메뉴 건너뛰기




Volumn 111, Issue 12, 2014, Pages 4626-4631

Structural dynamics of troponin during activation of skeletal muscle

Author keywords

Excitation contraction coupling; Muscle regulation; Muscle signaling

Indexed keywords

CALCIUM ION; FLUORESCENT DYE; MYOSIN; TROPOMYOSIN; TROPONIN;

EID: 84896950145     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1321868111     Document Type: Article
Times cited : (35)

References (43)
  • 1
    • 0000244537 scopus 로고
    • Structural changes in the actin- and myosin-containing filaments during contraction
    • Huxley HE (1973) Structural changes in the actin- and myosin-containing filaments during contraction. Cold Spring Harb Symp Quant Biol 37:361-376.
    • (1973) Cold Spring Harb Symp Quant Biol , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 2
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M (2000) Regulation of contraction in striated muscle. Physiol Rev 80(2):853-924. (Pubitemid 30164950)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 3
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop DF, Geeves MA (1993) Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament. Biophys J 65(2):693-701. (Pubitemid 23263882)
    • (1993) Biophysical Journal , vol.65 , Issue.2 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 4
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • Bremel RD, Weber A (1972) Cooperation within actin filament in vertebrate skeletal muscle. Nat New Biol 238(82):97-101.
    • (1972) Nat New Biol , vol.238 , Issue.82 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 7
    • 84863531575 scopus 로고    scopus 로고
    • Conformation of the troponin core complex in the thin filaments of skeletal muscle during relaxation and active contraction
    • Knowles AC, Irving M, Sun YB (2012) Conformation of the troponin core complex in the thin filaments of skeletal muscle during relaxation and active contraction. J Mol Biol 421(1):125-137.
    • (2012) J Mol Biol , vol.421 , Issue.1 , pp. 125-137
    • Knowles, A.C.1    Irving, M.2    Sun, Y.B.3
  • 8
    • 0029088936 scopus 로고
    • Structures of the troponin C regulatory domains in the apo and calcium-saturated states
    • Gagné SM, Tsuda S, Li MX, Smillie LB, Sykes BD (1995) Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nat Struct Biol 2(9):784-789.
    • (1995) Nat Struct Biol , vol.2 , Issue.9 , pp. 784-789
    • Gagné, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 9
    • 0037588762 scopus 로고    scopus 로고
    • 2+-saturated form
    • DOI 10.1038/nature01780
    • Takeda S, Yamashita A, Maeda K, Maéda Y (2003) Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. Nature 424(6944):35-41. (Pubitemid 36834832)
    • (2003) Nature , vol.424 , Issue.6944 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Maeda, Y.4
  • 10
    • 17044414488 scopus 로고    scopus 로고
    • Ca(2+)-regulated structural changes in troponin
    • Vinogradova MV, et al. (2005) Ca(2+)-regulated structural changes in troponin. Proc Natl Acad Sci USA 102(14):5038-5043.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.14 , pp. 5038-5043
    • Vinogradova, M.V.1
  • 11
    • 0030066749 scopus 로고    scopus 로고
    • Laser photolysis of caged calcium: Rates of calcium release by nitrophenyl-EGTA and DM-nitrophen
    • Ellis-Davies GC, Kaplan JH, Barsotti RJ (1996) Laser photolysis of caged calcium: Rates of calcium release by nitrophenyl-EGTA and DM-nitrophen. Biophys J 70(2):1006-1016. (Pubitemid 26028315)
    • (1996) Biophysical Journal , vol.70 , Issue.2 I , pp. 1006-1016
    • Ellis-Davies, G.C.R.1    Kaplan, J.H.2    Barsotti, R.J.3
  • 13
    • 0028175920 scopus 로고
    • Modulation of Ca2+ exchange with the Ca(2+)-specific regulatory sites of troponin C
    • Johnson JD, Nakkula RJ, Vasulka C, Smillie LB (1994) Modulation of Ca2+ exchange with the Ca(2+)-specific regulatory sites of troponin C. J Biol Chem 269(12):8919-8923.
    • (1994) J Biol Chem , vol.269 , Issue.12 , pp. 8919-8923
    • Johnson, J.D.1    Nakkula, R.J.2    Vasulka, C.3    Smillie, L.B.4
  • 15
    • 84885434032 scopus 로고    scopus 로고
    • The working stroke of the myosin II motor in muscle is not tightly coupled to release of orthophosphate from its active site
    • Caremani M, Melli L, Dolfi M, Lombardi V, Linari M (2013) The working stroke of the myosin II motor in muscle is not tightly coupled to release of orthophosphate from its active site. J Physiol 591(Pt 20):5187-5205.
    • (2013) J Physiol , vol.591 , Issue.PART 20 , pp. 5187-5205
    • Caremani, M.1    Melli, L.2    Dolfi, M.3    Lombardi, V.4    Linari, M.5
  • 16
    • 73949138935 scopus 로고    scopus 로고
    • A kinetic model that explains the effect of inorganic phosphate on the mechanics and energetics of isometric contraction of fast skeletal muscle
    • Linari M, Caremani M, Lombardi V (2010) A kinetic model that explains the effect of inorganic phosphate on the mechanics and energetics of isometric contraction of fast skeletal muscle. Proc Biol Sci 277(1678):19-27.
    • (2010) Proc Biol Sci , vol.277 , Issue.1678 , pp. 19-27
    • Linari, M.1    Caremani, M.2    Lombardi, V.3
  • 18
    • 58849127838 scopus 로고    scopus 로고
    • The effect of myofilament compliance on kinetics of force generation by myosin motors in muscle
    • Linari M, Piazzesi G, Lombardi V (2009) The effect of myofilament compliance on kinetics of force generation by myosin motors in muscle. Biophys J 96(2):583-592.
    • (2009) Biophys J , vol.96 , Issue.2 , pp. 583-592
    • Linari, M.1    Piazzesi, G.2    Lombardi, V.3
  • 20
    • 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(3):325-342.
    • (1986) J Mol Biol , vol.188 , Issue.3 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Faruqi, A.R.3    Hendrix, J.4
  • 21
    • 0037304613 scopus 로고    scopus 로고
    • An x-ray diffraction study on early structural changes in skeletal muscle contraction
    • Yagi N (2003) An x-ray diffraction study on early structural changes in skeletal muscle contraction. Biophys J 84(2 Pt 1):1093-1102.
    • (2003) Biophys J , vol.84 , Issue.2 PART 1 , pp. 1093-1102
    • Yagi, N.1
  • 22
    • 61549107574 scopus 로고    scopus 로고
    • Dynamics of thin-filament activation in rabbit skeletal muscle fibers examined by time-resolved x-ray diffraction
    • Tamura T, Wakayama J, Inoue K, Yagi N, Iwamoto H (2009) Dynamics of thin-filament activation in rabbit skeletal muscle fibers examined by time-resolved x-ray diffraction. Biophys J 96(3):1045-1055.
    • (2009) Biophys J , vol.96 , Issue.3 , pp. 1045-1055
    • Tamura, T.1    Wakayama, J.2    Inoue, K.3    Yagi, N.4    Iwamoto, H.5
  • 23
    • 0022606964 scopus 로고
    • Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain. A possible route of information transfer in activation of muscle contraction
    • Grabarek Z, Leavis PC, Gergely J (1986) Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain. A possible route of information transfer in activation of muscle contraction. J Biol Chem 261(2):608-613. (Pubitemid 16161713)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.2 , pp. 608-613
    • Grabarek, Z.1    Leavis, P.C.2    Gergely, J.3
  • 24
    • 0021918919 scopus 로고
    • Kinetic studies of calcium and magnesium binding to troponin C
    • Rosenfeld SS, Taylor EW (1985) Kinetic studies of calcium and magnesium binding to troponin C. J Biol Chem 260(1):242-251. (Pubitemid 15164042)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.1 , pp. 242-251
    • Rosenfeld, S.S.1    Taylor, E.W.2
  • 25
    • 0021916996 scopus 로고
    • Kinetic studies of calcium binding to regulatory complexes from skeletal muscle
    • Rosenfeld SS, Taylor EW (1985) Kinetic studies of calcium binding to regulatory complexes from skeletal muscle. J Biol Chem 260(1):252-261. (Pubitemid 15164043)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.1 , pp. 252-261
    • Rosenfeld, S.S.1    Taylor, E.W.2
  • 26
    • 84866516401 scopus 로고    scopus 로고
    • 2+-controlled changes of skeletal troponin I in psoas myofibrils
    • 2+-controlled changes of skeletal troponin I in psoas myofibrils. Biophys J 103(6):1254-1264.
    • (2012) Biophys J , vol.103 , Issue.6 , pp. 1254-1264
    • Lopez-Davila, A.J.1
  • 27
    • 77952801332 scopus 로고    scopus 로고
    • Monitoring the structural behavior of troponin andmyoplasmic free Ca2+ concentration during twitch of frog skeletalmuscle
    • Matsuo T, Iwamoto H, Yagi N (2010) Monitoring the structural behavior of troponin andmyoplasmic free Ca2+ concentration during twitch of frog skeletalmuscle. Biophys J 99(1):193-200.
    • (2010) Biophys J , vol.99 , Issue.1 , pp. 193-200
    • Matsuo, T.1    Iwamoto, H.2    Yagi, N.3
  • 28
    • 79954425826 scopus 로고    scopus 로고
    • Mechanism of latency relaxation in frog skeletal muscle
    • Yagi N (2011) Mechanism of latency relaxation in frog skeletal muscle. Prog Biophys Mol Biol 105(3):180-186.
    • (2011) Prog Biophys Mol Biol , vol.105 , Issue.3 , pp. 180-186
    • Yagi, N.1
  • 29
    • 53549085959 scopus 로고    scopus 로고
    • Structural changes in the muscle thin filament during contractions caused by single and double electrical pulses
    • Matsuo T, Yagi N (2008) Structural changes in the muscle thin filament during contractions caused by single and double electrical pulses. J Mol Biol 383(5):1019-1036.
    • (2008) J Mol Biol , vol.383 , Issue.5 , pp. 1019-1036
    • Matsuo, T.1    Yagi, N.2
  • 31
    • 0032734506 scopus 로고    scopus 로고
    • Kinetics of thin filament activation probed by fluorescence of N- ((2(lodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazolelabeled troponin I incorporated into skinned fibers of rabbit psoas muscle: Implications for regulation of muscle contraction
    • Brenner B, Chalovich JM (1999) Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz- 2-oxa-1,3-diazolelabeled troponin I incorporated into skinned fibers of rabbit psoas muscle: Implications for regulation of muscle contraction. Biophys J 77(5):2692-2708. (Pubitemid 29519514)
    • (1999) Biophysical Journal , vol.77 , Issue.5 , pp. 2692-2708
    • Brenner, B.1    Chalovich, J.M.2
  • 32
    • 0028179144 scopus 로고
    • Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • Lehman W, Craig R, Vibert P (1994) Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 368(6466):65-67.
    • (1994) Nature , vol.368 , Issue.6466 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 33
    • 33644941942 scopus 로고    scopus 로고
    • An atomic model of the thin filament in the relaxed and Ca2+-activated states
    • Pirani A, et al. (2006) An atomic model of the thin filament in the relaxed and Ca2+-activated states. J Mol Biol 357(3):707-717.
    • (2006) J Mol Biol , vol.357 , Issue.3 , pp. 707-717
    • Pirani, A.1
  • 34
    • 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(1):33-55.
    • (1973) J Mol Biol , vol.75 , Issue.1 , pp. 33-55
    • Parry, D.A.1    Squire, J.M.2
  • 35
    • 79955552373 scopus 로고    scopus 로고
    • Motion of myosin head domains during activation and force development in skeletal muscle
    • Reconditi M, et al. (2011) Motion of myosin head domains during activation and force development in skeletal muscle. Proc Natl Acad Sci USA 108(17):7236-7240.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.17 , pp. 7236-7240
    • Reconditi, M.1
  • 36
    • 77951623260 scopus 로고    scopus 로고
    • The molecular basis of the steep force-calcium relation in heart muscle
    • Sun YB, Irving M (2010) The molecular basis of the steep force-calcium relation in heart muscle. J Mol Cell Cardiol 48(5):859-865.
    • (2010) J Mol Cell Cardiol , vol.48 , Issue.5 , pp. 859-865
    • Sun, Y.B.1    Irving, M.2
  • 37
    • 13844272490 scopus 로고    scopus 로고
    • 2+ versus crossbridge contribution to force in rabbit skeletal fibres
    • DOI 10.1113/jphysiol.2004.077891
    • Moreno-Gonzalez A, Fredlund J, Regnier M (2005) Cardiac troponin C (TnC) and a site I skeletal TnC mutant alter Ca2+ versus crossbridge contribution to force in rabbit skeletal fibres. J Physiol 562(Pt 3):873-884. (Pubitemid 40246800)
    • (2005) Journal of Physiology , vol.562 , Issue.3 , pp. 873-884
    • Moreno-Gonzalez, A.1    Fredlund, J.2    Regnier, M.3
  • 38
    • 0029658403 scopus 로고    scopus 로고
    • The relationship between the intracellular Ca2+ transient and the isometric twitch force in frog muscle fibres
    • Sun YB, Lou F, Edman KA (1996) The relationship between the intracellular Ca2+ transient and the isometric twitch force in frog muscle fibres. Exp Physiol 81(5):711-724.
    • (1996) Exp Physiol , vol.81 , Issue.5 , pp. 711-724
    • Sun, Y.B.1    Lou, F.2    Edman, K.A.3
  • 39
    • 0017904793 scopus 로고
    • Calcium transients in isolated amphibian skeletal muscle fibres: Detection with aequorin
    • Blinks JR, Rüdel R, Taylor SR (1978) Calcium transients in isolated amphibian skeletal muscle fibres: Detection with aequorin. J Physiol 277:291-323. (Pubitemid 8343200)
    • (1978) Journal of Physiology , vol.277 , pp. 291-323
    • Blinks, J.R.1    Rudel, R.2    Taylor, S.R.3
  • 40
    • 70450177756 scopus 로고    scopus 로고
    • Structural changes in myosin motors and filaments during relaxation of skeletal muscle
    • Brunello E, et al. (2009) Structural changes in myosin motors and filaments during relaxation of skeletal muscle. J Physiol 587(Pt 18):4509-4521.
    • (2009) J Physiol , vol.587 , Issue.PART 18 , pp. 4509-4521
    • Brunello, E.1
  • 41
    • 0025364519 scopus 로고
    • Following tetanic stimulation, relaxation is accelerated by quick stretches of frog single muscle fibres
    • Lombardi V, Piazzesi G, Goldman YE (1990) Following tetanic stimulation, relaxation is accelerated by quick stretches of frog single muscle fibres. J Physiol 426:38P. (Pubitemid 20224771)
    • (1990) Journal of Physiology , vol.426
    • Lombardi, V.1    Piazzesi, G.2    Goldman, Y.E.3
  • 42
    • 0028180638 scopus 로고
    • Variation in myoplasmic Ca2+ concentration during contraction and relaxation studied by the indicator fluo-3 in frog muscle fibres
    • Caputo C, Edman KA, Lou F, Sun YB (1994) Variation in myoplasmic Ca2+ concentration during contraction and relaxation studied by the indicator fluo-3 in frog muscle fibres. J Physiol 478(Pt 1):137-148.
    • (1994) J Physiol , vol.478 , Issue.PART 1 , pp. 137-148
    • Caputo, C.1    Edman, K.A.2    Lou, F.3    Sun, Y.B.4
  • 43
    • 0032031751 scopus 로고    scopus 로고
    • A homobifunctional rhodamine for labeling proteins with defined orientations of a fluorophore
    • DOI 10.1021/bc970174e
    • Corrie JE, Craik JS, Munasinghe VR (1998) A homobifunctional rhodamine for labeling proteins with defined orientations of a fluorophore. Bioconjug Chem 9(2):160-167. (Pubitemid 28147132)
    • (1998) Bioconjugate Chemistry , vol.9 , Issue.2 , pp. 160-167
    • Corrie, J.E.T.1    Craik, J.S.2    Munasinghe, V.R.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.