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Volumn 592, Issue , 2007, Pages 253-264

Regulation by myosin: How calcium regulates some myosins, past and present

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; CALCIUM; GLYCINE; NUCLEOTIDE DERIVATIVE; TROPOMYOSIN;

EID: 84934438140     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-4-431-38453-3_21     Document Type: Conference Paper
Times cited : (20)

References (57)
  • 1
    • 0008819950 scopus 로고
    • Studies on muscle
    • A. Szent-Györgyi, Studies on muscle, Acta Physiol. Scand. 9(Suppl. 25), 25 (1945).
    • (1945) Acta Physiol. Scand , vol.9 , Issue.SUPPL. 25 , pp. 25
    • Szent-Györgyi, A.1
  • 2
    • 0001353052 scopus 로고
    • The double array of filaments in cross-striated muscle
    • H. E. Huxley, The double array of filaments in cross-striated muscle, J. Biophys. Biochem. Cytol. 3, 631-648 (1957).
    • (1957) J. Biophys. Biochem. Cytol , vol.3 , pp. 631-648
    • Huxley, H.E.1
  • 3
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction. Interference microscopy of living muscle fibers
    • A. F. Huxley and A. F. Niedergerke, Structural changes in muscle during contraction. Interference microscopy of living muscle fibers, Nature 173, 971-978 (1954).
    • (1954) Nature , vol.173 , pp. 971-978
    • Huxley, A.F.1    Niedergerke, A.F.2
  • 4
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
    • H. E. Huxley and J. Hanson, Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation, Nature 173, 979-978 (1954).
    • (1954) Nature , vol.173 , pp. 979-978
    • Huxley, H.E.1    Hanson, J.2
  • 5
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • A. F. Huxley, Muscle structure and theories of contraction, Progr. Biophys. Biophys. Chem. 7, 255-318 (1957).
    • (1957) Progr. Biophys. Biophys. Chem , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 6
    • 0013850715 scopus 로고
    • Induced changes in orientation of the cross bridges of glycerinated insect flight muscle
    • M. K. Reedy, K. C. Holmes, and R. T. Tregear, Induced changes in orientation of the cross bridges of glycerinated insect flight muscle, Nature 207, 1276-1280 (1965).
    • (1965) Nature , vol.207 , pp. 1276-1280
    • Reedy, M.K.1    Holmes, K.C.2    Tregear, R.T.3
  • 7
    • 0001164833 scopus 로고
    • Essential relaxing factor in muscle other than myokinase and creatine-phosphokinase
    • S. Kumagai, S. Ebashi, and F. Takeda, Essential relaxing factor in muscle other than myokinase and creatine-phosphokinase, Nature 176, 166 (1955).
    • (1955) Nature , vol.176 , pp. 166
    • Kumagai, S.1    Ebashi, S.2    Takeda, F.3
  • 8
    • 0004819601 scopus 로고
    • Study of the kinetics of calcium transport by isolated fragmented sarcoplasmic reticulum
    • A. Weber, R. Herz, and I. Reiss, Study of the kinetics of calcium transport by isolated fragmented sarcoplasmic reticulum, Biochem. Z. 345, 329-369 (1966).
    • (1966) Biochem. Z , vol.345 , pp. 329-369
    • Weber, A.1    Herz, R.2    Reiss, I.3
  • 9
    • 0004367246 scopus 로고
    • Die calciumpumpe der " erschlaffungsgrana" des muskels und ihre abhangigkeit von der ATP-spaltung
    • W. Hasselbach and N. Makinose, Die calciumpumpe der " erschlaffungsgrana" des muskels und ihre abhangigkeit von der ATP-spaltung, Biochem. Z. 333, 94-111 (1961).
    • (1961) Biochem. Z , vol.333 , pp. 94-111
    • Hasselbach, W.1    Makinose, N.2
  • 10
    • 84968965880 scopus 로고
    • Adenosine triphosphate-linked concentration of calcium ions in a particular fraction of rabbit muscle
    • S. Ebashi and F. Lippman, Adenosine triphosphate-linked concentration of calcium ions in a particular fraction of rabbit muscle, J. Cell. Biol. 14, 389-400 (1962).
    • (1962) J. Cell. Biol , vol.14 , pp. 389-400
    • Ebashi, S.1    Lippman, F.2
  • 11
    • 0001714579 scopus 로고
    • Third component participating in the superprecipitation of "natural actomyosin
    • S. Ebashi, Third component participating in the superprecipitation of "natural actomyosin", Nature 200, 1010 (1963).
    • (1963) Nature , vol.200 , pp. 1010
    • Ebashi, S.1
  • 12
    • 0000519978 scopus 로고
    • A new protein component participating in the superprecipitation of myosin B
    • S. Ebashi and F. Ebashi, A new protein component participating in the superprecipitation of myosin B, J. Biochem. 55, 604-613 (1964).
    • (1964) J. Biochem , vol.55 , pp. 604-613
    • Ebashi, S.1    Ebashi, F.2
  • 13
    • 0014396206 scopus 로고
    • Calcium ion and muscle contraction
    • S. Ebashi and M. Endo, Calcium ion and muscle contraction, Progr. Biophys. Mol. Biol. 18, 123-183 (1968).
    • (1968) Progr. Biophys. Mol. Biol , vol.18 , pp. 123-183
    • Ebashi, S.1    Endo, M.2
  • 14
    • 0015222719 scopus 로고
    • Paramyosin and the filaments of molluscan "catch" muscles II. Native filaments: Isolation and characterization
    • A. G. Szent-Györgyi, C. Cohen, and J. Kendrick-Jones. Paramyosin and the filaments of molluscan "catch" muscles II. Native filaments: isolation and characterization, J. Mol. Biol. 56, 239-258 (1971).
    • (1971) J. Mol. Biol , vol.56 , pp. 239-258
    • Szent-Györgyi, A.G.1    Cohen, C.2    Kendrick-Jones, J.3
  • 16
    • 0016680461 scopus 로고
    • Regulation of muscular contraction: Distribution of actin control and myosin control in the animal kingdom
    • W. Lehman and A. G. Szent-Györgyi, Regulation of muscular contraction: Distribution of actin control and myosin control in the animal kingdom, J. Gen. Physiol. 66, 1-30 (1975).
    • (1975) J. Gen. Physiol , vol.66 , pp. 1-30
    • Lehman, W.1    Szent-Györgyi, A.G.2
  • 17
    • 0017883851 scopus 로고
    • Troponin-like proteins from muscles of the scallop, Aequipecten irradians
    • A. Goldberg and W. Lehman, Troponin-like proteins from muscles of the scallop, Aequipecten irradians. Biochem. J. 171, 413-418 (1978).
    • (1978) Biochem. J , vol.171 , pp. 413-418
    • Goldberg, A.1    Lehman, W.2
  • 18
    • 0022870153 scopus 로고
    • Troponin from Akazara scallop striated adductor muscles
    • T. Ojima and K. Mishita, Troponin from Akazara scallop striated adductor muscles, J. Biol. Chem. 261, 16749-16754 (1986).
    • (1986) J. Biol. Chem , vol.261 , pp. 16749-16754
    • Ojima, T.1    Mishita, K.2
  • 19
    • 0019057604 scopus 로고
    • Calcium regulation in clam foot muscle. Calcium sensitivity of clam foot myosin
    • G. Ashiba, T. Asada, and S. Watanabe, Calcium regulation in clam foot muscle. Calcium sensitivity of clam foot myosin, J. Biochem. 58, 837-846 (1980).
    • (1980) J. Biochem , vol.58 , pp. 837-846
    • Ashiba, G.1    Asada, T.2    Watanabe, S.3
  • 20
    • 0022429887 scopus 로고
    • Calcium regulation of molluscan myosin ATPase in the absence of actin
    • C. Wells and C. R. Bagshaw, Calcium regulation of molluscan myosin ATPase in the absence of actin, Nature 313, 696-697 (1985).
    • (1985) Nature , vol.313 , pp. 696-697
    • Wells, C.1    Bagshaw, C.R.2
  • 21
    • 0017869701 scopus 로고
    • Reversible loss of calcium control of tension in scallop striated muscle associated with the removal of regulatory light chains
    • R. N. Simmons and A. G. Szent-Györgyi, Reversible loss of calcium control of tension in scallop striated muscle associated with the removal of regulatory light chains, Nature 273, 62-64 (1978).
    • (1978) Nature , vol.273 , pp. 62-64
    • Simmons, R.N.1    Szent-Györgyi, A.G.2
  • 22
    • 0021414819 scopus 로고
    • Tryptic digestion of scallop S1: Evidence for a complex between the two light chains and a heavy-chain peptide
    • E. M. Szentkiralyi, Tryptic digestion of scallop S1: evidence for a complex between the two light chains and a heavy-chain peptide, J. Muscle Res. Cell. Motil. 5, 147-164 (1987).
    • (1987) J. Muscle Res. Cell. Motil , vol.5 , pp. 147-164
    • Szentkiralyi, E.M.1
  • 24
    • 0018800868 scopus 로고
    • Characterization of homologous divalent metal ion binding sites of vertebrate myosins using paramagnetic resonance spectroscopy
    • C. R. Bagshaw and J. Kendrick-Jones, Characterization of homologous divalent metal ion binding sites of vertebrate myosins using paramagnetic resonance spectroscopy, J. Mol Biol. 130, 317-336 (1979).
    • (1979) J. Mol Biol , vol.130 , pp. 317-336
    • Bagshaw, C.R.1    Kendrick-Jones, J.2
  • 25
    • 0019325152 scopus 로고
    • Regulatory light chains and scallop myosin: Full dissociation and cooperative effects
    • P. D. Chantler and A. G. Szent-Györgyi, Regulatory light chains and scallop myosin: full dissociation and cooperative effects, J. Mol. Biol. 138, 473-499 (1980).
    • (1980) J. Mol. Biol , vol.138 , pp. 473-499
    • Chantler, P.D.1    Szent-Györgyi, A.G.2
  • 26
    • 0025954262 scopus 로고
    • Complete primary structure of a scallop striated muscle myosin heavy chain
    • L. Nyitray, E. B. Goodwin, and A. G. Szent-Györgyi, Complete primary structure of a scallop striated muscle myosin heavy chain, J. Biol. Chem. 266, 18469-18476 (1991).
    • (1991) J. Biol. Chem , vol.266 , pp. 18469-18476
    • Nyitray, L.1    Goodwin, E.B.2    Szent-Györgyi, A.G.3
  • 27
    • 0026064038 scopus 로고
    • Myosin light chains and troponin C: Structural and evolutionary relationships revealed by amino acid sequence comparisons
    • J. H. Collins, Myosin light chains and troponin C: structural and evolutionary relationships revealed by amino acid sequence comparisons, J. Muscle Res. Cell Motil. 12, 3-25 (1991).
    • (1991) J. Muscle Res. Cell Motil , vol.12 , pp. 3-25
    • Collins, J.H.1
  • 28
    • 0019326536 scopus 로고
    • Hybrid formation between scallop myofibrils and foreign regulatory light-chains
    • J. R. Sellers, P. D. Chantler, and A. G. Szent-Györgyi, Hybrid formation between scallop myofibrils and foreign regulatory light-chains, J. Mol. Biol. 144, 223-245 (1980).
    • (1980) J. Mol. Biol , vol.144 , pp. 223-245
    • Sellers, J.R.1    Chantler, P.D.2    Szent-Györgyi, A.G.3
  • 29
    • 0019471806 scopus 로고
    • The role of myosin light chains in regulating actin-myosin interaction
    • J. M. Scholey, K. A. Taylor, and J. Kendrick-Jones, The role of myosin light chains in regulating actin-myosin interaction, Biochimie 63, 255-271 (1981).
    • (1981) Biochimie , vol.63 , pp. 255-271
    • Scholey, J.M.1    Taylor, K.A.2    Kendrick-Jones, J.3
  • 32
    • 0029147558 scopus 로고
    • Role of essential light chain EF hand domain in calcium binding and regulation of scallop myosin
    • S. Fromherz and A. G. Szent-Györgyi, Role of essential light chain EF hand domain in calcium binding and regulation of scallop myosin, Proc. Natl. Acad. Sci. USA 92, 7652-7656 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7652-7656
    • Fromherz, S.1    Szent-Györgyi, A.G.2
  • 34
    • 0029643912 scopus 로고    scopus 로고
    • Structure of the regulatory domain of scallop myosin at 2 Å resolution; implications for regulation
    • A. Houdusse and C. Cohen, Structure of the regulatory domain of scallop myosin at 2 Å resolution; implications for regulation, Structure (London) 4, 21-32 (1996).
    • (1996) Structure (London) , vol.4 , pp. 21-32
    • Houdusse, A.1    Cohen, C.2
  • 35
    • 0028576992 scopus 로고
    • Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue
    • A. Jancso and A. G. Szent-Györgyi, Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue, Proc. Natl. Acad. Sci. USA 91, 8762-8766 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8762-8766
    • Jancso, A.1    Szent-Györgyi, A.G.2
  • 37
    • 0023914852 scopus 로고
    • Transient-kinetic studies of the adenosine triphosphate activity of scallop heavy meronyosin
    • A. P. Jackson and C. R. Bagshaw, Transient-kinetic studies of the adenosine triphosphate activity of scallop heavy meronyosin, Biochem. J. 251, 515-526 (1988).
    • (1988) Biochem. J , vol.251 , pp. 515-526
    • Jackson, A.P.1    Bagshaw, C.R.2
  • 38
    • 0023908534 scopus 로고
    • Kinetic trapping of intermediates of the scallop heavy meromyosin adenosine triphosphatase reaction revealed by formycin nucleotides
    • A. P. Jackson. and C. R. Bagshaw, Kinetic trapping of intermediates of the scallop heavy meromyosin adenosine triphosphatase reaction revealed by formycin nucleotides, Biochem. J. 251, 527-540 (1988).
    • (1988) Biochem. J , vol.251 , pp. 527-540
    • Jackson, A.P.1    Bagshaw, C.R.2
  • 39
    • 0028574171 scopus 로고
    • Scallop striated and smooth muscle myosin heavy chain isoforms are produced by alternative RNA splicing from a single gene
    • L. Nyitray, A. Jancso, Y. Ochiai, L. Graf, and A. G. Szent-Györgyi, Scallop striated and smooth muscle myosin heavy chain isoforms are produced by alternative RNA splicing from a single gene, Proc. Natl. Acad. Sci. USA 91, 12686-12690 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12686-12690
    • Nyitray, L.1    Jancso, A.2    Ochiai, Y.3    Graf, L.4    Szent-Györgyi, A.G.5
  • 40
    • 0029909606 scopus 로고    scopus 로고
    • Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins
    • C. L. Perreault-Micale, V. N. Kalabokis, L. Nyitray, and A. G. Szent-Györgyi, Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins, J. Muscle. Res. Cell Motil. 14, 543-553 (1996).
    • (1996) J. Muscle. Res. Cell Motil , vol.14 , pp. 543-553
    • Perreault-Micale, C.L.1    Kalabokis, V.N.2    Nyitray, L.3    Szent-Györgyi, A.G.4
  • 41
    • 0032546576 scopus 로고    scopus 로고
    • Loop I can modulate ADP affinity, ATPase activity, and motility of different scallop myosins. Transient kinetic analysis of S1 isoforms
    • S. E. Kurzawa-Goertz, C. L. Perreault-Micale, K. M. Trybus, A. G. Szent-Györgyi, and M. A. Geeves, Loop I can modulate ADP affinity, ATPase activity, and motility of different scallop myosins. Transient kinetic analysis of S1 isoforms, Biochemistry 37, 7517-7525 (1998).
    • (1998) Biochemistry , vol.37 , pp. 7517-7525
    • Kurzawa-Goertz, S.E.1    Perreault-Micale, C.L.2    Trybus, K.M.3    Szent-Györgyi, A.G.4    Geeves, M.A.5
  • 43
    • 0345195989 scopus 로고    scopus 로고
    • Cooperativity and regulation of scallop myosin and myosin fragments
    • V. N. Kalabokis and A. G. Szent-Györgyi, Cooperativity and regulation of scallop myosin and myosin fragments, Biochemistry 36, 15834-15840 (1997).
    • (1997) Biochemistry , vol.36 , pp. 15834-15840
    • Kalabokis, V.N.1    Szent-Györgyi, A.G.2
  • 45
    • 0036645692 scopus 로고    scopus 로고
    • A kinetic model of the co-operative binding of calcium and ADP to scallop (Argo-pecten irradians) heavy meromyosin
    • M. Nyitrai, A. G. Szent-Györgyi, and M. A. Geeves, A kinetic model of the co-operative binding of calcium and ADP to scallop (Argo-pecten irradians) heavy meromyosin, Biochem. J. 365, 19-30 (2002).
    • (2002) Biochem. J , vol.365 , pp. 19-30
    • Nyitrai, M.1    Szent-Györgyi, A.G.2    Geeves, M.A.3
  • 46
    • 0037444793 scopus 로고    scopus 로고
    • Interactions of the two heads of scallop (Argo-pecten irradians) heavy meromyosin with actin: Influence of calcium and nucleotides
    • M. Nyitrai, A. G. Szent-Györgyi, and M. A. Geeves, Interactions of the two heads of scallop (Argo-pecten irradians) heavy meromyosin with actin: influence of calcium and nucleotides, Biochem. J. 370, 839-848 (2003).
    • (2003) Biochem. J , vol.370 , pp. 839-848
    • Nyitrai, M.1    Szent-Györgyi, A.G.2    Geeves, M.A.3
  • 47
    • 0041343065 scopus 로고    scopus 로고
    • Ionic interactions play a role in the regulatory mechanism of scallop heavy meromyosin
    • M. Nyitray, W. F. Stafford, A. G. Szent-Györgyi, and M. A. Geeves, Ionic interactions play a role in the regulatory mechanism of scallop heavy meromyosin, Biophys. J. 85, 1053-1562 (2003).
    • (2003) Biophys. J , vol.85 , pp. 1053-1562
    • Nyitray, M.1    Stafford, W.F.2    Szent-Györgyi, A.G.3    Geeves, M.A.4
  • 48
    • 0022370052 scopus 로고
    • A conformational transition in gizzard heavy meromyosin involving the head tail junction, resulting in changes in sedimentation coefficient, ATPase activity, and orientation of heads
    • H. Suzuki, W. F. Stafford, H. S. Slayter, and J. C. Seidel, A conformational transition in gizzard heavy meromyosin involving the head tail junction, resulting in changes in sedimentation coefficient, ATPase activity, and orientation of heads, J. Biol. Chem. 260, 4810-14817 (1985).
    • (1985) J. Biol. Chem , vol.260 , pp. 4810-14817
    • Suzuki, H.1    Stafford, W.F.2    Slayter, H.S.3    Seidel, J.C.4
  • 49
    • 0033611141 scopus 로고    scopus 로고
    • Visualization of head-interactions in the inhibited state of smooth muscle myosin
    • D. Wendt, D. Taylor, T. Messier, K. M. Trybus, and K. A. Taylor, Visualization of head-interactions in the inhibited state of smooth muscle myosin, J. Cell. Biol. 147, 1385-1389 (1999).
    • (1999) J. Cell. Biol , vol.147 , pp. 1385-1389
    • Wendt, D.1    Taylor, D.2    Messier, T.3    Trybus, K.M.4    Taylor, K.A.5
  • 50
    • 0038545279 scopus 로고    scopus 로고
    • Refined model of the 10S conformation of smooth muscle by cryo-electron microscopy 3D image reconstruction
    • J. Liu, T. Wendt, D. Taylor, and K. Taylor, Refined model of the 10S conformation of smooth muscle by cryo-electron microscopy 3D image reconstruction, J. Mol. Biol. 329, 963-972 (2003).
    • (2003) J. Mol. Biol , vol.329 , pp. 963-972
    • Liu, J.1    Wendt, T.2    Taylor, D.3    Taylor, K.4
  • 54
    • 0019731755 scopus 로고
    • Mechanics and energetics of contraction in striated muscle of the sea scallop
    • J. A. Rall, Mechanics and energetics of contraction in striated muscle of the sea scallop, Placopecten magellanicus, J. Physiol. 321, 287-295 (1981).
    • (1981) Placopecten magellanicus, J. Physiol , vol.321 , pp. 287-295
    • Rall, J.A.1
  • 55
    • 0022240738 scopus 로고
    • Structural changes that occur in scallop myosin filaments upon activation
    • P. Vibert and R. Craig, Structural changes that occur in scallop myosin filaments upon activation, J. Cell. Biol. 101, 830-837 (1985).
    • (1985) J. Cell. Biol , vol.101 , pp. 830-837
    • Vibert, P.1    Craig, R.2
  • 56
    • 0037436352 scopus 로고    scopus 로고
    • 2+ causes release of myosin heads from the thick filament surface on the milliseconds time scale
    • 2+ causes release of myosin heads from the thick filament surface on the milliseconds time scale, J. Mol. Biol. 327, 145-158 (2003).
    • (2003) J. Mol. Biol , vol.327 , pp. 145-158
    • Zhao, F.-Q.1    Craig, R.2


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