메뉴 건너뛰기




Volumn 110, Issue 21, 2013, Pages 8561-8566

Structural basis of the relaxed state of a Ca2+-regulated myosin filament and its evolutionary implications

Author keywords

3D reconstruction; Molluscan muscle; Muscle regulation; Scallop muscle; Thick filament structure

Indexed keywords

CALCIUM ION; MYOSIN;

EID: 84878128694     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1218462110     Document Type: Article
Times cited : (43)

References (53)
  • 1
    • 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.
    • (2000) Physiol Rev , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 2
    • 0027300234 scopus 로고
    • Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function
    • Sweeney HL, Bowman BF, Stull JT (1993) Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function. Am J Physiol 264(5 Pt 1):C1085-C1095.
    • (1993) Am J Physiol , vol.264 , Issue.5 PART 1
    • Sweeney, H.L.1    Bowman, B.F.2    Stull, J.T.3
  • 3
    • 0028558668 scopus 로고
    • Role of myosin light chains
    • Trybus KM (1994) Role of myosin light chains. J Muscle Res Cell Motil 15(6): 587-594.
    • (1994) J Muscle Res Cell Motil , vol.15 , Issue.6 , pp. 587-594
    • Trybus, K.M.1
  • 4
    • 0019877301 scopus 로고
    • Phosphorylation-dependent regulation of Limulus myosin
    • Sellers JR (1981) Phosphorylation-dependent regulation of Limulus myosin. J Biol Chem 256(17): 9274-9278.
    • (1981) J Biol Chem , vol.256 , Issue.17 , pp. 9274-9278
    • Sellers, J.R.1
  • 5
    • 0016803961 scopus 로고
    • Calcium regulation of muscle contraction
    • Szent-Györgyi AG (1975) Calcium regulation of muscle contraction. Biophys J 15(7): 707-723.
    • (1975) Biophys J , vol.15 , Issue.7 , pp. 707-723
    • Szent-Györgyi, A.G.1
  • 7
    • 0023601047 scopus 로고
    • Structural changes accompanying phosphorylation of tarantula muscle myosin filaments
    • Craig R, Padrón R, Kendrick-Jones J (1987) Structural changes accompanying phosphorylation of tarantula muscle myosin filaments. J Cell Biol 105(3): 1319-1327.
    • (1987) J Cell Biol , vol.105 , Issue.3 , pp. 1319-1327
    • Craig, R.1    Padrón, R.2    Kendrick-Jones, J.3
  • 8
    • 79958748938 scopus 로고    scopus 로고
    • Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle
    • Stull JT, Kamm KE, Vandenboom R (2011) Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle. Arch Biochem Biophys 510(2): 120-128.
    • (2011) Arch Biochem Biophys , vol.510 , Issue.2 , pp. 120-128
    • Stull, J.T.1    Kamm, K.E.2    Vandenboom, R.3
  • 9
    • 0035836733 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2
    • Wendt T, Taylor D, Trybus KM, Taylor K (2001) Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2. Proc Natl Acad Sci USA 98(8): 4361-4366.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.8 , pp. 4361-4366
    • Wendt, T.1    Taylor, D.2    Trybus, K.M.3    Taylor, K.4
  • 10
    • 34548478783 scopus 로고    scopus 로고
    • Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state
    • Burgess SA, et al. (2007) Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state. J Mol Biol 372(5): 1165-1178.
    • (2007) J Mol Biol , vol.372 , Issue.5 , pp. 1165-1178
    • Burgess, S.A.1
  • 11
    • 85012414651 scopus 로고
    • Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle
    • Huxley HE (1963) Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J Mol Biol 7(3): 281-308.
    • (1963) J Mol Biol , vol.7 , Issue.3 , pp. 281-308
    • Huxley, H.E.1
  • 12
    • 33646009721 scopus 로고    scopus 로고
    • Structure and function of myosin filaments
    • Craig R, Woodhead JL (2006) Structure and function of myosin filaments. Curr Opin Struct Biol 16(2): 204-212.
    • (2006) Curr Opin Struct Biol , vol.16 , Issue.2 , pp. 204-212
    • Craig, R.1    Woodhead, J.L.2
  • 13
    • 24144484776 scopus 로고    scopus 로고
    • Atomic model of a myosin filament in the relaxed state
    • Woodhead JL, et al. (2005) Atomic model of a myosin filament in the relaxed state. Nature 436(7054): 1195-1199.
    • (2005) Nature , vol.436 , Issue.7054 , pp. 1195-1199
    • Woodhead, J.L.1
  • 14
    • 2342536996 scopus 로고    scopus 로고
    • Estimating metazoan divergence times with a molecular clock
    • Peterson KJ, et al. (2004) Estimating metazoan divergence times with a molecular clock. Proc Natl Acad Sci USA 101(17): 6536-6541.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.17 , pp. 6536-6541
    • Peterson, K.J.1
  • 15
    • 40649098633 scopus 로고    scopus 로고
    • Three-dimensional structure of vertebrate cardiac muscle myosin filaments
    • Zoghbi ME, Woodhead JL, Moss RL, Craig R (2008) Three-dimensional structure of vertebrate cardiac muscle myosin filaments. Proc Natl Acad Sci USA 105(7): 2386-2390.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.7 , pp. 2386-2390
    • Zoghbi, M.E.1    Woodhead, J.L.2    Moss, R.L.3    Craig, R.4
  • 16
    • 58149092608 scopus 로고    scopus 로고
    • Head-head interaction characterizes the relaxed state of Limulus muscle myosin filaments
    • Zhao FQ, Craig R, Woodhead JL (2009) Head-head interaction characterizes the relaxed state of Limulus muscle myosin filaments. J Mol Biol 385(2): 423-431.
    • (2009) J Mol Biol , vol.385 , Issue.2 , pp. 423-431
    • Zhao, F.Q.1    Craig, R.2    Woodhead, J.L.3
  • 17
    • 47049110451 scopus 로고    scopus 로고
    • Head-head and head-tail interaction: A general mechanism for switching off myosin II activity in cells
    • Jung HS, Komatsu S, Ikebe M, Craig R (2008) Head-head and head-tail interaction: A general mechanism for switching off myosin II activity in cells. Mol Biol Cell 19(8): 3234-3242.
    • (2008) Mol Biol Cell , vol.19 , Issue.8 , pp. 3234-3242
    • Jung, H.S.1    Komatsu, S.2    Ikebe, M.3    Craig, R.4
  • 18
    • 43149115617 scopus 로고    scopus 로고
    • Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution
    • Jung HS, et al. (2008) Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution. Proc Natl Acad Sci USA 105(16): 6022-6026.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.16 , pp. 6022-6026
    • Jung, H.S.1
  • 19
    • 0016695131 scopus 로고
    • Diversity of cross-bridge configurations in invertebrate muscles
    • Wray JS, Vibert PJ, Cohen C (1975) Diversity of cross-bridge configurations in invertebrate muscles. Nature 257(5527): 561-564.
    • (1975) Nature , vol.257 , Issue.5527 , pp. 561-564
    • Wray, J.S.1    Vibert, P.J.2    Cohen, C.3
  • 20
    • 0020552088 scopus 로고
    • Electron microscopy and image analysis of myosin filaments from scallop striated muscle
    • Vibert P, Craig R (1983) Electron microscopy and image analysis of myosin filaments from scallop striated muscle. J Mol Biol 165(2): 303-320.
    • (1983) J Mol Biol , vol.165 , Issue.2 , pp. 303-320
    • Vibert, P.1    Craig, R.2
  • 21
    • 0026588964 scopus 로고
    • Helical reconstruction of frozen-hydrated scallop myosin filaments
    • Vibert P (1992) Helical reconstruction of frozen-hydrated scallop myosin filaments. J Mol Biol 223(3): 661-671.
    • (1992) J Mol Biol , vol.223 , Issue.3 , pp. 661-671
    • Vibert, P.1
  • 22
    • 0017074536 scopus 로고
    • Structure of the cross-striated adductor muscle of the scallop
    • Millman BM, Bennett PM (1976) Structure of the cross-striated adductor muscle of the scallop. J Mol Biol 103(3): 439-467.
    • (1976) J Mol Biol , vol.103 , Issue.3 , pp. 439-467
    • Millman, B.M.1    Bennett, P.M.2
  • 23
    • 0037436352 scopus 로고    scopus 로고
    • Ca2+ causes release of myosin heads from the thick filament surface on the milliseconds time scale
    • Zhao FQ, Craig R (2003) Ca2+ causes release of myosin heads from the thick filament surface on the milliseconds time scale. J Mol Biol 327(1): 145-158.
    • (2003) J Mol Biol , vol.327 , Issue.1 , pp. 145-158
    • Zhao, F.Q.1    Craig, R.2
  • 24
    • 0345528058 scopus 로고    scopus 로고
    • Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Å resolution: Flexibility and function in the head
    • Gourinath S, et al. (2003) Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Å resolution: Flexibility and function in the head. Structure 11(12): 1621-1627.
    • (2003) Structure , vol.11 , Issue.12 , pp. 1621-1627
    • Gourinath, S.1
  • 25
    • 70350735944 scopus 로고    scopus 로고
    • The onoff switch in regulated myosins: Different triggers but related mechanisms
    • Himmel DM, Mui S, O'Neall-Hennessey E, Szent-Györgyi AG, Cohen C (2009) The onoff switch in regulated myosins: Different triggers but related mechanisms. J Mol Biol 394(3): 496-505.
    • (2009) J Mol Biol , vol.394 , Issue.3 , pp. 496-505
    • Himmel, D.M.1    Mui, S.2    O'Neall-Hennessey, E.3    Szent-Györgyi, A.G.4    Cohen, C.5
  • 26
    • 37549054688 scopus 로고    scopus 로고
    • An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins
    • Brown JH, et al. (2008) An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins. J Mol Biol 375(5): 1434-1443.
    • (2008) J Mol Biol , vol.375 , Issue.5 , pp. 1434-1443
    • Brown, J.H.1
  • 27
    • 56249115186 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity
    • Alamo L, et al. (2008) Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity. J Mol Biol 384(4): 780-797.
    • (2008) J Mol Biol , vol.384 , Issue.4 , pp. 780-797
    • Alamo, L.1
  • 28
    • 84855793610 scopus 로고    scopus 로고
    • Phosphorylated smooth muscle heavy meromyosin shows an open conformation linked to activation
    • Baumann BA, et al. (2012) Phosphorylated smooth muscle heavy meromyosin shows an open conformation linked to activation. J Mol Biol 415(2): 274-287.
    • (2012) J Mol Biol , vol.415 , Issue.2 , pp. 274-287
    • Baumann, B.A.1
  • 29
    • 0026607882 scopus 로고
    • Location of paramyosin in relation to the subfilaments within the thick filaments of scallop striated muscle
    • Castellani L, Vibert P (1992) Location of paramyosin in relation to the subfilaments within the thick filaments of scallop striated muscle. J Muscle Res Cell Motil 13(2): 174-182.
    • (1992) J Muscle Res Cell Motil , vol.13 , Issue.2 , pp. 174-182
    • Castellani, L.1    Vibert, P.2
  • 30
    • 0018328198 scopus 로고
    • Structure of the backbone in myosin filaments of muscle
    • Wray JS (1979) Structure of the backbone in myosin filaments of muscle. Nature 277(5691): 37-40.
    • (1979) Nature , vol.277 , Issue.5691 , pp. 37-40
    • Wray, J.S.1
  • 31
    • 0016680461 scopus 로고
    • Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom
    • Lehman W, Szent-Györgyi AG (1975) Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom. J Gen Physiol 66(1): 1-30.
    • (1975) J Gen Physiol , vol.66 , Issue.1 , pp. 1-30
    • Lehman, W.1    Szent-Györgyi, A.G.2
  • 32
    • 0035896017 scopus 로고    scopus 로고
    • Calcium-dependent structural changes in scallop heavy meromyosin
    • Stafford WF, et al. (2001) Calcium-dependent structural changes in scallop heavy meromyosin. J Mol Biol 307(1): 137-147.
    • (2001) J Mol Biol , vol.307 , Issue.1 , pp. 137-147
    • Stafford, W.F.1
  • 33
    • 0042827941 scopus 로고    scopus 로고
    • Evaluation of the symmetric model for myosin-linked regulation: Effect of site-directed mutations in the regulatory light chain on scallop myosin
    • Colegrave M, Patel H, Offer G, Chantler PD (2003) Evaluation of the symmetric model for myosin-linked regulation: Effect of site-directed mutations in the regulatory light chain on scallop myosin. Biochem J 374(Pt 1): 89-96.
    • (2003) Biochem J , vol.374 , Issue.PART 1 , pp. 89-96
    • Colegrave, M.1    Patel, H.2    Offer, G.3    Chantler, P.D.4
  • 34
    • 63949085530 scopus 로고    scopus 로고
    • The 7-stranded structure of relaxed scallop muscle myosin filaments: Support for a common head configuration in myosinregulated muscles
    • AL-Khayat HA, Morris EP, Squire JM (2009) The 7-stranded structure of relaxed scallop muscle myosin filaments: Support for a common head configuration in myosinregulated muscles. J Struct Biol 166(2): 183-194.
    • (2009) J Struct Biol , vol.166 , Issue.2 , pp. 183-194
    • Al-Khayat, H.A.1    Morris, E.P.2    Squire, J.M.3
  • 35
    • 0025811993 scopus 로고
    • On the relationship between distance information derived from cross-linking and from resonance energy transfer, with specific reference to sites located on myosin heads
    • Chantler PD, Tao T, Stafford WF, 3rd (1991) On the relationship between distance information derived from cross-linking and from resonance energy transfer, with specific reference to sites located on myosin heads. Biophys J 59(6): 1242-1250.
    • (1991) Biophys J , vol.59 , Issue.6 , pp. 1242-1250
    • Chantler, P.D.1    Tao, T.2    Stafford Iii, W.F.3
  • 36
    • 0026644741 scopus 로고
    • Regulatory light-chain Cys-55 sites on the two heads of myosin can come within 2Å of each other
    • Bower SM, Wang Y, Chantler PD (1992) Regulatory light-chain Cys-55 sites on the two heads of myosin can come within 2Å of each other. FEBS Lett 310(2): 132-134.
    • (1992) FEBS Lett , vol.310 , Issue.2 , pp. 132-134
    • Bower, S.M.1    Wang, Y.2    Chantler, P.D.3
  • 37
    • 0041343065 scopus 로고    scopus 로고
    • Ionic interactions play a role in the regulatory mechanism of scallop heavy meromyosin
    • Nyitrai M, Stafford WF, Szent-Györgyi AG, Geeves MA (2003) Ionic interactions play a role in the regulatory mechanism of scallop heavy meromyosin. Biophys J 85(2): 1053-1062.
    • (2003) Biophys J , vol.85 , Issue.2 , pp. 1053-1062
    • Nyitrai, M.1    Stafford, W.F.2    Szent-Györgyi, A.G.3    Geeves, M.A.4
  • 38
    • 0042808434 scopus 로고    scopus 로고
    • Visualization of an unstable coiled coil from the scallop myosin rod
    • Li Y, et al. (2003) Visualization of an unstable coiled coil from the scallop myosin rod. Nature 424(6946): 341-345.
    • (2003) Nature , vol.424 , Issue.6946 , pp. 341-345
    • Li, Y.1
  • 39
    • 10044234207 scopus 로고    scopus 로고
    • The requirement for mechanical coupling between head and S2 domains in smooth muscle myosin ATPase regulation and its implications for dimeric motor function
    • Tama F, Feig M, Liu J, Brooks CL, 3rd, Taylor KA (2005) The requirement for mechanical coupling between head and S2 domains in smooth muscle myosin ATPase regulation and its implications for dimeric motor function. J Mol Biol 345(4): 837-854.
    • (2005) J Mol Biol , vol.345 , Issue.4 , pp. 837-854
    • Tama, F.1    Feig, M.2    Liu, J.3    Brooks Iii, C.L.4    Taylor, K.A.5
  • 40
    • 33845230991 scopus 로고    scopus 로고
    • Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment
    • Blankenfeldt W, Thomä NH, Wray JS, Gautel M, Schlichting I (2006) Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment. Proc Natl Acad Sci USA 103(47): 17713-17717.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.47 , pp. 17713-17717
    • Blankenfeldt, W.1    Thomä, N.H.2    Wray, J.S.3    Gautel, M.4    Schlichting, I.5
  • 41
    • 76249092553 scopus 로고    scopus 로고
    • Myosin ATP turnover rate is a mechanism involved in thermogenesis in resting skeletal muscle fibers
    • Stewart MA, Franks-Skiba K, Chen S, Cooke R (2010) Myosin ATP turnover rate is a mechanism involved in thermogenesis in resting skeletal muscle fibers. Proc Natl Acad Sci USA 107(1): 430-435.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.1 , pp. 430-435
    • Stewart, M.A.1    Franks-Skiba, K.2    Chen, S.3    Cooke, R.4
  • 43
    • 81055155880 scopus 로고    scopus 로고
    • A molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filaments
    • Brito R, et al. (2011) A molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filaments. J Mol Biol 414(1): 44-61.
    • (2011) J Mol Biol , vol.414 , Issue.1 , pp. 44-61
    • Brito, R.1
  • 44
    • 0019731755 scopus 로고
    • Mechanics and energetics of contraction in striated muscle of the sea scallop, Placopecten magellanicus
    • Rall JA (1981) Mechanics and energetics of contraction in striated muscle of the sea scallop, Placopecten magellanicus. J Physiol 321: 287-295.
    • (1981) J Physiol , vol.321 , pp. 287-295
    • Rall, J.A.1
  • 45
    • 47049110051 scopus 로고    scopus 로고
    • Millisecond time-resolved changes occurring in Ca2+-regulated myosin filaments upon relaxation
    • Zhao FQ, Craig R (2008) Millisecond time-resolved changes occurring in Ca2+-regulated myosin filaments upon relaxation. J Mol Biol 381(2): 256-260.
    • (2008) J Mol Biol , vol.381 , Issue.2 , pp. 256-260
    • Zhao, F.Q.1    Craig, R.2
  • 46
    • 0017672926 scopus 로고
    • Assembly of smooth muscle myosin into side-polar filaments
    • Craig R, Megerman J (1977) Assembly of smooth muscle myosin into side-polar filaments. J Cell Biol 75(3): 990-996.
    • (1977) J Cell Biol , vol.75 , Issue.3 , pp. 990-996
    • Craig, R.1    Megerman, J.2
  • 47
    • 0029987687 scopus 로고    scopus 로고
    • Myosin filament structure in vertebrate smooth muscle
    • Xu JQ, Harder BA, Uman P, Craig R (1996) Myosin filament structure in vertebrate smooth muscle. J Cell Biol 134(1): 53-66.
    • (1996) J Cell Biol , vol.134 , Issue.1 , pp. 53-66
    • Xu, J.Q.1    Harder, B.A.2    Uman, P.3    Craig, R.4
  • 48
    • 0019326536 scopus 로고
    • Hybrid formation between scallop myofibrils and foreign regulatory light-chains
    • Sellers JR, Chantler PD, Szent-Györgyi AG (1980) Hybrid formation between scallop myofibrils and foreign regulatory light-chains. J Mol Biol 144(3): 223-245.
    • (1980) J Mol Biol , vol.144 , Issue.3 , pp. 223-245
    • Sellers, J.R.1    Chantler, P.D.2    Szent-Györgyi, A.G.3
  • 49
    • 0015833973 scopus 로고
    • General model of myosin filament structure. 3. Molecular packing arrangements in myosin filaments
    • Squire JM (1973) General model of myosin filament structure. 3. Molecular packing arrangements in myosin filaments. J Mol Biol 77(2): 291-323.
    • (1973) J Mol Biol , vol.77 , Issue.2 , pp. 291-323
    • Squire, J.M.1
  • 50
    • 0037053416 scopus 로고    scopus 로고
    • Mass determination of native smooth muscle myosin filaments by scanning transmission electron microscopy
    • Tonino P, Simon M, Craig R (2002) Mass determination of native smooth muscle myosin filaments by scanning transmission electron microscopy. J Mol Biol 318(4): 999-1007.
    • (2002) J Mol Biol , vol.318 , Issue.4 , pp. 999-1007
    • Tonino, P.1    Simon, M.2    Craig, R.3
  • 51
    • 84863655007 scopus 로고    scopus 로고
    • Independent evolution of striated muscles in cnidarians and bilaterians
    • Steinmetz PR, et al. (2012) Independent evolution of striated muscles in cnidarians and bilaterians. Nature 487(7406): 231-234.
    • (2012) Nature , vol.487 , Issue.7406 , pp. 231-234
    • Steinmetz, P.R.1
  • 52
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, et al. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116(1): 190-199.
    • (1996) J Struct Biol , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1
  • 53
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem 25(13): 1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.