, Y.J.1    Liu, J.2    Hitchcock-DeGregori, S.3
  • 14
    • 0027082784 scopus 로고
    • Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly
    • Willadsen K.A., Butters C.A., Hill L.E., and Tobacman L.S. Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly. J. Biol. Chem. 267 (1992) 23746-23752
    • (1992) J. Biol. Chem. , vol.267 , pp. 23746-23752
    • Willadsen, K.A.1    Butters, C.A.2    Hill, L.E.3    Tobacman, L.S.4
  • 15
    • 38949114989 scopus 로고    scopus 로고
    • Role of actin C-terminus in regulation of striated muscle thin filaments
    • Śliwińska M., Skórzewski R., and Moraczewska M. Role of actin C-terminus in regulation of striated muscle thin filaments. Biophys. J. 94 (2008) 1341-1347
    • (2008) Biophys. J. , vol.94 , pp. 1341-1347
    • Śliwińska, M.1    Skórzewski, R.2    Moraczewska, M.3
  • 16
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • McKillop D.F., and Geeves M.A. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65 (1993) 693-701
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 17
    • 0028179144 scopus 로고
    • Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • Lehman W., Craig R., and Vibert P. Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 368 (1994) 65-67
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 18
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • Vibert P., Craig R., and Lehman W. Steric-model for activation of muscle thin filaments. J. Mol. Biol. 266 (1997) 8-14
    • (1997) J. Mol. Biol. , vol.266 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 19
    • 0021136773 scopus 로고
    • Comparison of effects of smooth and skeletal muscle tropomyosins on interactions of actin and myosin subfragment 1
    • Williams D.L., Greene L.E., and Eisenberg E. Comparison of effects of smooth and skeletal muscle tropomyosins on interactions of actin and myosin subfragment 1. Biochemistry 23 (1984) 4150-4155
    • (1984) Biochemistry , vol.23 , pp. 4150-4155
    • Williams, D.L.1    Greene, L.E.2    Eisenberg, E.3
  • 20
    • 0021365083 scopus 로고
    • Comparison of the effects of smooth and skeletal tropomyosin on skeletal actomyosin subfragment 1 ATPase
    • Lehrer S.S., and Morris E.P. Comparison of the effects of smooth and skeletal tropomyosin on skeletal actomyosin subfragment 1 ATPase. J. Biol. Chem. 259 (1984) 2070-2072
    • (1984) J. Biol. Chem. , vol.259 , pp. 2070-2072
    • Lehrer, S.S.1    Morris, E.P.2
  • 21
    • 0019940941 scopus 로고
    • Steady-state kinetic studies on the actin-activation of skeletal muscle meromyosin subfragments. Effects of skeletal, smooth and non-muscle tropomyosins
    • Sobieszek A. Steady-state kinetic studies on the actin-activation of skeletal muscle meromyosin subfragments. Effects of skeletal, smooth and non-muscle tropomyosins. J. Mol. Biol. 157 (1982) 275-286
    • (1982) J. Mol. Biol. , vol.157 , pp. 275-286
    • Sobieszek, A.1
  • 22
    • 0030927201 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon
    • Hodgkinson J.L., Marston S.B., Craig R., Vibert P., and Lehman W. Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon. Biophys. J. 72 (1997) 2398-2404
    • (1997) Biophys. J. , vol.72 , pp. 2398-2404
    • Hodgkinson, J.L.1    Marston, S.B.2    Craig, R.3    Vibert, P.4    Lehman, W.5
  • 24
    • 0026558989 scopus 로고
    • Removing the two C-terminal residues of actin affects the filament structure
    • O'Donoghue S.I., Miki M., and dos Remedios C.G. Removing the two C-terminal residues of actin affects the filament structure. Arch. Biochem. Biophys. 293 (1992) 110-116
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 110-116
    • O'Donoghue, S.I.1    Miki, M.2    dos Remedios, C.G.3
  • 25
    • 0027452835 scopus 로고
    • Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions
    • Mossakowska M., Moraczewska J., Khaitlina S.Y., and Strzelecka-Gołaszewska H. Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions. Biochem. J. 289 (1993) 897-902
    • (1993) Biochem. J. , vol.289 , pp. 897-902
    • Mossakowska, M.1    Moraczewska, J.2    Khaitlina, S.Y.3    Strzelecka-Gołaszewska, H.4
  • 26
    • 0029847601 scopus 로고    scopus 로고
    • 2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin
    • 2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin. Biochem. J. 316 (1996) 713-721
    • (1996) Biochem. J. , vol.316 , pp. 713-721
    • Strzelecka-Gołaszewska, H.1    Woźniak, A.2    Hult, T.3    Lindberg, U.4
  • 27
    • 58149184468 scopus 로고    scopus 로고
    • Involvement of actin C-terminus in regulation of actomyosin ATPase by tropomyosin isoforms, Biophysical Society Meeting Abstracts
    • Suppl.
    • Moraczewska J., Skórzewski R., Śliwińska M., and Borys D. Involvement of actin C-terminus in regulation of actomyosin ATPase by tropomyosin isoforms, Biophysical Society Meeting Abstracts. Biophys. J. (2006) Suppl.
    • (2006) Biophys. J.
    • Moraczewska, J.1    Skórzewski, R.2    Śliwińska, M.3    Borys, D.4
  • 28
    • 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. 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 (1971) 4866-4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 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. 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 (1999) 15885-15892
    • (1999) Biochemistry , vol.38 , pp. 15885-15892
    • Moraczewska, J.1    Nicholson-Flynn, K.2    Hitchcock-DeGregori, S.E.3
  • 30
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian S.S., and Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85 (1982) 55-71
    • (1982) Methods Enzymol. , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 31
  • 32
    • 0020013525 scopus 로고
    • Special instrumentation and techniques for kinetic studies of contractile systems
    • White H.D. Special instrumentation and techniques for kinetic studies of contractile systems. Methods Enzymol. 85 (1982) 698-708
    • (1982) Methods Enzymol. , vol.85 , pp. 698-708
    • White, H.D.1
  • 33
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • McGhee J.D., and von Hippel P.H. Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. J. Mol. Biol. 86 (1974) 469-489
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    von Hippel, P.H.2
  • 34
    • 0026672241 scopus 로고
    • Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules
    • Hill L.E., Mehegan J.P., Butters C.A., and Tobacman L.S. Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules. J. Biol. Chem. 267 (1992) 16106-16113
    • (1992) J. Biol. Chem. , vol.267 , pp. 16106-16113
    • Hill, L.E.1    Mehegan, J.P.2    Butters, C.A.3    Tobacman, L.S.4
  • 35
    • 0017072908 scopus 로고
    • Tropomyosin binding to F-actin induced by myosin heads
    • Eaton B.L. Tropomyosin binding to F-actin induced by myosin heads. Science 192 (1976) 1337-1339
    • (1976) Science , vol.192 , pp. 1337-1339
    • Eaton, B.L.1
  • 36
    • 17544365077 scopus 로고    scopus 로고
    • Opposite effects of myosin subfragment 1 on binding of cardiac troponin and tropomyosin to the thin filament
    • Cassell M., and Tobacman L.S. Opposite effects of myosin subfragment 1 on binding of cardiac troponin and tropomyosin to the thin filament. J. Biol. Chem. 271 (1996) 12867-12872
    • (1996) J. Biol. Chem. , vol.271 , pp. 12867-12872
    • Cassell, M.1    Tobacman, L.S.2
  • 37
    • 0030838333 scopus 로고    scopus 로고
    • Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity. The role of tropomyosin flexibility and end-to-end interactions
    • Lehrer S.S., Golitsina N.L., and Geeves M.A. Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity. The role of tropomyosin flexibility and end-to-end interactions. Biochemistry 36 (1997) 13449-13454
    • (1997) Biochemistry , vol.36 , pp. 13449-13454
    • Lehrer, S.S.1    Golitsina, N.L.2    Geeves, M.A.3
  • 42
    • 0027240526 scopus 로고
    • Cooperative interactions between adjacent troponin-tropomyosin complexes may be transmitted through the actin filament
    • Butters C.A., Willadsen K.A., and Tobacman L.S. Cooperative interactions between adjacent troponin-tropomyosin complexes may be transmitted through the actin filament. J. Biol. Chem. 268 (1993) 15565-15570
    • (1993) J. Biol. Chem. , vol.268 , pp. 15565-15570
    • Butters, C.A.1    Willadsen, K.A.2    Tobacman, L.S.3
  • 43
    • 37349077586 scopus 로고    scopus 로고
    • Tropomyosin's periods are quasi-equivalent for actin binding but have specific regulatory functions
    • Singh A., and Hitchcock-DeGregori S.E. Tropomyosin's periods are quasi-equivalent for actin binding but have specific regulatory functions. Biochemistry 46 (2007) 14917-14927
    • (2007) Biochemistry , vol.46 , pp. 14917-14927
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 44
    • 43749096824 scopus 로고    scopus 로고
    • Conserved ASP 137 imparts flexibility to tropomyosin and affects function
    • Sumida J.P., Wu E., and Lehrer S.S. Conserved ASP 137 imparts flexibility to tropomyosin and affects function. J. Biol. Chem. 283 (2008) 6728-6734
    • (2008) J. Biol. Chem. , vol.283 , pp. 6728-6734
    • Sumida, J.P.1    Wu, E.2    Lehrer, S.S.3


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