메뉴 건너뛰기




Volumn 105, Issue 10, 2013, Pages 2374-2384

Direct observation of phosphate inhibiting the Force-generating capacity of a miniensemble of myosin molecules

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MYOSIN; PHOSPHATE;

EID: 84887970247     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.09.046     Document Type: Article
Times cited : (54)

References (53)
  • 1
    • 0022405269 scopus 로고
    • The effects of ADP and phosphate on the contraction of muscle fibers
    • R. Cooke, and E. Pate The effects of ADP and phosphate on the contraction of muscle fibers Biophys. J. 48 1985 789 798
    • (1985) Biophys. J. , vol.48 , pp. 789-798
    • Cooke, R.1    Pate, E.2
  • 2
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres
    • J.A. Dantzig, and Y.E. Goldman E. Homsher Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres J. Physiol. 451 1992 247 278
    • (1992) J. Physiol. , vol.451 , pp. 247-278
    • Dantzig, J.A.1    Goldman, Y.E.2    Homsher, E.3
  • 3
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • M.G. Hibberd, and J.A. Dantzig Y.E. Goldman Phosphate release and force generation in skeletal muscle fibers Science 228 1985 1317 1319
    • (1985) Science , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Goldman, Y.E.3
  • 5
    • 13444280378 scopus 로고    scopus 로고
    • Coupling between phosphate release and force generation in muscle actomyosin
    • Y. Takagi, H. Shuman, and Y.E. Goldman Coupling between phosphate release and force generation in muscle actomyosin Philos. Trans. R. Soc. Lond. B Biol. Sci. 359 2004 1913 1920
    • (2004) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.359 , pp. 1913-1920
    • Takagi, Y.1    Shuman, H.2    Goldman, Y.E.3
  • 7
    • 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
  • 8
    • 0021964341 scopus 로고
    • Oxygen exchange between phosphate and water accompanies calcium-regulated ATPase activity of skinned fibers from rabbit skeletal muscle
    • M.G. Hibberd, and M.R. Webb D.R. Trentham Oxygen exchange between phosphate and water accompanies calcium-regulated ATPase activity of skinned fibers from rabbit skeletal muscle J. Biol. Chem. 260 1985 3496 3500
    • (1985) J. Biol. Chem. , vol.260 , pp. 3496-3500
    • Hibberd, M.G.1    Webb, M.R.2    Trentham, D.R.3
  • 9
    • 0026073088 scopus 로고
    • Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle
    • M. Kawai, and H.R. Halvorson Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle Biophys. J. 59 1991 329 342
    • (1991) Biophys. J. , vol.59 , pp. 329-342
    • Kawai, M.1    Halvorson, H.R.2
  • 10
    • 0034084354 scopus 로고    scopus 로고
    • The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle
    • C. Tesi, and F. Colomo C. Poggesi The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle Biophys. J. 78 2000 3081 3092
    • (2000) Biophys. J. , vol.78 , pp. 3081-3092
    • Tesi, C.1    Colomo, F.2    Poggesi, C.3
  • 11
    • 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
  • 12
    • 33644795090 scopus 로고    scopus 로고
    • The molecular basis of cross-bridge function
    • discussion 23, 359-369
    • K.C. Holmes The molecular basis of cross-bridge function Adv. Exp. Med. Biol. 565 2005 13 22 discussion 23, 359-369
    • (2005) Adv. Exp. Med. Biol. , vol.565 , pp. 13-22
    • Holmes, K.C.1
  • 13
    • 0024392532 scopus 로고
    • Addition of phosphate to active muscle fibers probes actomyosin states within the powerstroke
    • E. Pate, and R. Cooke Addition of phosphate to active muscle fibers probes actomyosin states within the powerstroke Pflugers Arch. 414 1989 73 81
    • (1989) Pflugers Arch. , vol.414 , pp. 73-81
    • Pate, E.1    Cooke, R.2
  • 14
    • 42949118930 scopus 로고    scopus 로고
    • Inorganic phosphate binds to the empty nucleotide binding pocket of conventional myosin II
    • M. Amrute-Nayak, and M. Antognozzi B. Brenner Inorganic phosphate binds to the empty nucleotide binding pocket of conventional myosin II J. Biol. Chem. 283 2008 3773 3781
    • (2008) J. Biol. Chem. , vol.283 , pp. 3773-3781
    • Amrute-Nayak, M.1    Antognozzi, M.2    Brenner, B.3
  • 15
    • 79958801934 scopus 로고    scopus 로고
    • Phosphate enhances myosin-powered actin filament velocity under acidic conditions in a motility assay
    • E.P. Debold, and M.A. Turner S. Walcott Phosphate enhances myosin-powered actin filament velocity under acidic conditions in a motility assay Am. J. Physiol. Regul. Integr. Comp. Physiol. 300 2011 R1401 R1408
    • (2011) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.300
    • Debold, E.P.1    Turner, M.A.2    Walcott, S.3
  • 16
    • 33947388779 scopus 로고    scopus 로고
    • An accelerated state of myosin-based actin motility
    • A.M. Hooft, and E.J. Maki J.E. Baker An accelerated state of myosin-based actin motility Biochemistry 46 2007 3513 3520
    • (2007) Biochemistry , vol.46 , pp. 3513-3520
    • Hooft, A.M.1    Maki, E.J.2    Baker, J.E.3
  • 17
    • 84875224119 scopus 로고    scopus 로고
    • Actin sliding velocities are influenced by the driving forces of actin-myosin binding
    • T.J. Stewart, and D.R. Jackson Jr. J.E. Baker Actin sliding velocities are influenced by the driving forces of actin-myosin binding Cell. Mol. Bioeng. 6 2013 26 37
    • (2013) Cell. Mol. Bioeng. , vol.6 , pp. 26-37
    • Stewart, T.J.1    Jackson, Jr.D.R.2    Baker, J.E.3
  • 18
    • 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
    • R. Dominguez, and Y. Freyzon C. Cohen 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 1998 559 571
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Cohen, C.3
  • 19
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • I. Rayment, and W.R. Rypniewski H.M. Holden Three-dimensional structure of myosin subfragment-1: a molecular motor Science 261 1993 50 58
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1    Rypniewski, W.R.2    Holden, H.M.3
  • 20
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • M.A. Geeves, and K.C. Holmes Structural mechanism of muscle contraction Annu. Rev. Biochem. 68 1999 687 728
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 21
    • 0029159959 scopus 로고
    • X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4
    • A.J. Fisher, and C.A. Smith I. Rayment X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4- Biochemistry 34 1995 8960 8972
    • (1995) Biochemistry , vol.34 , pp. 8960-8972
    • Fisher, A.J.1    Smith, C.A.2    Rayment, I.3
  • 22
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • J.T. Finer, R.M. Simmons, and J.A. Spudich Single myosin molecule mechanics: piconewton forces and nanometre steps Nature 368 1994 113 119
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 23
    • 33645758327 scopus 로고    scopus 로고
    • Force generation in single conventional actomyosin complexes under high dynamic load
    • Y. Takagi, and E.E. Homsher H. Shuman Force generation in single conventional actomyosin complexes under high dynamic load Biophys. J. 90 2006 1295 1307
    • (2006) Biophys. J. , vol.90 , pp. 1295-1307
    • Takagi, Y.1    Homsher, E.E.2    Shuman, H.3
  • 24
    • 0023783575 scopus 로고
    • Demembranated muscle fibers catalyze a more rapid exchange between phosphate and adenosine triphosphate than actomyosin subfragment 1
    • R. Bowater, and J. Sleep Demembranated muscle fibers catalyze a more rapid exchange between phosphate and adenosine triphosphate than actomyosin subfragment 1 Biochemistry 27 1988 5314 5323
    • (1988) Biochemistry , vol.27 , pp. 5314-5323
    • Bowater, R.1    Sleep, J.2
  • 25
    • 0028789904 scopus 로고
    • Influence of inorganic phosphate and pH on ATP utilization in fast and slow skeletal muscle fibers
    • E.J. Potma, I.A. van Graas, and G.J. Stienen Influence of inorganic phosphate and pH on ATP utilization in fast and slow skeletal muscle fibers Biophys. J. 69 1995 2580 2589
    • (1995) Biophys. J. , vol.69 , pp. 2580-2589
    • Potma, E.J.1    Van Graas, I.A.2    Stienen, G.J.3
  • 26
    • 58749110524 scopus 로고    scopus 로고
    • Effect of inorganic phosphate on the force and number of myosin cross-bridges during the isometric contraction of permeabilized muscle fibers from rabbit psoas
    • M. Caremani, and J. Dantzig M. Linari Effect of inorganic phosphate on the force and number of myosin cross-bridges during the isometric contraction of permeabilized muscle fibers from rabbit psoas Biophys. J. 95 2008 5798 5808
    • (2008) Biophys. J. , vol.95 , pp. 5798-5808
    • Caremani, M.1    Dantzig, J.2    Linari, M.3
  • 27
    • 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
    • M. Linari, M. Caremani, and V. Lombardi 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 2010 19 27
    • (2010) Proc. Biol. Sci. , vol.277 , pp. 19-27
    • Linari, M.1    Caremani, M.2    Lombardi, V.3
  • 28
    • 33847680889 scopus 로고    scopus 로고
    • Dynamics of the unbound head during myosin v processive translocation
    • A.R. Dunn, and J.A. Spudich Dynamics of the unbound head during myosin V processive translocation Nat. Struct. Mol. Biol. 14 2007 246 248
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 246-248
    • Dunn, A.R.1    Spudich, J.A.2
  • 29
    • 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
  • 30
    • 1642317185 scopus 로고    scopus 로고
    • Some precautions in using chelators to buffer metals in biological solutions
    • C. Patton, S. Thompson, and D. Epel Some precautions in using chelators to buffer metals in biological solutions Cell Calcium 35 2004 427 431
    • (2004) Cell Calcium , vol.35 , pp. 427-431
    • Patton, C.1    Thompson, S.2    Epel, D.3
  • 31
    • 0041731921 scopus 로고    scopus 로고
    • A mutant heterodimeric myosin with one inactive head generates maximal displacement
    • N.M. Kad, and A.S. Rovner K.M. Trybus A mutant heterodimeric myosin with one inactive head generates maximal displacement J. Cell Biol. 162 2003 481 488
    • (2003) J. Cell Biol. , vol.162 , pp. 481-488
    • Kad, N.M.1    Rovner, A.S.2    Trybus, K.M.3
  • 32
    • 0031604170 scopus 로고    scopus 로고
    • Versatile optical traps with feedback control
    • K. Visscher, and S.M. Block Versatile optical traps with feedback control Methods Enzymol. 298 1998 460 489
    • (1998) Methods Enzymol. , vol.298 , pp. 460-489
    • Visscher, K.1    Block, S.M.2
  • 34
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • K. Svoboda, and S.M. Block Force and velocity measured for single kinesin molecules Cell 77 1994 773 784
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 35
    • 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
  • 36
    • 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
  • 37
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • G.I. Bell Models for the specific adhesion of cells to cells Science 200 1978 618 627
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 38
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • S.B. Marston, and E.W. Taylor Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles J. Mol. Biol. 139 1980 573 600
    • (1980) J. Mol. Biol. , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, E.W.2
  • 39
    • 52749093471 scopus 로고    scopus 로고
    • Effect of low pH on single skeletal muscle myosin mechanics and kinetics
    • E.P. Debold, S.E. Beck, and D.M. Warshaw Effect of low pH on single skeletal muscle myosin mechanics and kinetics Am. J. Physiol. Cell Physiol. 295 2008 C173 C179
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Debold, E.P.1    Beck, S.E.2    Warshaw, D.M.3
  • 40
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • R.W. Lymn, and E.W. Taylor Mechanism of adenosine triphosphate hydrolysis by actomyosin Biochemistry 10 1971 4617 4624
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 41
    • 4444242939 scopus 로고    scopus 로고
    • Repriming the actomyosin crossbridge cycle
    • W. Steffen, and J. Sleep Repriming the actomyosin crossbridge cycle Proc. Natl. Acad. Sci. USA 101 2004 12904 12909
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12904-12909
    • Steffen, W.1    Sleep, J.2
  • 42
    • 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
  • 43
    • 33645429016 scopus 로고
    • Exact stochastic simulation of coupled chemical reactions
    • D.T. Gillespie Exact stochastic simulation of coupled chemical reactions J. Phys. Chem. 81 1977 2340 2361
    • (1977) J. Phys. Chem. , vol.81 , pp. 2340-2361
    • Gillespie, D.T.1
  • 44
    • 0031656226 scopus 로고    scopus 로고
    • The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer
    • C. Veigel, and M.L. Bartoo J.E. Molloy The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer Biophys. J. 75 1998 1424 1438
    • (1998) Biophys. J. , vol.75 , pp. 1424-1438
    • Veigel, C.1    Bartoo, M.L.2    Molloy, J.E.3
  • 46
    • 0031041817 scopus 로고    scopus 로고
    • Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap
    • W.H. Guilford, and D.E. Dupuis D.M. Warshaw Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap Biophys. J. 72 1997 1006 1021
    • (1997) Biophys. J. , vol.72 , pp. 1006-1021
    • Guilford, W.H.1    Dupuis, D.E.2    Warshaw, D.M.3
  • 47
    • 0033551045 scopus 로고    scopus 로고
    • Two heads of myosin are better than one for generating force and motion
    • M.J. Tyska, and D.E. Dupuis S. Lowey Two heads of myosin are better than one for generating force and motion Proc. Natl. Acad. Sci. USA 96 1999 4402 4407
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4402-4407
    • Tyska, M.J.1    Dupuis, D.E.2    Lowey, S.3
  • 49
    • 84868332179 scopus 로고    scopus 로고
    • The effects of phosphate and acidosis on regulated thin-filament velocity in an in vitro motility assay
    • E.P. Debold, T.J. Longyear, and M.A. Turner The effects of phosphate and acidosis on regulated thin-filament velocity in an in vitro motility assay J. Appl. Physiol. 113 2012 1413 1422
    • (2012) J. Appl. Physiol. , vol.113 , pp. 1413-1422
    • Debold, E.P.1    Longyear, T.J.2    Turner, M.A.3
  • 50
    • 78649329189 scopus 로고    scopus 로고
    • Emerging complex pathways of the actomyosin powerstroke
    • A. Málnási-Csizmadia, and M. Kovács Emerging complex pathways of the actomyosin powerstroke Trends Biochem. Sci. 35 2010 684 690
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 684-690
    • Málnási-Csizmadia, A.1    Kovács, M.2
  • 51
    • 84862822844 scopus 로고    scopus 로고
    • A novel actin binding site of myosin required for effective muscle contraction
    • B.H. Várkuti, and Z. Yang A. Málnási-Csizmadia A novel actin binding site of myosin required for effective muscle contraction Nat. Struct. Mol. Biol. 19 2012 299 306
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 299-306
    • Várkuti, B.H.1    Yang, Z.2    Málnási-Csizmadia, A.3
  • 52
    • 47749142424 scopus 로고    scopus 로고
    • i control flux through the branched kinetic cycle of myosin v
    • i control flux through the branched kinetic cycle of myosin V J. Biol. Chem. 283 2008 17477 17484
    • (2008) J. Biol. Chem. , vol.283 , pp. 17477-17484
    • Kad, N.M.1    Trybus, K.M.2    Warshaw, D.M.3
  • 53
    • 0019003415 scopus 로고
    • Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1
    • J.A. Sleep, and R.L. Hutton Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1 Biochemistry 19 1980 1276 1283
    • (1980) Biochemistry , vol.19 , pp. 1276-1283
    • Sleep, J.A.1    Hutton, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.