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Volumn 108, Issue 1, 2011, Pages 120-125

X-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN; TROPOMYOSIN; TROPONIN;

EID: 78651062651     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1014599107     Document Type: Article
Times cited : (83)

References (50)
  • 1
    • 33749003228 scopus 로고    scopus 로고
    • Contributions of stretch activation to length-dependent contraction in murine myocardium
    • Stelzer JE, Moss RL (2006) Contributions of stretch activation to length-dependent contraction in murine myocardium. J Gen Physiol 128:461-471.
    • (2006) J Gen Physiol , vol.128 , pp. 461-471
    • Stelzer, J.E.1    Moss, R.L.2
  • 3
    • 0000285809 scopus 로고
    • Insect diversity and cladistic constraints
    • Wheeler QD (1990) Insect diversity and cladistic constraints. Ann Entomol Soc Am 83:1031-1047.
    • (1990) Ann Entomol Soc Am , vol.83 , pp. 1031-1047
    • Wheeler, Q.D.1
  • 4
    • 78651022505 scopus 로고
    • The excitation and contraction of the flight muscles of insects
    • Pringle JWS (1949) The excitation and contraction of the flight muscles of insects. J Physiol 108:226-232.
    • (1949) J Physiol , vol.108 , pp. 226-232
    • Pringle, J.W.S.1
  • 5
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley HE (1969) The mechanism of muscular contraction. Science 164:1356-1365.
    • (1969) Science , vol.164 , pp. 1356-1365
    • Huxley, H.E.1
  • 6
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction
    • Kress M, Huxley HE, Faruqi AR, Hendrix J (1986) Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction. J Mol Biol 188:325-342.
    • (1986) J Mol Biol , vol.188 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Faruqi, A.R.3    Hendrix, J.4
  • 7
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I, et al. (1993) Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58-65.
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1
  • 9
    • 17044414488 scopus 로고    scopus 로고
    • 2+-regulated structural changes in troponin
    • 2+-regulated structural changes in troponin. Proc Natl Acad Sci USA 102:5038-5043.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5038-5043
    • Vinogradova, M.V.1
  • 10
    • 77958534194 scopus 로고    scopus 로고
    • Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactions
    • Wu S, et al. (2010) Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactions. PLoS One 5:e12643.
    • (2010) PLoS One , vol.5
    • Wu, S.1
  • 11
    • 0031934618 scopus 로고    scopus 로고
    • X-ray diffraction indicates that active cross-bridges bind to actin target zones in insect flight muscle
    • Tregear RT, et al. (1998) X-ray diffraction indicates that active cross-bridges bind to actin target zones in insect flight muscle. Biophys J 74:1439-1451.
    • (1998) Biophys J , vol.74 , pp. 1439-1451
    • Tregear, R.T.1
  • 12
    • 0028235402 scopus 로고
    • Gold/Fab immuno electron microscopy localization of troponin H and troponin T in Lethocerusflight-muscle
    • Reedy MC, Reedy MK, Leonard KR, Bullard B (1994) Gold/Fab immuno electron microscopy localization of troponin H and troponin T in Lethocerusflight- muscle. J Mol Biol 239:52-67.
    • (1994) J Mol Biol , vol.239 , pp. 52-67
    • Reedy, M.C.1    Reedy, M.K.2    Leonard, K.R.3    Bullard, B.4
  • 13
    • 0000105113 scopus 로고
    • Synchrotron radiation as a source for X-ray diffraction
    • Rosenbaum G, Holmes KC, Witz J (1971) Synchrotron radiation as a source for X-ray diffraction. Nature 230:434-437.
    • (1971) Nature , vol.230 , pp. 434-437
    • Rosenbaum, G.1    Holmes, K.C.2    Witz, J.3
  • 14
    • 0018260965 scopus 로고
    • The Croonian Lecture, 1977. Stretch activation of muscle: Function and mechanism
    • Pringle JW (1978) The Croonian Lecture, 1977. Stretch activation of muscle: Function and mechanism. Proc Roy Soc Lond B Biol Sci 201:107-130.
    • (1978) Proc Roy Soc Lond B Biol Sci , vol.201 , pp. 107-130
    • Pringle, J.W.1
  • 15
    • 0015174379 scopus 로고
    • Mechanical activation and isometric oscillation in insect fibrillar muscle
    • Schadler M, Steiger GJ, Ruegg JC (1971) Mechanical activation and isometric oscillation in insect fibrillar muscle. Pflug Arch Eur J Phy 330:217-229.
    • (1971) Pflug Arch Eur J Phy , vol.330 , pp. 217-229
    • Schadler, M.1    Steiger, G.J.2    Ruegg, J.C.3
  • 16
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle
    • Huxley HE, Stewart A, Sosa H, Irving T (1994) X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys J 67:2411-2421.
    • (1994) Biophys J , vol.67 , pp. 2411-2421
    • Huxley, H.E.1    Stewart, A.2    Sosa, H.3    Irving, T.4
  • 17
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction
    • Wakabayashi K, et al. (1994) X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys J 67:2422-2435.
    • (1994) Biophys J , vol.67 , pp. 2422-2435
    • Wakabayashi, K.1
  • 18
    • 0026534392 scopus 로고
    • Myosin head movements are synchronous with the elementary force-generating process in muscle
    • Irving M, Lombardi V, Piazzesi G, Ferenczi MA (1992) Myosin head movements are synchronous with the elementary force-generating process in muscle. Nature 357:156-158.
    • (1992) Nature , vol.357 , pp. 156-158
    • Irving, M.1    Lombardi, V.2    Piazzesi, G.3    Ferenczi, M.A.4
  • 19
    • 33646957003 scopus 로고
    • Evidence of crossbridge movement during contraction of insect flight muscle
    • Tregear RT, Miller A (1969) Evidence of crossbridge movement during contraction of insect flight muscle. Nature 222:1184-1185.
    • (1969) Nature , vol.222 , pp. 1184-1185
    • Tregear, R.T.1    Miller, A.2
  • 20
    • 12744261252 scopus 로고    scopus 로고
    • Molecular dynamics of cyclically contracting insect flight muscle in vivo
    • Dickinson M, et al. (2005) Molecular dynamics of cyclically contracting insect flight muscle in vivo. Nature 433:330-334.
    • (2005) Nature , vol.433 , pp. 330-334
    • Dickinson, M.1
  • 21
    • 33747055586 scopus 로고    scopus 로고
    • The myosin filament superlattice in the flight muscles of flies: A-band lattice optimisation for stretch-activation?
    • Squire JM, et al. (2006) The myosin filament superlattice in the flight muscles of flies: A-band lattice optimisation for stretch-activation? J Mol Biol 361:823-838.
    • (2006) J Mol Biol , vol.361 , pp. 823-838
    • Squire, J.M.1
  • 22
    • 0018403331 scopus 로고
    • X-ray diffraction patterns from molecular arrangements with 38-nm periodicities around muscle thin filaments
    • Maeda Y (1979) X-ray diffraction patterns from molecular arrangements with 38-nm periodicities around muscle thin filaments. Nature 277:670-672.
    • (1979) Nature , vol.277 , pp. 670-672
    • Maeda, Y.1
  • 23
    • 0000244537 scopus 로고
    • Structural changes in actin-containing and myosin-containing filaments during contraction
    • Huxley HE (1973) Structural changes in actin-containing and myosin-containing filaments during contraction. Cold Spring Harbor Symp Quant Biol 37:361-376.
    • (1973) Cold Spring Harbor Symp Quant Biol , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 24
    • 0000733783 scopus 로고
    • X-Ray evidence for a conformational change in actin-containing filaments of vertebrate striated-muscle
    • Haselgrove JC (1973) X-Ray evidence for a conformational change in actin-containing filaments of vertebrate striated-muscle. Cold Spring Harbor Symp Quant Biol 37:341-352.
    • (1973) Cold Spring Harbor Symp Quant Biol , vol.37 , pp. 341-352
    • Haselgrove, J.C.1
  • 25
    • 0015935349 scopus 로고
    • Structural role of tropomyosin in muscle regulation: Analysis of the X-ray diffraction patterns from relaxed and contracting muscles
    • Parry DA, Squire JM (1973) Structural role of tropomyosin in muscle regulation: Analysis of the X-ray diffraction patterns from relaxed and contracting muscles. J Mol Biol 75:33-55.
    • (1973) J Mol Biol , vol.75 , pp. 33-55
    • Parry, D.A.1    Squire, J.M.2
  • 26
    • 33747767574 scopus 로고    scopus 로고
    • A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle
    • Poole KJ, et al. (2006) A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle. J Struct Biol 155:273-284.
    • (2006) J Struct Biol , vol.155 , pp. 273-284
    • Poole, K.J.1
  • 27
    • 85025365054 scopus 로고
    • An X-ray and light-diffraction study of filament lattice of striated muscle in living state and in rigor
    • Elliott GF, Lowy J, Worthington CR (1963) An X-ray and light-diffraction study of filament lattice of striated muscle in living state and in rigor. J Mol Biol 6:295-305.
    • (1963) J Mol Biol , vol.6 , pp. 295-305
    • Elliott, G.F.1    Lowy, J.2    Worthington, C.R.3
  • 28
    • 0025742843 scopus 로고
    • 2+-activated skinned fibres of the rabbit psoas muscle
    • 2+-activated skinned fibres of the rabbit psoas muscle. J Physiol 441:703-718.
    • (1991) J Physiol , vol.441 , pp. 703-718
    • Brenner, B.1    Yu, L.C.2
  • 29
    • 0035134731 scopus 로고    scopus 로고
    • Time-resolved X-ray diffraction by skinned skeletal muscle fibers during activation and shortening
    • Hoskins BK, Ashley CC, Rapp G, Griffiths PJ (2001) Time-resolved X-ray diffraction by skinned skeletal muscle fibers during activation and shortening. Biophys J 80:398-414.
    • (2001) Biophys J , vol.80 , pp. 398-414
    • Hoskins, B.K.1    Ashley, C.C.2    Rapp, G.3    Griffiths, P.J.4
  • 30
    • 85011215091 scopus 로고
    • X-ray diffraction studies on large-scale molecular structure of insect muscle
    • Worthington CR (1961) X-ray diffraction studies on large-scale molecular structure of insect muscle. J Mol Biol 3:618-633.
    • (1961) J Mol Biol , vol.3 , pp. 618-633
    • Worthington, C.R.1
  • 31
    • 0025906508 scopus 로고
    • Time-resolved X-ray diffraction studies on stretch-activated insect flight muscle
    • Rapp G, Guth K, Maeda Y, Poole KJ, Goody RS (1991) Time-resolved X-ray diffraction studies on stretch-activated insect flight muscle. J Muscle Res Cell Motil 12:208-215.
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 208-215
    • Rapp, G.1    Guth, K.2    Maeda, Y.3    Poole, K.J.4    Goody, R.S.5
  • 32
    • 0042092511 scopus 로고    scopus 로고
    • Myosin head configuration in relaxed insect flight muscle: X-ray modeled resting cross-bridges in a pre-powerstroke state are poised for actin binding
    • Al-Khayat HA, Hudson L, Reedy MK, Irving TC, Squire JM (2003) Myosin head configuration in relaxed insect flight muscle: X-ray modeled resting cross-bridges in a pre-powerstroke state are poised for actin binding. Biophys J 85:1063-1079.
    • (2003) Biophys J , vol.85 , pp. 1063-1079
    • Al-Khayat, H.A.1    Hudson, L.2    Reedy, M.K.3    Irving, T.C.4    Squire, J.M.5
  • 34
    • 0018580286 scopus 로고
    • Filament geometry and the activation of insect flight muscles
    • Wray JS (1979) Filament geometry and the activation of insect flight muscles. Nature 280:325-326.
    • (1979) Nature , vol.280 , pp. 325-326
    • Wray, J.S.1
  • 35
    • 0021636506 scopus 로고
    • A possible mechanism of length activation in insect fibrillar flight muscle
    • Abbott RH, Cage PE (1984) A possible mechanism of length activation in insect fibrillar flight muscle. J Muscle Res Cell Motil 5:387-397.
    • (1984) J Muscle Res Cell Motil , vol.5 , pp. 387-397
    • Abbott, R.H.1    Cage, P.E.2
  • 36
    • 0015477902 scopus 로고
    • Forces acting between muscle filaments. 1. Filament lattice spacing in bee flight muscle
    • Garamvölgyi N (1972) Forces acting between muscle filaments. 1. Filament lattice spacing in bee flight muscle. Acta Biochim Biophys Acad Sci Hung 7:157-164.
    • (1972) Acta Biochim Biophys Acad Sci Hung , vol.7 , pp. 157-164
    • Garamvölgyi, N.1
  • 37
    • 0014480867 scopus 로고
    • Distributed representations for actin-myosin interaction in oscillatory contraction of muscle
    • Thorson J, White DCS (1969) Distributed representations for actin-myosin interaction in oscillatory contraction of muscle. Biophys J 9:360-390.
    • (1969) Biophys J , vol.9 , pp. 360-390
    • Thorson, J.1    White, D.C.S.2
  • 38
    • 0027517018 scopus 로고
    • Interplay between passive tension and strong and weak binding cross-bridges in insect indirect flight muscle. A functional dissection by gelsolin-mediated thin filament removal
    • Granzier HL, Wang K (1993) Interplay between passive tension and strong and weak binding cross-bridges in insect indirect flight muscle. A functional dissection by gelsolin-mediated thin filament removal. J Gen Physiol 101:235-270.
    • (1993) J Gen Physiol , vol.101 , pp. 235-270
    • Granzier, H.L.1    Wang, K.2
  • 40
    • 1842562372 scopus 로고    scopus 로고
    • A troponin switch that regulates muscle contraction by stretch instead of calcium
    • Agianian B, et al. (2004) A troponin switch that regulates muscle contraction by stretch instead of calcium. EMBO J 23:772-779.
    • (2004) EMBO J , vol.23 , pp. 772-779
    • Agianian, B.1
  • 41
    • 48749092701 scopus 로고    scopus 로고
    • Reverse actin sliding triggers strong myosin binding that moves tropomyosin
    • Bekyarova TI, et al. (2008) Reverse actin sliding triggers strong myosin binding that moves tropomyosin. Proc Natl Acad Sci USA 105:10372-10377.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10372-10377
    • Bekyarova, T.I.1
  • 42
    • 77954380093 scopus 로고    scopus 로고
    • Fast X-ray recordings reveal dynamic action of contractile and regulatory proteins in stretch-activated insect flight muscle
    • Iwamoto H, Inoue K, Yagi N (2010) Fast X-ray recordings reveal dynamic action of contractile and regulatory proteins in stretch-activated insect flight muscle. Biophys J 99:184-192.
    • (2010) Biophys J , vol.99 , pp. 184-192
    • Iwamoto, H.1    Inoue, K.2    Yagi, N.3
  • 43
    • 4444284766 scopus 로고
    • Flight-tone and wing-stroke frequency of insects and the dynamics of insect flight
    • Sotavalta O (1952) Flight-tone and wing-stroke frequency of insects and the dynamics of insect flight. Nature 170:1057-1058.
    • (1952) Nature , vol.170 , pp. 1057-1058
    • Sotavalta, O.1
  • 44
    • 33751251988 scopus 로고    scopus 로고
    • An exceptionally fast actomyosin reaction powers insect flight muscle
    • Swank DM, Vishnudas VK, Maughan DW (2006) An exceptionally fast actomyosin reaction powers insect flight muscle. Proc Natl Acad Sci USA 103:17543-17547.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17543-17547
    • Swank, D.M.1    Vishnudas, V.K.2    Maughan, D.W.3
  • 45
    • 33745698376 scopus 로고    scopus 로고
    • The function of elastic proteins in the oscillatory contraction of insect flight muscle
    • Bullard B, Burkart C, Labeit S, Leonard K (2005) The function of elastic proteins in the oscillatory contraction of insect flight muscle. J Muscle Res Cell Motil 26:479-485.
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 479-485
    • Bullard, B.1    Burkart, C.2    Labeit, S.3    Leonard, K.4
  • 46
    • 0034627831 scopus 로고    scopus 로고
    • Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila
    • Hakeda S, Endo S, Saigo K (2000) Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila. J Cell Biol 148:101-114.
    • (2000) J Cell Biol , vol.148 , pp. 101-114
    • Hakeda, S.1    Endo, S.2    Saigo, K.3
  • 47
    • 0033514477 scopus 로고    scopus 로고
    • The stretch-activation response may be critical to the proper functioning of the mammalian heart
    • Vemuri R, et al. (1999) The stretch-activation response may be critical to the proper functioning of the mammalian heart. Proc Natl Acad Sci USA 96:1048-1053.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1048-1053
    • Vemuri, R.1
  • 48
    • 77951623075 scopus 로고    scopus 로고
    • Myofilament length dependent activation
    • de Tombe PP, et al. (2010) Myofilament length dependent activation. J Mol Cell Cardiol 48:851-858.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 851-858
    • De Tombe, P.P.1
  • 49
    • 59849109729 scopus 로고    scopus 로고
    • Close proximity of myosin loop 3 to troponin determined by triangulation of resonance energy transfer distance measurements
    • Patel DA, Root DD (2009) Close proximity of myosin loop 3 to troponin determined by triangulation of resonance energy transfer distance measurements. Biochemistry 48:357-369.
    • (2009) Biochemistry , vol.48 , pp. 357-369
    • Patel, D.A.1    Root, D.D.2
  • 50
    • 0027999088 scopus 로고
    • Oblique section 3-D reconstruction of relaxed insect flight muscle reveals the cross-bridge lattice in helical registration
    • Schmitz H, Lucaveche C, Reedy MK, Taylor KA (1994) Oblique section 3-D reconstruction of relaxed insect flight muscle reveals the cross-bridge lattice in helical registration. Biophys J 67:1620-1633.
    • (1994) Biophys J , vol.67 , pp. 1620-1633
    • Schmitz, H.1    Lucaveche, C.2    Reedy, M.K.3    Taylor, K.A.4


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