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Volumn 99, Issue 5, 2010, Pages 1546-1555

The influence of myosin converter and relay domains on cross-bridge kinetics of Drosophila indirect flight muscle

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EID: 77956578914     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.06.047     Document Type: Article
Times cited : (16)

References (45)
  • 1
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment, I., H. M. Holden., R. A. Milligan. 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    Holden, H.M.2    Milligan, R.A.3
  • 2
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • Dominguez, R., Y. Freyzon., C. Cohen. 1998. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell. 94:559-571.
    • (1998) Cell. , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Cohen, C.3
  • 3
    • 0034711237 scopus 로고    scopus 로고
    • The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever
    • Warshaw, D. M., W. H. Guilford., K. M. Trybus. 2000. The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever. J. Biol. Chem. 275:37167-37172.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37167-37172
    • Warshaw, D.M.1    Guilford, W.H.2    Trybus, K.M.3
  • 4
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever-arm hypothesis of muscle contraction
    • Holmes, K. C. 1997. The swinging lever-arm hypothesis of muscle contraction. Curr. Biol. 7: R112-R118.
    • (1997) Curr. Biol. , vol.7
    • Holmes, K.C.1
  • 5
    • 17844400134 scopus 로고    scopus 로고
    • Structural mechanism of the recovery stroke in the myosin molecular motor
    • Fischer, S., B. Windshügel., J. C. Smith. 2005. Structural mechanism of the recovery stroke in the myosin molecular motor. Proc. Natl. Acad. Sci. USA. 102:6873-6878.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6873-6878
    • Fischer, S.1    Windshügel, B.2    Smith, J.C.3
  • 7
    • 33847769745 scopus 로고    scopus 로고
    • Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin
    • Kad, N. M., J. B. Patlak., D. M. Warshaw. 2007. Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin. Biophys. J. 92:1623-1631.
    • (2007) Biophys. J. , vol.92 , pp. 1623-1631
    • Kad, N.M.1    Patlak, J.B.2    Warshaw, D.M.3
  • 8
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • Veigel, C., J. E. Molloy., J. Kendrick-Jones. 2003. Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers. Nat. Cell Biol. 5:980-986.
    • (2003) Nat. Cell. Biol. , vol.5 , pp. 980-986
    • Veigel, C.1    Molloy, J.E.2    Kendrick-Jones, J.3
  • 9
    • 0029113048 scopus 로고
    • Strain-dependent cross-bridge cycle for muscle
    • Smith, D. A., and M. A. Geeves. 1995. Strain-dependent cross-bridge cycle for muscle. Biophys. J. 69:524-537.
    • (1995) Biophys. J. , vol.69 , pp. 524-537
    • Smith, D.A.1    Geeves, M.A.2
  • 10
    • 21544444439 scopus 로고    scopus 로고
    • Molecular mechanism of actomyosin-based motility
    • Geeves, M. A., R. Fedorov, and D. J. Manstein. 2005. Molecular mechanism of actomyosin-based motility. Cell. Mol. Life Sci. 62:1462-1477.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1462-1477
    • Geeves, M.A.1    Fedorov, R.2    Manstein, D.J.3
  • 11
    • 26844566272 scopus 로고    scopus 로고
    • The molecular mechanism of muscle contraction
    • Geeves, M. A., and K. C. Holmes. 2005. The molecular mechanism of muscle contraction. Adv. Protein Chem. 71:161-193.
    • (2005) Adv. Protein Chem. , vol.71 , pp. 161-193
    • Geeves, M.A.1    Holmes, K.C.2
  • 12
    • 0037133680 scopus 로고    scopus 로고
    • Mutation of the myosin converter domain alters cross-bridge elasticity
    • Köhler, J., G. Winkler., T. Kraft. 2002. Mutation of the myosin converter domain alters cross-bridge elasticity. Proc. Natl. Acad. Sci. USA. 99:3557-3562.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3557-3562
    • Köhler, J.1    Winkler, G.2    Kraft, T.3
  • 13
    • 68849085387 scopus 로고    scopus 로고
    • Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance
    • Seebohm, B., F. Matinmehr., T. Kraft. 2009. Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance. Biophys. J. 97:806-824.
    • (2009) Biophys. J. , vol.97 , pp. 806-824
    • Seebohm, B.1    Matinmehr, F.2    Kraft, T.3
  • 14
    • 0024366590 scopus 로고
    • Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons
    • George, E. L., M. B. Ober, and C. P. Emerson, Jr. 1989. Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons. Mol. Cell. Biol. 9:2957-2974
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2957-2974
    • George, E.L.1    Ober, M.B.2    Emerson Jr., C.P.3
  • 15
    • 85031341097 scopus 로고
    • published erratum appears in, Sep
    • (published erratum appears in Mol. Cell. Biol. 1989 Sep; 9 (9):4118).
    • (1989) Mol. Cell. Biol. , vol.9 , Issue.9 , pp. 4118
  • 16
    • 0020678384 scopus 로고
    • Drosophila muscle myosin heavy chain encoded by a single gene in a cluster of muscle mutations
    • Bernstein, S. I., K. Mogami., C. P. Emerson, Jr. 1983. Drosophila muscle myosin heavy chain encoded by a single gene in a cluster of muscle mutations. Nature. 302:393-397.
    • (1983) Nature , vol.302 , pp. 393-397
    • Bernstein, S.I.1    Mogami, K.2    Emerson Jr., C.P.3
  • 17
    • 0036222885 scopus 로고    scopus 로고
    • The myosin converter domain modulates muscle performance
    • Swank, D. M., A. F. Knowles., S. I. Bernstein. 2002. The myosin converter domain modulates muscle performance. Nat. Cell Biol. 4:312-316.
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 312-316
    • Swank, D.M.1    Knowles, A.F.2    Bernstein, S.I.3
  • 18
    • 33646196389 scopus 로고    scopus 로고
    • An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics
    • Swank, D. M., J. Braddock., D. W. Maughan. 2006. An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics. Biophys. J. 90:2427-2435.
    • (2006) Biophys. J. , vol.90 , pp. 2427-2435
    • Swank, D.M.1    Braddock, J.2    Maughan, D.W.3
  • 19
    • 4444288620 scopus 로고    scopus 로고
    • Alternative N-terminal regions of Drosophila myosin heavy chain tune muscle kinetics for optimal power output
    • Swank, D. M., W. A. Kronert., D. W. Maughan. 2004. Alternative N-terminal regions of Drosophila myosin heavy chain tune muscle kinetics for optimal power output. Biophys. J. 87:1805-1814.
    • (2004) Biophys. J. , vol.87 , pp. 1805-1814
    • Swank, D.M.1    Kronert, W.A.2    Maughan, D.W.3
  • 20
    • 58149356271 scopus 로고    scopus 로고
    • Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics
    • Yang, C., S. Ramanath., D. M. Swank. 2008. Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics. Biophys. J. 95:5228-5237.
    • (2008) Biophys. J. , vol.95 , pp. 5228-5237
    • Yang, C.1    Ramanath, S.2    Swank, D.M.3
  • 22
    • 0033454349 scopus 로고    scopus 로고
    • An integrated view of insect flight muscle: Genes, motor molecules, and motion
    • Maughan, D. W., and J. O. Vigoreaux. 1999. An integrated view of insect flight muscle: genes, motor molecules, and motion. News Physiol. Sci. 14:87-92.
    • (1999) News Physiol. Sci. , vol.14 , pp. 87-92
    • Maughan, D.W.1    Vigoreaux, J.O.2
  • 23
    • 0346118918 scopus 로고    scopus 로고
    • Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling
    • Miller, B. M., M. Nyitrai., M. A. Geeves. 2003. Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling. J. Biol. Chem. 278:50293-50300.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50293-50300
    • Miller, B.M.1    Nyitrai, M.2    Geeves, M.A.3
  • 24
    • 43449134103 scopus 로고    scopus 로고
    • Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function
    • Kronert, W. A., C. M. Dambacher., S. I. Bernstein. 2008. Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function. J. Mol. Biol. 379:443-456.
    • (2008) J. Mol. Biol. , vol.379 , pp. 443-456
    • Kronert, W.A.1    Dambacher, C.M.2    Bernstein, S.I.3
  • 25
    • 0019308296 scopus 로고
    • Sinusoidal analysis: A high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish
    • Kawai, M., and P. W. Brandt. 1980. Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish. J. Muscle Res. Cell Motil. 1:279-303.
    • (1980) J. Muscle Res. Cell. Motil , vol.1 , pp. 279-303
    • Kawai, M.1    Brandt, P.W.2
  • 26
    • 33751251988 scopus 로고    scopus 로고
    • An exceptionally fast actomyosin reaction powers insect flight muscle
    • Swank, D. M., V. K. Vishnudas, and D. W. Maughan. 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
  • 27
    • 77956564362 scopus 로고
    • Elementary steps of contraction probed by sinusoidal analysis technique in rabbit psoas fibers
    • H. Sugi and G. J. Pollack, editors. Plenum Press, New York
    • Kawai, M., Y. Zhao, and H. R. Halvorson. 1992. Elementary steps of contraction probed by sinusoidal analysis technique in rabbit psoas fibers. In Mechanisms of myofilament sliding in muscle contraction. H. Sugi and G. J. Pollack, editors. Plenum Press, New York.
    • (1992) Mechanisms of Myofilament Sliding in Muscle Contraction
    • Kawai, M.1    Zhao, Y.2    Halvorson, H.R.3
  • 28
    • 28944440487 scopus 로고    scopus 로고
    • What limits the velocity of fast-skeletal muscle contraction in mammals?
    • Nyitrai, M., R. Rossi., M. A. Geeves. 2006. What limits the velocity of fast-skeletal muscle contraction in mammals? J. Mol. Biol. 355:432-442.
    • (2006) J. Mol. Biol. , vol.355 , pp. 432-442
    • Nyitrai, M.1    Rossi, R.2    Geeves, M.A.3
  • 29
    • 0034665602 scopus 로고    scopus 로고
    • Determining structure/function relationships for sarcomeric myosin heavy chain by genetic and transgenic manipulation of Drosophila
    • Swank, D. M., L. Wells., S. I. Bernstein. 2000. Determining structure/function relationships for sarcomeric myosin heavy chain by genetic and transgenic manipulation of Drosophila. Microsc. Res. Tech. 50:430-442.
    • (2000) Microsc. Res. Tech. , vol.50 , pp. 430-442
    • Swank, D.M.1    Wells, L.2    Bernstein, S.I.3
  • 30
    • 0019974315 scopus 로고
    • Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog
    • Godt, R. E., and B. D. Lindley. 1982. Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog. J. Gen. Physiol. 80:279-297.
    • (1982) J. Gen. Physiol. , vol.80 , pp. 279-297
    • Godt, R.E.1    Lindley, B.D.2
  • 31
    • 0030779404 scopus 로고    scopus 로고
    • Phosphorylation-dependent power output of transgenic flies: An integrated study
    • Dickinson, M. H., C. J. Hyatt., D. W. Maughan. 1997. Phosphorylation- dependent power output of transgenic flies: an integrated study. Biophys. J. 73:3122-3134.
    • (1997) Biophys. J. , vol.73 , pp. 3122-3134
    • Dickinson, M.H.1    Hyatt, C.J.2    Maughan, D.W.3
  • 32
    • 0037059561 scopus 로고    scopus 로고
    • Alterations of myocardial dynamic stiffness implicating abnormal crossbridge function in human mitral regurgitation heart failure
    • Mulieri, L. A., W. Barnes., D. W. Maughan. 2002. Alterations of myocardial dynamic stiffness implicating abnormal crossbridge function in human mitral regurgitation heart failure. Circ. Res. 90:66-72.
    • (2002) Circ. Res. , vol.90 , pp. 66-72
    • Mulieri, L.A.1    Barnes, W.2    Maughan, D.W.3
  • 33
    • 0011460619 scopus 로고
    • Correlation between exponential processes and crossbridge kinetics
    • Approach. B. M. Twarog, R. J. C. Levine, and M. M. Dewey, editors. Raven Press, New York
    • Kawai, M. 1982. Correlation between exponential processes and crossbridge kinetics. In Basic Biology of Muscles: A Comparative Approach. B. M. Twarog, R. J. C. Levine, and M. M. Dewey, editors. Raven Press, New York.
    • (1982) Basic Biology of Muscles: A Comparative
    • Kawai, M.1
  • 34
    • 27744571222 scopus 로고    scopus 로고
    • Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles
    • Galler, S., B. G. Wang, and M. Kawai. 2005. Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles. Biophys. J. 89:3248-3260.
    • (2005) Biophys. J. , vol.89 , pp. 3248-3260
    • Galler, S.1    Wang, B.G.2    Kawai, M.3
  • 35
    • 0035119730 scopus 로고    scopus 로고
    • Spatially and temporally regulated expression of myosin heavy chain alternative exons during Drosophila embryogenesis
    • Zhang, S., and S. I. Bernstein. 2001. Spatially and temporally regulated expression of myosin heavy chain alternative exons during Drosophila embryogenesis. Mech. Dev. 101:35-45.
    • (2001) Mech. Dev. , vol.101 , pp. 35-45
    • Zhang, S.1    Bernstein, S.I.2
  • 36
    • 0035824536 scopus 로고    scopus 로고
    • Differing ADP release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers
    • Weiss, S., R. Rossi., M. A. Geeves. 2001. Differing ADP release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers. J. Biol. Chem. 276:45902-45908.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45902-45908
    • Weiss, S.1    Rossi, R.2    Geeves, M.A.3
  • 37
    • 0036156643 scopus 로고    scopus 로고
    • Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins
    • Fujita, H., D. Sasaki., M. Kawai. 2002. Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins. Biophys. J. 82:915-928.
    • (2002) Biophys. J. , vol.82 , pp. 915-928
    • Fujita, H.1    Sasaki, D.2    Kawai, M.3
  • 38
    • 34547650842 scopus 로고    scopus 로고
    • Two-state model of acto-myosin attachment-detachment predicts C-process of sinusoidal analysis
    • Palmer, B. M., T. Suzuki., D. W. Maughan. 2007. Two-state model of acto-myosin attachment-detachment predicts C-process of sinusoidal analysis. Biophys. J. 93:760-769.
    • (2007) Biophys. J. , vol.93 , pp. 760-769
    • Palmer, B.M.1    Suzuki, T.2    Maughan, D.W.3
  • 39
    • 34547129596 scopus 로고    scopus 로고
    • Selective perturbation of the myosin recovery stroke by point mutations at the base of the lever arm affects ATP hydrolysis and phosphate release
    • Málnási-Csizmadia, A., J. Tóth., M. Kovács. 2007. Selective perturbation of the myosin recovery stroke by point mutations at the base of the lever arm affects ATP hydrolysis and phosphate release. J. Biol. Chem. 282:17658-17664.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17658-17664
    • Málnási-Csizmadia, A.1    Tóth, J.2    Kovács, M.3
  • 40
    • 0024392532 scopus 로고
    • Addition of phosphate to active muscle fibers probes actomyosin states within the powerstroke
    • Pate, E., and R. Cooke. 1989. Addition of phosphate to active muscle fibers probes actomyosin states within the powerstroke. Pflugers Arch. 414:73-81.
    • (1989) Pflugers Arch. , vol.414 , pp. 73-81
    • Pate, E.1    Cooke, R.2
  • 41
    • 65849096732 scopus 로고    scopus 로고
    • Alternative exon 9-encoded relay domains affect more than one communication pathway in the Drosophila myosin head
    • Bloemink, M. J., C. M. Dambacher., S. I. Bernstein. 2009. Alternative exon 9-encoded relay domains affect more than one communication pathway in the Drosophila myosin head. J. Mol. Biol. 389:707-721.
    • (2009) J. Mol. Biol. , vol.389 , pp. 707-721
    • Bloemink, M.J.1    Dambacher, C.M.2    Bernstein, S.I.3
  • 42
    • 33847181200 scopus 로고    scopus 로고
    • The principal motions involved in the coupling mechanism of the recovery stroke of the myosin motor
    • Mesentean, S., S. Koppole., S. Fischer. 2007. The principal motions involved in the coupling mechanism of the recovery stroke of the myosin motor. J. Mol. Biol. 367:591-602.
    • (2007) J. Mol. Biol. , vol.367 , pp. 591-602
    • Mesentean, S.1    Koppole, S.2    Fischer, S.3
  • 43
    • 0035379648 scopus 로고    scopus 로고
    • The myosin relay helix to converter interface remains intact throughout the actomyosin ATPase cycle
    • Shih, W. M., and J. A. Spudich. 2001. The myosin relay helix to converter interface remains intact throughout the actomyosin ATPase cycle. J. Biol. Chem. 276:19491-19494.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19491-19494
    • Shih, W.M.1    Spudich, J.A.2
  • 44
    • 0037435594 scopus 로고    scopus 로고
    • Dictyostelium myosin II mutations that uncouple the converter swing and ATP hydrolysis cycle
    • Sasaki, N., R. Ohkura, and K. Sutoh. 2003. Dictyostelium myosin II mutations that uncouple the converter swing and ATP hydrolysis cycle. Biochemistry. 42:90-95.
    • (2003) Biochemistry , vol.42 , pp. 90-95
    • Sasaki, N.1    Ohkura, R.2    Sutoh, K.3
  • 45
    • 0031559585 scopus 로고    scopus 로고
    • Fine tuning a molecular motor: The location of alternative domains in the Drosophila myosin head
    • Bernstein, S. I., and R. A. Milligan. 1997. Fine tuning a molecular motor: the location of alternative domains in the Drosophila myosin head. J. Mol. Biol. 271:1-6.
    • (1997) J. Mol. Biol. , vol.271 , pp. 1-6
    • Bernstein, S.I.1    Milligan, R.A.2


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