메뉴 건너뛰기




Volumn 3, Issue 4, 2014, Pages 846-865

The intriguing dual lattices of the myosin filaments in vertebrate striated muscles: Evolution and advantage

Author keywords

Bare region; Electron microscopy; M band; Myosin filament; Myosin filament lattice; Thick filament; Vertebrate striated muscle; X ray diffraction

Indexed keywords

VERTEBRATA;

EID: 84914095928     PISSN: None     EISSN: 20797737     Source Type: Journal    
DOI: 10.3390/biology3040846     Document Type: Review
Times cited : (22)

References (49)
  • 1
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction; interference microscopy of living muscle fibres
    • Huxley, A.F.; Niedergerke, R. Structural changes in muscle during contraction; interference microscopy of living muscle fibres. Nature 1954, 173, 971-973.
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 2
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
    • Huxley, H.; Hanson, J. Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 1954, 173, 973-976.
    • (1954) Nature , vol.173 , pp. 973-976
    • Huxley, H.1    Hanson, J.2
  • 3
    • 85012414651 scopus 로고
    • Electron microscopic studies on the structure of natural and synthetic protein filaments from striated muscle
    • Huxley, H.E. Electron microscopic studies on the structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol. 1963, 7, 281-308.
    • (1963) J. Mol. Biol , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 4
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley, H.E. The mechanism of muscular contraction. Science 1969, 164, 1356-1365.
    • (1969) Science , vol.164 , pp. 1356-1365
    • Huxley, H.E.1
  • 5
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn, R.W.; Taylor, E.W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 1971, 10, 4617-4624.
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 6
    • 0001353052 scopus 로고
    • The double array of filaments in cross-striated muscle
    • Huxley, H.E. The double array of filaments in cross-striated muscle. J. Biophys. Biochem. Cyt. 1957, 3, 631.
    • (1957) J. Biophys. Biochem. Cyt , vol.3 , pp. 631
    • Huxley, H.E.1
  • 7
    • 0000700952 scopus 로고
    • Electron microscope studies of the organisation of the filaments in striated muscle
    • Huxley, H.E. Electron microscope studies of the organisation of the filaments in striated muscle. Biochim. Biophys. Acta 1953, 12, 387-394.
    • (1953) Biochim. Biophys. Acta , vol.12 , pp. 387-394
    • Huxley, H.E.1
  • 8
    • 85010916780 scopus 로고
    • The structure of f-actin and of action filaments isolated from muscle
    • Hanson, J.; Lowy, J. The structure of f-actin and of action filaments isolated from muscle. J. Mol. Biol. 1963, 6, 48-60.
    • (1963) J. Mol. Biol , vol.6 , pp. 48-60
    • Hanson, J.1    Lowy, J.2
  • 9
    • 85010249552 scopus 로고
    • The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor
    • Huxley, H.E.; Brown, W. The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 1967, 30, 383-434.
    • (1967) J. Mol. Biol , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 10
    • 0022471785 scopus 로고
    • “Crystalline” myosin cross-bridge array in relaxed bony fish muscle. Low-angle X-ray diffraction from plaice fin muscle and its interpretation
    • Harford, J.; Squire, J. “Crystalline” myosin cross-bridge array in relaxed bony fish muscle. Low-angle X-ray diffraction from plaice fin muscle and its interpretation. Biophys. J. 1986, 50, 145-155.
    • (1986) Biophys. J. , vol.50 , pp. 145-155
    • Harford, J.1    Squire, J.2
  • 11
    • 0015227575 scopus 로고
    • General model for the structure of all myosin-containing filaments
    • Squire, J.M. General model for the structure of all myosin-containing filaments. Nature 1971, 233, 457-462.
    • (1971) Nature , vol.233 , pp. 457-462
    • Squire, J.M.1
  • 12
    • 0015506523 scopus 로고
    • General model of myosin filament structure. II. Myosin filaments and cross-bridge interactions in vertebrate striated and insect flight muscles
    • Squire, J.M. General model of myosin filament structure. II. Myosin filaments and cross-bridge interactions in vertebrate striated and insect flight muscles. J. Mol. Biol. 1972, 72, 125-138.
    • (1972) J. Mol. Biol , vol.72 , pp. 125-138
    • Squire, J.M.1
  • 13
    • 0016320138 scopus 로고
    • Symmetry and three-dimensional arrangement of filaments in vertebrate striated muscle
    • Squire, J.M. Symmetry and three-dimensional arrangement of filaments in vertebrate striated muscle. J. Mol. Biol. 1974, 90, 153–160.
    • (1974) J. Mol. Biol , vol.90 , pp. 153-160
    • Squire, J.M.1
  • 14
    • 0018117477 scopus 로고
    • Three-dimensional structure of the vertebrate muscle M-region
    • Luther, P.; Squire, J. Three-dimensional structure of the vertebrate muscle M-region. J. Mol. Biol. 1978, 125, 313–324.
    • (1978) J. Mol. Biol , vol.125 , pp. 313-324
    • Luther, P.1    Squire, J.2
  • 15
    • 0019873637 scopus 로고
    • Three-dimensional structure of the vertebrate muscle A-band. III. M-region structure and myosin filament symmetry
    • Luther, P.K.; Munro, P.M.; Squire, J.M. Three-dimensional structure of the vertebrate muscle A-band. III. M-region structure and myosin filament symmetry. J. Mol. Biol. 1981, 151, 703–730.
    • (1981) J. Mol. Biol. , vol.151 , pp. 703-730
    • Luther, P.K.1    Munro, P.M.2    Squire, J.M.3
  • 16
    • 0019331904 scopus 로고
    • Fraying of A-filaments into three subfilaments
    • Maw, M.C.; Rowe, A.J. Fraying of A-filaments into three subfilaments. Nature 1980, 286, 412–414.
    • (1980) Nature , vol.286 , pp. 412-414
    • Maw, M.C.1    Rowe, A.J.2
  • 17
    • 0022584589 scopus 로고
    • An ultrastructural study of cross-bridge arrangement in the frog thigh muscle thick filament
    • Kensler, R.W.; Stewart, M. An ultrastructural study of cross-bridge arrangement in the frog thigh muscle thick filament. Biophys. J. 1986, 49, 343–351.
    • (1986) Biophys. J , vol.49 , pp. 343-351
    • Kensler, R.W.1    Stewart, M.2
  • 18
    • 0019124921 scopus 로고
    • Three-dimensional structure of the vertebrate muscle A-band. II. The myosin filament superlattice
    • Luther, P.K.; Squire, J.M. Three-dimensional structure of the vertebrate muscle A-band. II. The myosin filament superlattice. J. Mol. Biol. 1980, 141, 409–439.
    • (1980) J. Mol. Biol. , vol.141 , pp. 409-439
    • Luther, P.K.1    Squire, J.M.2
  • 19
    • 0014311964 scopus 로고
    • The ultrastructure of the M line in skeletal muscle
    • Knappeis, G.G.; Carlsen, F. The ultrastructure of the M line in skeletal muscle. J. Cell Biol. 1968, 38, 202–211.
    • (1968) J. Cell Biol , vol.38 , pp. 202-211
    • Knappeis, G.G.1    Carlsen, F.2
  • 20
    • 0017325762 scopus 로고
    • Fine structure of the A-band in cryo-sections. The structure of the A-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained
    • Sjostrom, M.; Squire, J.M. Fine structure of the A-band in cryo-sections. The structure of the A-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained. J. Mol. Biol. 1977, 109, 49–68.
    • (1977) J. Mol. Biol. , vol.109 , pp. 49-68
    • Sjostrom, M.1    Squire, J.M.2
  • 21
    • 0021246491 scopus 로고
    • Three-dimensional reconstruction from tilted sections of fish muscle M-band
    • Luther, P.K.; Crowther, R.A. Three-dimensional reconstruction from tilted sections of fish muscle M-band. Nature 1984, 307, 566–568.
    • (1984) Nature , vol.307 , pp. 566-568
    • Luther, P.K.1    Crowther, R.A.2
  • 22
    • 24344470264 scopus 로고    scopus 로고
    • The M-band: An elastic web that crosslinks thick filaments in the center of the sarcomere
    • Agarkova, I.; Perriard, J.C. The M-band: An elastic web that crosslinks thick filaments in the center of the sarcomere. Trends Cell Biol. 2005, 15, 477–485.
    • (2005) Trends Cell Biol , vol.15 , pp. 477-485
    • Agarkova, I.1    Perriard, J.C.2
  • 23
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: Localization of defined domains of myomesin, M-protein, and the 250-kd carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann, W.M.; Gautel, M.; Steiner, F.; van der Ven, P.F.; Weber, K.; Furst, D.O. The structure of the sarcomeric M band: Localization of defined domains of myomesin, M-protein, and the 250-kd carboxy-terminal region of titin by immunoelectron microscopy. J. Cell Biol. 1996, 134, 1441–1453.
    • (1996) J. Cell Biol , vol.134 , pp. 1441-1453
    • Obermann, W.M.1    Gautel, M.2    Steiner, F.3    Van Der Ven, P.F.4    Weber, K.5    Furst, D.O.6
  • 25
    • 0016838353 scopus 로고
    • Structure of muscle filaments from immunohistochemical and ultrastructural studies
    • Pepe, F.A. Structure of muscle filaments from immunohistochemical and ultrastructural studies. J. Histochem. Cytochem. 1975, 23, 543–562.
    • (1975) J. Histochem. Cytochem , vol.23 , pp. 543-562
    • Pepe, F.A.1
  • 26
    • 0030250140 scopus 로고    scopus 로고
    • Evolution of myosin filament arrangements in vertebrate skeletal muscle
    • Luther, P.K.; Squire, J.M.; Forey, P.L. Evolution of myosin filament arrangements in vertebrate skeletal muscle. J. Morphol. 1996, 229, 325–335.
    • (1996) J. Morphol , vol.229 , pp. 325-335
    • Luther, P.K.1    Squire, J.M.2    Forey, P.L.3
  • 27
    • 84971113792 scopus 로고
    • The orientation of muscle fibres in the myomeres of fishes
    • Alexander, R.M. The orientation of muscle fibres in the myomeres of fishes. J. Marine Biol. Assoc. UK 1969, 49, 263–290.
    • (1969) J. Marine Biol. Assoc. UK , vol.49 , pp. 263-290
    • Alexander, R.M.1
  • 29
    • 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.; Squire, J.M. M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles. J. Muscle Res. Cell Motil. 1994, 15, 633–645.
    • (1994) J. Muscle Res. Cell Motil , vol.15 , pp. 633-645
    • Pask, H.T.1    Jones, K.L.2    Luther, P.K.3    Squire, J.M.4
  • 30
    • 77958502526 scopus 로고    scopus 로고
    • Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis
    • Al-Khayat, H.A.; Kensler, R.W.; Morris, E.P.; Squire, J.M. Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis. J. Mol. Biol. 2010, 403, 763–776.
    • (2010) J. Mol. Biol , vol.403 , pp. 763-776
    • Al-Khayat, H.A.1    Kensler, R.W.2    Morris, E.P.3    Squire, J.M.4
  • 31
    • 0031034775 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric 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.; Furst, D.O. Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin. Embo. J. 1997, 16, 211–220.
    • (1997) Embo. J. , vol.16 , pp. 211-220
    • Obermann, W.M.1    Gautel, M.2    Weber, K.3    Furst, D.O.4
  • 33
    • 0014432527 scopus 로고
    • Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor cross-bridge lattice
    • Reedy, M.K. Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor cross-bridge lattice. J. Mol. Biol. 1968, 31, 155–176.
    • (1968) J. Mol. Biol , vol.31 , pp. 155-176
    • Reedy, M.K.1
  • 34
    • 0026351550 scopus 로고
    • The 4-stranded helical arrangement of myosin heads on insect (Lethocerus) flight muscle thick filaments
    • Morris, E.P.; Squire, J.M.; Fuller, G.W. The 4-stranded helical arrangement of myosin heads on insect (Lethocerus) flight muscle thick filaments. J. Struct. Biol. 1991, 107, 221–226.
    • (1991) J. Struct. Biol , vol.107 , pp. 221-226
    • Morris, E.P.1    Squire, J.M.2    Fuller, G.W.3
  • 35
    • 0019815071 scopus 로고
    • Fraction of myosin heads bound to thin filaments in rigor fibrils from insect flight and vertebrate muscles
    • Lovell, S.J.; Knight, P.J.; Harrington, W.F. Fraction of myosin heads bound to thin filaments in rigor fibrils from insect flight and vertebrate muscles. Nature 1981, 293, 664–666.
    • (1981) Nature , vol.293 , pp. 664-666
    • Lovell, S.J.1    Knight, P.J.2    Harrington, W.F.3
  • 37
    • 0014104305 scopus 로고
    • Recent X-ray diffraction and electron microscope studies of striated muscle
    • Huxley, H.E. Recent X-ray diffraction and electron microscope studies of striated muscle. J. Gen. Physiol. 1967, 50, S71–S83.
    • (1967) J. Gen. Physiol , vol.50 , pp. S71-S83
    • Huxley, H.E.1
  • 38
    • 0013854361 scopus 로고
    • X-ray diffraction from living striated muscle during contraction
    • Elliott, G.F.; Lowy, J.; Millman, B.M. X-ray diffraction from living striated muscle during contraction. Nature 1965, 206, 1357–1358.
    • (1965) Nature , vol.206 , pp. 1357-1358
    • Elliott, G.F.1    Lowy, J.2    Millman, B.M.3
  • 39
    • 0014202446 scopus 로고
    • Low-angle X-ray diffraction studies of living striated muscle during contraction
    • Elliott, G.F.; Lowy, J.; Millman, B.M. Low-angle X-ray diffraction studies of living striated muscle during contraction. J. Mol. Biol. 1967, 25, 31–45.
    • (1967) J. Mol. Biol , vol.25 , pp. 31-45
    • Elliott, G.F.1    Lowy, J.2    Millman, B.M.3
  • 40
    • 85048208724 scopus 로고    scopus 로고
    • Gerald Elliott
    • Squire, J.M. Obituary: Professor Gerald Elliott. J. Muscle Res. Cell Motil. 2013, 34, 429–436.
    • (2013) Obituary: Professor , vol.34 , pp. 429-436
    • Squire, J.M.1
  • 41
    • 84871480306 scopus 로고    scopus 로고
    • Head-head interactions of resting myosin crossbridges in intact frog skeletal muscles, revealed by synchrotron X-ray fiber diffraction
    • Oshima, K.; Sugimoto, Y.; Irving, T.C.; Wakabayashi, K. Head-head interactions of resting myosin crossbridges in intact frog skeletal muscles, revealed by synchrotron X-ray fiber diffraction. PLoS One 2012, 7, e52421.
    • (2012) Plos One , vol.7
    • Oshima, K.1    Sugimoto, Y.2    Irving, T.C.3    Wakabayashi, K.4
  • 42
    • 0030729013 scopus 로고    scopus 로고
    • Myosin head configuration in relaxed fish muscle: Resting state myosin heads must swing axially by up to 150 Å or turn upside down to reach rigor
    • Hudson, L.; Harford, J.J.; Denny, R.C.; Squire, J.M. Myosin head configuration in relaxed fish muscle: Resting state myosin heads must swing axially by up to 150 Å or turn upside down to reach rigor. J. Mol. Biol. 1997, 273, 440–455.
    • (1997) J. Mol. Biol , vol.273 , pp. 440-455
    • Hudson, L.1    Harford, J.J.2    Denny, R.C.3    Squire, J.M.4
  • 43
    • 33747809256 scopus 로고    scopus 로고
    • Refined structure of bony fish muscle myosin filaments from low-angle X-ray diffraction data
    • Al-Khayat, H.A.; Squire, J.M. Refined structure of bony fish muscle myosin filaments from low-angle X-ray diffraction data. J. Struct. Biol. 2006, 155, 218–229.
    • (2006) J. Struct. Biol , vol.155 , pp. 218-229
    • Al-Khayat, H.A.1    Squire, J.M.2
  • 44
    • 0021250322 scopus 로고
    • Three-dimensional reconstruction from a single oblique section of fish muscle M-band
    • Crowther, R.A.; Luther, P.K. Three-dimensional reconstruction from a single oblique section of fish muscle M-band. Nature 1984, 307, 569–570.
    • (1984) Nature , vol.307 , pp. 569-570
    • Crowther, R.A.1    Luther, P.K.2
  • 46
    • 55549097137 scopus 로고    scopus 로고
    • Direct modeling of X-ray diffraction pattern from contracting skeletal muscle
    • Koubassova, N.A.; Bershitsky, S.Y.; Ferenczi, M.A.; Tsaturyan, A.K. Direct modeling of X-ray diffraction pattern from contracting skeletal muscle. Biophys. J. 2008, 95, 2880–2894.
    • (2008) Biophys. J , vol.95 , pp. 2880-2894
    • Koubassova, N.A.1    Bershitsky, S.Y.2    Ferenczi, M.A.3    Tsaturyan, A.K.4
  • 47
    • 0035997061 scopus 로고    scopus 로고
    • Direct modeling of X-ray diffraction pattern from skeletal muscle in rigor
    • Koubassova, N.A.; Tsaturyan, A.K. Direct modeling of X-ray diffraction pattern from skeletal muscle in rigor. Biophys. J. 2002, 83, 1082–1097.
    • (2002) Biophys. J , vol.83 , pp. 1082-1097
    • Koubassova, N.A.1    Tsaturyan, A.K.2
  • 48
    • 79953057626 scopus 로고    scopus 로고
    • Modelling X-ray diffraction from the myosin superlattice of vertebrate muscle
    • Wojtas, D.H.; Yoon, C.; Millane, R.; Squire, J. Modelling X-ray diffraction from the myosin superlattice of vertebrate muscle. Biophys. J. 2009, 96, 615a–616a.
    • (2009) Biophys. J , vol.96 , pp. 615a-616a
    • Wojtas, D.H.1    Yoon, C.2    Millane, R.3    Squire, J.4
  • 49
    • 0020583740 scopus 로고
    • Co-ordinated electron microscopy and X-ray studies of glycerinated insect flight muscle. I. X-ray diffraction monitoring during preparation for electron microscopy of muscle fibres fixed in rigor, in ATP and in AMPPNP
    • Reedy, M.K.; Goody, R.S.; Hofmann, W.; Rosenbaum, G. Co-ordinated electron microscopy and X-ray studies of glycerinated insect flight muscle. I. X-ray diffraction monitoring during preparation for electron microscopy of muscle fibres fixed in rigor, in ATP and in AMPPNP. J. Muscle Res. Cell Motil. 1983, 4, 25–53.
    • (1983) J. Muscle Res. Cell Motil , vol.4 , pp. 25-53
    • Reedy, M.K.1    Goody, R.S.2    Hofmann, W.3    Rosenbaum, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.