메뉴 건너뛰기




Volumn 105, Issue 6, 2013, Pages 1466-1474

The kinetics of mechanically coupled myosins exhibit group size-dependent regimes

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MYOSIN;

EID: 84884307405     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.07.054     Document Type: Article
Times cited : (28)

References (50)
  • 1
    • 0036218298 scopus 로고    scopus 로고
    • The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules
    • J.E. Baker, and C. Brosseau D.M. Warshaw The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules Biophys. J. 82 2002 2134 2147
    • (2002) Biophys. J. , vol.82 , pp. 2134-2147
    • Baker, J.E.1    Brosseau, C.2    Warshaw, D.M.3
  • 2
    • 0041707669 scopus 로고    scopus 로고
    • The unique properties of tonic smooth muscle emerge from intrinsic as well as intermolecular behaviors of myosin molecules
    • J.E. Baker, and C. Brosseau D.M. Warshaw The unique properties of tonic smooth muscle emerge from intrinsic as well as intermolecular behaviors of myosin molecules J. Biol. Chem. 278 2003 28533 28539
    • (2003) J. Biol. Chem. , vol.278 , pp. 28533-28539
    • Baker, J.E.1    Brosseau, C.2    Warshaw, D.M.3
  • 3
    • 68849121787 scopus 로고    scopus 로고
    • The energetics of allosteric regulation of ADP release from myosin heads
    • D.R. Jackson Jr., and J.E. Baker The energetics of allosteric regulation of ADP release from myosin heads Phys. Chem. Chem. Phys. 11 2009 4808 4814
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 4808-4814
    • Jackson Jr., D.R.1    Baker, J.E.2
  • 4
    • 84864691712 scopus 로고    scopus 로고
    • Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements
    • S. Walcott, D.M. Warshaw, and E.P. Debold Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements Biophys. J. 103 2012 501 510
    • (2012) Biophys. J. , vol.103 , pp. 501-510
    • Walcott, S.1    Warshaw, D.M.2    Debold, E.P.3
  • 5
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • A.F. Huxley, and R.M. Simmons Proposed mechanism of force generation in striated muscle Nature 233 1971 533 538
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 6
    • 0018877621 scopus 로고
    • Cross-bridge model of muscle contraction. Quantitative analysis
    • E. Eisenberg, T.L. Hill, and Y. Chen Cross-bridge model of muscle contraction. Quantitative analysis Biophys. J. 29 1980 195 227
    • (1980) Biophys. J. , vol.29 , pp. 195-227
    • Eisenberg, E.1    Hill, T.L.2    Chen, Y.3
  • 7
    • 30444437723 scopus 로고    scopus 로고
    • Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin
    • M. Capitanio, and M. Canepari R. Bottinelli Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin Proc. Natl. Acad. Sci. USA 103 2006 87 92
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 87-92
    • Capitanio, M.1    Canepari, M.2    Bottinelli, R.3
  • 8
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • C. Veigel, and J.E. Molloy J. Kendrick-Jones Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers Nat. Cell Biol. 5 2003 980 986
    • (2003) Nat. Cell Biol. , vol.5 , pp. 980-986
    • Veigel, C.1    Molloy, J.E.2    Kendrick-Jones, J.3
  • 9
    • 33847769745 scopus 로고    scopus 로고
    • Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin
    • N.M. Kad, and J.B. Patlak D.M. Warshaw Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin Biophys. J. 92 2007 1623 1631
    • (2007) Biophys. J. , vol.92 , pp. 1623-1631
    • Kad, N.M.1    Patlak, J.B.2    Warshaw, D.M.3
  • 10
    • 13444263735 scopus 로고    scopus 로고
    • Adenosine diphosphate and strain sensitivity in myosin motors
    • M. Nyitrai, and M. Geeves Adenosine diphosphate and strain sensitivity in myosin motors Philos. Trans. Roy. Soc. B. Biol. Sci 359 2004 1867 1877
    • (2004) Philos. Trans. Roy. Soc. B. Biol. Sci , vol.359 , pp. 1867-1877
    • Nyitrai, M.1    Geeves, M.2
  • 11
    • 84855381766 scopus 로고    scopus 로고
    • Pre-power-stroke cross-bridges contribute to force transients during imposed shortening in isolated muscle fibers
    • F.C. Minozzo, L. Hilbert, and D.E. Rassier Pre-power-stroke cross-bridges contribute to force transients during imposed shortening in isolated muscle fibers PLoS ONE 7 2012 e29356
    • (2012) PLoS ONE , vol.7 , pp. 29356
    • Minozzo, F.C.1    Hilbert, L.2    Rassier, D.E.3
  • 12
    • 75749090448 scopus 로고    scopus 로고
    • Coordination and collective properties of molecular motors: Theory
    • T. Guérin, and J. Prost J.-F. Joanny Coordination and collective properties of molecular motors: theory Curr. Opin. Cell Biol. 22 2010 14 20
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 14-20
    • Guérin, T.1    Prost, J.2    Joanny, J.-F.3
  • 13
    • 0037076389 scopus 로고    scopus 로고
    • Push or pull? Teams of motor proteins have it both ways
    • T. Duke Push or pull? Teams of motor proteins have it both ways Proc. Natl. Acad. Sci. USA 99 2002 6521 6523
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6521-6523
    • Duke, T.1
  • 14
    • 0033052976 scopus 로고    scopus 로고
    • Molecular model of muscle contraction
    • T.A. Duke Molecular model of muscle contraction Proc. Natl. Acad. Sci. USA 96 1999 2770 2775
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2770-2775
    • Duke, T.A.1
  • 15
    • 0034728963 scopus 로고    scopus 로고
    • Cooperativity of myosin molecules through strain-dependent chemistry
    • T. Duke Cooperativity of myosin molecules through strain-dependent chemistry Philos. Trans. Roy. Soc. B. Biol. Sci. 355 2000 529 538
    • (2000) Philos. Trans. Roy. Soc. B. Biol. Sci. , vol.355 , pp. 529-538
    • Duke, T.1
  • 16
    • 0042344863 scopus 로고    scopus 로고
    • Instabilities in the transient response of muscle
    • A. Vilfan, and T. Duke Instabilities in the transient response of muscle Biophys. J. 85 2003 818 827
    • (2003) Biophys. J. , vol.85 , pp. 818-827
    • Vilfan, A.1    Duke, T.2
  • 17
    • 0031826028 scopus 로고    scopus 로고
    • Acting on actin: The electric motility assay
    • D. Riveline, and A. Ott J. Prost Acting on actin: the electric motility assay Eur. Biophys. J. 27 1998 403 408
    • (1998) Eur. Biophys. J. , vol.27 , pp. 403-408
    • Riveline, D.1    Ott, A.2    Prost, J.3
  • 18
    • 70349857816 scopus 로고    scopus 로고
    • Spontaneous oscillations of a minimal actomyosin system under elastic loading
    • P.Y. Plaçais, and M. Balland P. Martin Spontaneous oscillations of a minimal actomyosin system under elastic loading Phys. Rev. Lett. 103 2009 158102
    • (2009) Phys. Rev. Lett. , vol.103 , pp. 158102
    • Plaçais, P.Y.1    Balland, M.2    Martin, P.3
  • 19
    • 1842681965 scopus 로고    scopus 로고
    • Myosin v processivity: Multiple kinetic pathways for head-to-head coordination
    • J.E. Baker, and E.B. Krementsova D.M. Warshaw Myosin V processivity: multiple kinetic pathways for head-to-head coordination Proc. Natl. Acad. Sci. USA 101 2004 5542 5546
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5542-5546
    • Baker, J.E.1    Krementsova, E.B.2    Warshaw, D.M.3
  • 20
    • 25444437003 scopus 로고    scopus 로고
    • A force-dependent state controls the coordination of processive myosin v
    • T.J. Purcell, H.L. Sweeney, and J.A. Spudich A force-dependent state controls the coordination of processive myosin V Proc. Natl. Acad. Sci. USA 102 2005 13873 13878
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13873-13878
    • Purcell, T.J.1    Sweeney, H.L.2    Spudich, J.A.3
  • 21
    • 70849119718 scopus 로고    scopus 로고
    • Mechanochemical model for myosin v
    • E.M. Craig, and H. Linke Mechanochemical model for myosin V Proc. Natl. Acad. Sci. USA 106 2009 18261 18266
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18261-18266
    • Craig, E.M.1    Linke, H.2
  • 22
    • 78650651853 scopus 로고    scopus 로고
    • Simultaneous observation of tail and head movements of myosin v during processive motion
    • H. Lu, and G.G. Kennedy K.M. Trybus Simultaneous observation of tail and head movements of myosin V during processive motion J. Biol. Chem. 285 2010 42068 42074
    • (2010) J. Biol. Chem. , vol.285 , pp. 42068-42074
    • Lu, H.1    Kennedy, G.G.2    Trybus, K.M.3
  • 23
    • 0028280745 scopus 로고
    • Smooth, cardiac and skeletal muscle myosin force and motion generation assessed by cross-bridge mechanical interactions in vitro
    • D.E. Harris, and S.S. Work D.M. Warshaw Smooth, cardiac and skeletal muscle myosin force and motion generation assessed by cross-bridge mechanical interactions in vitro J. Muscle Res. Cell Motil. 15 1994 11 19
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 11-19
    • Harris, D.E.1    Work, S.S.2    Warshaw, D.M.3
  • 24
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • D.M. Warshaw, and J.M. Desrosiers K.M. Trybus Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro J. Cell Biol. 111 1990 453 463
    • (1990) J. Cell Biol. , vol.111 , pp. 453-463
    • Warshaw, D.M.1    Desrosiers, J.M.2    Trybus, K.M.3
  • 27
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • J.D. Pardee, and J.A. Spudich Purification of muscle actin Methods Enzymol. 85 Pt B 1982 164 181
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 28
    • 53449089110 scopus 로고    scopus 로고
    • Affinity for MgADP and force of unbinding from actin of myosin purified from tonic and phasic smooth muscle
    • R. Léguillette, and N.B. Zitouni A.-M. Lauzon Affinity for MgADP and force of unbinding from actin of myosin purified from tonic and phasic smooth muscle Am. J. Physiol. Cell Physiol. 295 2008 C653 C660
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Léguillette, R.1    Zitouni, N.B.2    Lauzon, A.-M.3
  • 29
    • 0026642621 scopus 로고
    • Computer-assisted tracking of actin filament motility
    • S.S. Work, and D.M. Warshaw Computer-assisted tracking of actin filament motility Anal. Biochem. 202 1992 275 285
    • (1992) Anal. Biochem. , vol.202 , pp. 275-285
    • Work, S.S.1    Warshaw, D.M.2
  • 30
    • 0028080839 scopus 로고
    • Calmodulin-sensitive interactions of human nebulin fragments with actin and myosin
    • D. Root, and K. Wang Calmodulin-sensitive interactions of human nebulin fragments with actin and myosin Biochemistry 33 1994 12581 12591
    • (1994) Biochemistry , vol.33 , pp. 12581-12591
    • Root, D.1    Wang, K.2
  • 31
    • 84872187948 scopus 로고    scopus 로고
    • Measuring collective transport by defined numbers of processive and nonprocessive kinesin motors
    • K. Furuta, and A. Furuta H. Kojima Measuring collective transport by defined numbers of processive and nonprocessive kinesin motors Proc. Natl. Acad. Sci. USA 110 2013 501 506
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 501-506
    • Furuta, K.1    Furuta, A.2    Kojima, H.3
  • 32
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • T.Q. Uyeda, S.J. Kron, and J.A. Spudich Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin J. Mol. Biol. 214 1990 699 710
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.1    Kron, S.J.2    Spudich, J.A.3
  • 33
    • 0027272935 scopus 로고
    • Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
    • D.E. Harris, and D.M. Warshaw Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro J. Biol. Chem. 268 1993 14764 14768
    • (1993) J. Biol. Chem. , vol.268 , pp. 14764-14768
    • Harris, D.E.1    Warshaw, D.M.2
  • 34
    • 77955289401 scopus 로고    scopus 로고
    • Nonlinear elasticity and an 8-nm working stroke of single myosin molecules in myofilaments
    • M. Kaya, and H. Higuchi Nonlinear elasticity and an 8-nm working stroke of single myosin molecules in myofilaments Science 329 2010 686 689
    • (2010) Science , vol.329 , pp. 686-689
    • Kaya, M.1    Higuchi, H.2
  • 35
    • 69249172101 scopus 로고    scopus 로고
    • Drug effect unveils inter-head cooperativity and strain-dependent ADP release in fast skeletal actomyosin
    • N. Albet-Torres, and M.J. Bloemink A. Månsson Drug effect unveils inter-head cooperativity and strain-dependent ADP release in fast skeletal actomyosin J. Biol. Chem. 284 2009 22926 22937
    • (2009) J. Biol. Chem. , vol.284 , pp. 22926-22937
    • Albet-Torres, N.1    Bloemink, M.J.2    Månsson, A.3
  • 36
    • 0142187316 scopus 로고    scopus 로고
    • Random walks with thin filaments: Application of in vitro motility assay to the study of actomyosin regulation
    • S. Marston Random walks with thin filaments: application of in vitro motility assay to the study of actomyosin regulation J. Muscle Res. Cell Motil. 24 2003 149 156
    • (2003) J. Muscle Res. Cell Motil. , vol.24 , pp. 149-156
    • Marston, S.1
  • 37
    • 0029118276 scopus 로고
    • In vitro motility analysis of smooth muscle caldesmon control of actin-tropomyosin filament movement
    • I.D. Fraser, and S.B. Marston In vitro motility analysis of smooth muscle caldesmon control of actin-tropomyosin filament movement J. Biol. Chem. 270 1995 19688 19693
    • (1995) J. Biol. Chem. , vol.270 , pp. 19688-19693
    • Fraser, I.D.1    Marston, S.B.2
  • 38
    • 0028953460 scopus 로고
    • In vitro motility analysis of actin-tropomyosin regulation by troponin and calcium. The thin filament is switched as a single cooperative unit
    • I.D. Fraser, and S.B. Marston In vitro motility analysis of actin-tropomyosin regulation by troponin and calcium. The thin filament is switched as a single cooperative unit J. Biol. Chem. 270 1995 7836 7841
    • (1995) J. Biol. Chem. , vol.270 , pp. 7836-7841
    • Fraser, I.D.1    Marston, S.B.2
  • 39
    • 0030721473 scopus 로고    scopus 로고
    • 2+-dependent effects on actin-tropomyosin filament motility
    • 2+-dependent effects on actin-tropomyosin filament motility Biochem. J. 327 1997 335 340
    • (1997) Biochem. J. , vol.327 , pp. 335-340
    • Bing, W.1    Fraser, I.D.2    Marston, S.B.3
  • 40
    • 80052447606 scopus 로고    scopus 로고
    • Productive cooperation among processive motors depends inversely on their mechanochemical efficiency
    • J.W. Driver, and D.K. Jamison M.R. Diehl Productive cooperation among processive motors depends inversely on their mechanochemical efficiency Biophys. J. 101 2011 386 395
    • (2011) Biophys. J. , vol.101 , pp. 386-395
    • Driver, J.W.1    Jamison, D.K.2    Diehl, M.R.3
  • 41
    • 55549137369 scopus 로고    scopus 로고
    • Processive kinesins require loose mechanical coupling for efficient collective motility
    • P. Bieling, and I.A. Telley T. Surrey Processive kinesins require loose mechanical coupling for efficient collective motility EMBO Rep. 9 2008 1121 1127
    • (2008) EMBO Rep. , vol.9 , pp. 1121-1127
    • Bieling, P.1    Telley, I.A.2    Surrey, T.3
  • 42
    • 79953285218 scopus 로고    scopus 로고
    • Directional switching of the kinesin Cin8 through motor coupling
    • J. Roostalu, and C. Hentrich T. Surrey Directional switching of the kinesin Cin8 through motor coupling Science 332 2011 94 99
    • (2011) Science , vol.332 , pp. 94-99
    • Roostalu, J.1    Hentrich, C.2    Surrey, T.3
  • 43
    • 74149089077 scopus 로고    scopus 로고
    • Cooperative behavior of molecular motors: Cargo transport and traffic phenomena
    • R. Lipowsky, and J. Beeg M. Müller Cooperative behavior of molecular motors: Cargo transport and traffic phenomena Physica E 42 2010 649 661
    • (2010) Physica E , vol.42 , pp. 649-661
    • Lipowsky, R.1    Beeg, J.2    Müller, M.3
  • 44
    • 28444447392 scopus 로고    scopus 로고
    • Cooperative cargo transport by several molecular motors
    • S. Klumpp, and R. Lipowsky Cooperative cargo transport by several molecular motors Proc. Natl. Acad. Sci. USA 102 2005 17284 17289
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17284-17289
    • Klumpp, S.1    Lipowsky, R.2
  • 45
    • 38349030871 scopus 로고    scopus 로고
    • Transport of beads by several kinesin motors
    • J. Beeg, and S. Klumpp R. Lipowsky Transport of beads by several kinesin motors Biophys. J. 94 2008 532 541
    • (2008) Biophys. J. , vol.94 , pp. 532-541
    • Beeg, J.1    Klumpp, S.2    Lipowsky, R.3
  • 46
    • 84873350504 scopus 로고    scopus 로고
    • Bifurcation of velocity distributions in cooperative transport of filaments by fast and slow motors
    • X. Li, R. Lipowsky, and J. Kierfeld Bifurcation of velocity distributions in cooperative transport of filaments by fast and slow motors Biophys. J. 104 2013 666 676
    • (2013) Biophys. J. , vol.104 , pp. 666-676
    • Li, X.1    Lipowsky, R.2    Kierfeld, J.3
  • 47
    • 27744553633 scopus 로고    scopus 로고
    • Slip sliding away: Load-dependence of velocity generated by skeletal muscle myosin molecules in the laser trap
    • E.P. Debold, J.B. Patlak, and D.M. Warshaw Slip sliding away: load-dependence of velocity generated by skeletal muscle myosin molecules in the laser trap Biophys. J. 89 2005 L34 L36
    • (2005) Biophys. J. , vol.89
    • Debold, E.P.1    Patlak, J.B.2    Warshaw, D.M.3
  • 49
    • 84865168921 scopus 로고    scopus 로고
    • Critical motor number for fractional steps of cytoskeletal filaments in gliding assays
    • X. Li, R. Lipowsky, and J. Kierfeld Critical motor number for fractional steps of cytoskeletal filaments in gliding assays PLoS ONE 7 2012 e43219
    • (2012) PLoS ONE , vol.7 , pp. 43219
    • Li, X.1    Lipowsky, R.2    Kierfeld, J.3
  • 50
    • 0002643986 scopus 로고
    • The dip test of unimodality
    • J. Hartigan, and P. Hartigan The dip test of unimodality Ann. Stat. 13 1985 70 84
    • (1985) Ann. Stat. , vol.13 , pp. 70-84
    • Hartigan, J.1    Hartigan, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.