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Volumn 361, Issue 4, 2006, Pages 625-633

An Interplay between Protein Disorder and Structure Confers the Ca2+ Regulation of Striated Muscle

Author keywords

fly casting; striated muscle contraction; structural dynamics; thin filament; troponin

Indexed keywords

CALCIUM ION; TROPONIN I;

EID: 33746788578     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.06.031     Document Type: Article
Times cited : (56)

References (38)
  • 1
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon A.M., Homsher E., and Regnier M. Regulation of contraction in striated muscle. Physiol. Rev. 80 (2000) 853-924
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 2
    • 0016213363 scopus 로고
    • 2+ regulation of muscle contraction
    • 2+ regulation of muscle contraction. Biochemistry 13 (1974) 2697-2703
    • (1974) Biochemistry , vol.13 , pp. 2697-2703
    • Potter, J.D.1    Gergely, J.2
  • 3
    • 0015935352 scopus 로고
    • Purification and properties of the components from troponin
    • Greaser M.L., and Gergely J. Purification and properties of the components from troponin. J. Biol. Chem. 248 (1973) 2125-2133
    • (1973) J. Biol. Chem. , vol.248 , pp. 2125-2133
    • Greaser, M.L.1    Gergely, J.2
  • 4
    • 0016370438 scopus 로고
    • Regulatory mechanism of muscle contraction with special reference to the Catroponin-tropomyosin system
    • Ebashi S. Regulatory mechanism of muscle contraction with special reference to the Catroponin-tropomyosin system. Essays Biochem. 10 (1974) 1-36
    • (1974) Essays Biochem. , vol.10 , pp. 1-36
    • Ebashi, S.1
  • 5
    • 0023664677 scopus 로고
    • The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C
    • Heeley D.H., Golosinska K., and Smillie L.B. The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C. J. Biol. Chem. 262 (1987) 9971-9978
    • (1987) J. Biol. Chem. , vol.262 , pp. 9971-9978
    • Heeley, D.H.1    Golosinska, K.2    Smillie, L.B.3
  • 6
    • 0021875797 scopus 로고
    • The interaction of rabbit skeletal muscle troponin-T fragments with troponin-I
    • Pearlstone J.R., and Smillie L.B. The interaction of rabbit skeletal muscle troponin-T fragments with troponin-I. Can. J. Biochem. Cell Biol. 63 (1985) 212-218
    • (1985) Can. J. Biochem. Cell Biol. , vol.63 , pp. 212-218
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 8
    • 0042624696 scopus 로고    scopus 로고
    • Pulling the calcium trigger
    • Sykes B.D. Pulling the calcium trigger. Nat. Struct. Biol. 10 (2003) 588-589
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 588-589
    • Sykes, B.D.1
  • 11
    • 0035970288 scopus 로고    scopus 로고
    • Troponin organization on relaxed and activated thin filaments revealed by electron microscopy and three-dimensional reconstruction
    • Lehman W., Rosol M., Tobacman L.S., and Craig R. Troponin organization on relaxed and activated thin filaments revealed by electron microscopy and three-dimensional reconstruction. J. Mol. Biol. 307 (2001) 739-744
    • (2001) J. Mol. Biol. , vol.307 , pp. 739-744
    • Lehman, W.1    Rosol, M.2    Tobacman, L.S.3    Craig, R.4
  • 12
    • 0034703378 scopus 로고    scopus 로고
    • Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
    • Lehman W., Hatch V., Korman V., Rosol M., Thomas L., Maytum R., et al. Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments. J. Mol. Biol. 302 (2000) 593-606
    • (2000) J. Mol. Biol. , vol.302 , pp. 593-606
    • Lehman, W.1    Hatch, V.2    Korman, V.3    Rosol, M.4    Thomas, L.5    Maytum, R.6
  • 13
    • 0028179144 scopus 로고
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • 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
  • 14
    • 0029131118 scopus 로고
    • Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments
    • Lehman W., Vibert P., Uman P., and Craig R. Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J. Mol. Biol. 251 (1995) 191-196
    • (1995) J. Mol. Biol. , vol.251 , pp. 191-196
    • Lehman, W.1    Vibert, P.2    Uman, P.3    Craig, R.4
  • 16
    • 0036436914 scopus 로고    scopus 로고
    • Equilibrium unfolding and conformational plasticity of troponin I and T
    • Martins S.M., Chapeaurouge A., and Ferreira S.T. Equilibrium unfolding and conformational plasticity of troponin I and T. Eur. J. Biochem. 269 (2002) 5484-5491
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5484-5491
    • Martins, S.M.1    Chapeaurouge, A.2    Ferreira, S.T.3
  • 18
    • 0021106246 scopus 로고
    • Calcium-dependent inhibitory region of troponin: a proton nuclear magnetic resonance study on the interaction between troponin C and the synthetic peptide N alpha-acetyl[FPhe106]TnI-(104-115) amide
    • Cachia P.J., Sykes B.D., and Hodges R.S. Calcium-dependent inhibitory region of troponin: a proton nuclear magnetic resonance study on the interaction between troponin C and the synthetic peptide N alpha-acetyl[FPhe106]TnI-(104-115) amide. Biochemistry 22 (1983) 4145-4152
    • (1983) Biochemistry , vol.22 , pp. 4145-4152
    • Cachia, P.J.1    Sykes, B.D.2    Hodges, R.S.3
  • 19
    • 20444436795 scopus 로고    scopus 로고
    • Calcium-dependent changes in the flexibility of the regulatory domain of troponin C in the troponin complex
    • Blumenschein T.M.A., Stone D.B., Fletterick R.J., Mendelson R.A., and Sykes B.D. Calcium-dependent changes in the flexibility of the regulatory domain of troponin C in the troponin complex. J. Biol. Chem. 280 (2005) 21924-21932
    • (2005) J. Biol. Chem. , vol.280 , pp. 21924-21932
    • Blumenschein, T.M.A.1    Stone, D.B.2    Fletterick, R.J.3    Mendelson, R.A.4    Sykes, B.D.5
  • 21
    • 0030624544 scopus 로고    scopus 로고
    • NMR methods for the study of protein structure and dynamics
    • Kay L.E. NMR methods for the study of protein structure and dynamics. Biochem. Cell. Biol. 75 (1997) 1-15
    • (1997) Biochem. Cell. Biol. , vol.75 , pp. 1-15
    • Kay, L.E.1
  • 22
    • 18844478967 scopus 로고    scopus 로고
    • Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity
    • Gagne S.M., Tsuda S., Spyracopoulos L., Kay L.E., and Sykes B.D. Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity. J. Mol. Biol. 278 (1998) 667-686
    • (1998) J. Mol. Biol. , vol.278 , pp. 667-686
    • Gagne, S.M.1    Tsuda, S.2    Spyracopoulos, L.3    Kay, L.E.4    Sykes, B.D.5
  • 25
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson H.J., and Wright P.E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struck. Biol. 12 (2002) 54-60
    • (2002) Curr. Opin. Struck. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 26
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., and Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337 (2004) 635-645
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 27
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: the fly-casting mechanism
    • Shoemaker B.A., Portman J.J., and Wolynes P.G. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc. Natl Acad. Sci. USA 97 (2000) 8868-8873
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 28
    • 0037047089 scopus 로고    scopus 로고
    • Conformational change of the actomyosin complex drives the multiple stepping movement
    • Terada T.P., Sasai M., and Yomo T. Conformational change of the actomyosin complex drives the multiple stepping movement. Proc. Natl Acad. Sci. USA 99 (2002) 9202-9206
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9202-9206
    • Terada, T.P.1    Sasai, M.2    Yomo, T.3
  • 29
    • 13444253928 scopus 로고    scopus 로고
    • Mapping contacts between regulatory domains of skeletal muscle TnC and TnI by analyses of single-chain chimeras
    • Tiroli A.O., Tasic L., Oliveira C.L.P., Bloch C.J., Torriani I., Farah C.S., and Ramos C.H.I. Mapping contacts between regulatory domains of skeletal muscle TnC and TnI by analyses of single-chain chimeras. FEBS J. 272 (2005) 779-790
    • (2005) FEBS J. , vol.272 , pp. 779-790
    • Tiroli, A.O.1    Tasic, L.2    Oliveira, C.L.P.3    Bloch, C.J.4    Torriani, I.5    Farah, C.S.6    Ramos, C.H.I.7
  • 30
    • 0028137004 scopus 로고
    • Structural and regulatory functions of the NH2- and COOH-terminal regions of skeletal muscle troponin I
    • Farah C.S., Miyamoto C.A., Ramos C.H., da Silva A.C., Quaggio R.B., Fujimori K., et al. Structural and regulatory functions of the NH2- and COOH-terminal regions of skeletal muscle troponin I. J. Biol. Chem. 269 (1994) 5230-5240
    • (1994) J. Biol. Chem. , vol.269 , pp. 5230-5240
    • Farah, C.S.1    Miyamoto, C.A.2    Ramos, C.H.3    da Silva, A.C.4    Quaggio, R.B.5    Fujimori, K.6
  • 31
    • 12944327750 scopus 로고    scopus 로고
    • Energy landscapes and solved protein-folding problems
    • Wolynes P.G. Energy landscapes and solved protein-folding problems. Philos. Transact. A, Math. Phys. Eng. Sci. 363 (2005) 453-464
    • (2005) Philos. Transact. A, Math. Phys. Eng. Sci. , vol.363 , pp. 453-464
    • Wolynes, P.G.1
  • 33
    • 32244445605 scopus 로고    scopus 로고
    • Histidine button engineered into cardiac troponin I protects the ischemic and failing heart
    • Day S.M., Westfall M.V., Fomicheva E.V., Hoyer K., Yasuda S., Cross N.C.L., et al. Histidine button engineered into cardiac troponin I protects the ischemic and failing heart. Nat. Med. 12 (2006) 181-189
    • (2006) Nat. Med. , vol.12 , pp. 181-189
    • Day, S.M.1    Westfall, M.V.2    Fomicheva, E.V.3    Hoyer, K.4    Yasuda, S.5    Cross, N.C.L.6
  • 34
    • 17744382824 scopus 로고    scopus 로고
    • Structural based insights into the role of troponin in cardiac muscle pathophysiology
    • Li M.X., Wang X., and Sykes B.D. Structural based insights into the role of troponin in cardiac muscle pathophysiology. J. Muscle Res. Cell Motil. 25 (2004) 559-579
    • (2004) J. Muscle Res. Cell Motil. , vol.25 , pp. 559-579
    • Li, M.X.1    Wang, X.2    Sykes, B.D.3
  • 35
    • 30944444021 scopus 로고    scopus 로고
    • Sarcomeric proteins and familial hypertrophic cardiomyopathy: linking mutations in structural proteins to complex cardiovascular phenotypes
    • Tardiff J.C. Sarcomeric proteins and familial hypertrophic cardiomyopathy: linking mutations in structural proteins to complex cardiovascular phenotypes. Heart Fail. Rev. 10 (2005) 237-248
    • (2005) Heart Fail. Rev. , vol.10 , pp. 237-248
    • Tardiff, J.C.1
  • 36
    • 3042718653 scopus 로고    scopus 로고
    • Molecular and cellular aspects of troponin cardiomyopathies
    • Gomes A.V., and Potter J.D. Molecular and cellular aspects of troponin cardiomyopathies. Ann. N.Y. Acad. Sci. 1015 (2004) 214-224
    • (2004) Ann. N.Y. Acad. Sci. , vol.1015 , pp. 214-224
    • Gomes, A.V.1    Potter, J.D.2
  • 37
    • 0028891899 scopus 로고
    • NMR solution structure of calcium-saturated skeletal muscle troponin C
    • Slupsky C.M., and Sykes B.D. NMR solution structure of calcium-saturated skeletal muscle troponin C. Biochemistry 34 (1995) 15953-15964
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2


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