메뉴 건너뛰기




Volumn 18, Issue 1, 2006, Pages 68-73

Walking with myosin V

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; MOLECULAR MOTOR; MYOSIN HEAVY CHAIN; MYOSIN V;

EID: 30844455998     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2005.12.014     Document Type: Review
Times cited : (122)

References (45)
  • 2
    • 0037023745 scopus 로고    scopus 로고
    • Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport
    • M. Fukuda, T.S. Kuroda, and K. Mikoshiba Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport J Biol Chem 277 2002 12432 12436
    • (2002) J Biol Chem , vol.277 , pp. 12432-12436
    • Fukuda, M.1    Kuroda, T.S.2    Mikoshiba, K.3
  • 3
    • 0036107354 scopus 로고    scopus 로고
    • Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes
    • D.W. Provance, T.L. James, and J.A. Mercer Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes Traffic 3 2002 124 132
    • (2002) Traffic , vol.3 , pp. 124-132
    • Provance, D.W.1    James, T.L.2    Mercer, J.A.3
  • 9
    • 22244474260 scopus 로고    scopus 로고
    • Force-dependent stepping kinetics of myosin-V
    • A.E. Clemen, M. Vilfan, J. Jaud, J. Zhang, M. Barmann, and M. Rief Force-dependent stepping kinetics of myosin-V Biophys J 88 2005 4402 4410 Superstall forces result in backward stepping by myosin V.
    • (2005) Biophys J , vol.88 , pp. 4402-4410
    • Clemen, A.E.1    Vilfan, M.2    Jaud, J.3    Zhang, J.4    Barmann, M.5    Rief, M.6
  • 12
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • A. Yildiz, J.N. Forkey, S.A. McKinney, T. Ha, Y.E. Goldman, and P.R. Selvin Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization Science 300 2003 2061 2065
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 13
    • 28944449570 scopus 로고    scopus 로고
    • Step-size is determined by neck length in myosin V
    • T. Sakamoto, A. Yildiz, P.R. Selvin, and J.R. Sellers Step-size is determined by neck length in myosin V Biochemistry 44 2005 16203 16210 This study demonstrated that stepsize was proportional to neck length using myoV mutants.
    • (2005) Biochemistry , vol.44 , pp. 16203-16210
    • Sakamoto, T.1    Yildiz, A.2    Selvin, P.R.3    Sellers, J.R.4
  • 14
    • 4444384544 scopus 로고    scopus 로고
    • Nanometer localization of single green fluorescent proteins: Evidence that myosin V walks hand-over-hand via telemark configuration
    • G.E. Snyder, T. Sakamoto, J.A. Hammer III, J.R. Sellers, and P.R. Selvin Nanometer localization of single green fluorescent proteins: evidence that myosin V walks hand-over-hand via telemark configuration Biophys J 87 2004 1776 1783
    • (2004) Biophys J , vol.87 , pp. 1776-1783
    • Snyder, G.E.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Selvin, P.R.5
  • 15
    • 17844385071 scopus 로고    scopus 로고
    • Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity
    • D.M. Warshaw, G.G. Kennedy, S.S. Work, E.B. Krementsova, S. Beck, and K.M. Trybus Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity Biophys J 88 2005 L30 L32 This study uses FIONA with each myosin head labeled with a different color quantum dot to show that the heads move in an alternating hand-over-hand manner, while maintaining a 36-nm separation.
    • (2005) Biophys J , vol.88
    • Warshaw, D.M.1    Kennedy, G.G.2    Work, S.S.3    Krementsova, E.B.4    Beck, S.5    Trybus, K.M.6
  • 16
    • 13444292841 scopus 로고    scopus 로고
    • Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time
    • L.S. Churchman, Z. Okten, R.S. Rock, J.F. Dawson, and J.A. Spudich Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time Proc Natl Acad Sci USA 102 2005 1419 1423 This study uses myoV molecules with heads that were differentially labeled with Cy3 and Cy5-labeled calmodulin molecules to show that the heads move in an alternating hand-over-hand manner, while maintaining a 36 nm separation.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1419-1423
    • Churchman, L.S.1    Okten, Z.2    Rock, R.S.3    Dawson, J.F.4    Spudich, J.A.5
  • 19
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • C. Veigel, S. Schmitz, F. Wang, and J.R. Sellers Load-dependent kinetics of myosin-V can explain its high processivity Nat Cell Biol 7 2005 861 869 Using a method to rapidly detect myoV attachment to actin, a range of loads was exerted on single myoV heads. Both positive and negative loads affect the kinetics of the working stroke, produced in substeps.
    • (2005) Nat Cell Biol , vol.7 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 21
    • 0035969240 scopus 로고    scopus 로고
    • Myosin V exhibits a high duty cycle and large unitary displacement
    • J.R. Moore, E.B. Krementsova, K.M. Trybus, and D.M. Warshaw Myosin V exhibits a high duty cycle and large unitary displacement J Cell Biol 155 2001 625 635
    • (2001) J Cell Biol , vol.155 , pp. 625-635
    • Moore, J.R.1    Krementsova, E.B.2    Trybus, K.M.3    Warshaw, D.M.4
  • 22
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin V structures delineate essential features of chemo-mechanical transduction
    • P.D. Coureux, H.L. Sweeney, and A. Houdusse Three myosin V structures delineate essential features of chemo-mechanical transduction EMBO J 23 2004 4527 4537 Structural evidence for different myosin V structures is deduced from three different crystal forms.
    • (2004) EMBO J , vol.23 , pp. 4527-4537
    • Coureux, P.D.1    Sweeney, H.L.2    Houdusse, A.3
  • 23
    • 20544475925 scopus 로고    scopus 로고
    • Magnesium, ADP, and actin binding linkage of myosin V: Evidence for multiple myosin V-ADP and actomyosin V-ADP states
    • D.E. Hannemann, W. Cao, A.O. Olivares, J.P. Robblee, and E.M. De La Cruz Magnesium, ADP, and actin binding linkage of myosin V: evidence for multiple myosin V-ADP and actomyosin V-ADP states Biochemistry 44 2005 8826 8840
    • (2005) Biochemistry , vol.44 , pp. 8826-8840
    • Hannemann, D.E.1    Cao, W.2    Olivares, A.O.3    Robblee, J.P.4    De La Cruz, E.M.5
  • 24
    • 14044268874 scopus 로고    scopus 로고
    • Magnesium regulates ADP dissociation from myosin V
    • S.S. Rosenfeld, A. Houdusse, and H.L. Sweeney Magnesium regulates ADP dissociation from myosin V J Biol Chem 280 2005 6072 6079
    • (2005) J Biol Chem , vol.280 , pp. 6072-6079
    • Rosenfeld, S.S.1    Houdusse, A.2    Sweeney, H.L.3
  • 27
    • 1542267772 scopus 로고    scopus 로고
    • Functional role of loop 2 in myosin V
    • C.M. Yengo, and H.L. Sweeney Functional role of loop 2 in myosin V Biochemistry 43 2004 2605 2612
    • (2004) Biochemistry , vol.43 , pp. 2605-2612
    • Yengo, C.M.1    Sweeney, H.L.2
  • 28
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization
    • J.N. Forkey, M.E. Quinlan, M.A. Shaw, J.E. Corrie, and Y.E. Goldman Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization Nature 422 2003 399 404
    • (2003) Nature , vol.422 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.4    Goldman, Y.E.5
  • 29
    • 30844464706 scopus 로고    scopus 로고
    • An elastically tethered viscous load imposes a regular gait on the motion of myosin V. Simulations of the effect of transient force relaxation on a stochastic process
    • in press.
    • Schilstra MJ, Martin SR: An elastically tethered viscous load imposes a regular gait on the motion of myosin V. Simulations of the effect of transient force relaxation on a stochastic process. J Roy Soc Interface 2005, in press. A mathematical model is proposed where portions of myoV constitute an elastic tether to absorb abrupt mechanical transitions of the motor during movement of cargo in a crowded cytoplasm.
    • (2005) J Roy Soc Interface
    • Schilstra, M.J.1    Martin, S.R.2
  • 31
    • 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 Positive and negative strain in the presence of differing ATP concentrations is applied to probe the mechanics of a single myoV head.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13873-13878
    • Purcell, T.J.1    Sweeney, H.L.2    Spudich, J.A.3
  • 32
    • 1842681965 scopus 로고    scopus 로고
    • Myosin V processivity: Multiple kinetic pathways for head-to-head coordination
    • J.E. Baker, E.B. Krementsova, G.G. Kennedy, A. Armstrong, K.M. Trybus, and D.M. Warshaw Myosin V processivity: multiple kinetic pathways for head-to-head coordination Proc Natl Acad Sci USA 101 2004 5542 5546 Velocity and run length of single fluorescently labelled myoV molecules are measured at differing ATP and ADP concentrations. A kinetic model was developed to explain myoV processivity.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5542-5546
    • Baker, J.E.1    Krementsova, E.B.2    Kennedy, G.G.3    Armstrong, A.4    Trybus, K.M.5    Warshaw, D.M.6
  • 34
    • 4544232738 scopus 로고    scopus 로고
    • A model of myosin V processivity
    • S.S. Rosenfeld, and H.L. Sweeney A model of myosin V processivity J Biol Chem 279 2004 40100 40111 Solution kinetics of two-headed myoV bound to actin reveal strain-dependent ADP release.
    • (2004) J Biol Chem , vol.279 , pp. 40100-40111
    • Rosenfeld, S.S.1    Sweeney, H.L.2
  • 35
    • 24044451511 scopus 로고    scopus 로고
    • The structural basis of Myosin v processive movement as revealed by electron cryomicroscopy
    • N. Volkmann, H. Liu, L. Hazelwood, E.B. Krementsova, S. Lowey, K.M. Trybus, and D. Hanein The structural basis of Myosin v processive movement as revealed by electron cryomicroscopy Mol Cell 19 2005 595 605 Three-dimensional reconstructions of myoV bound to actin in various nucleotide states are presented, including a weakly bound form.
    • (2005) Mol Cell , vol.19 , pp. 595-605
    • Volkmann, N.1    Liu, H.2    Hazelwood, L.3    Krementsova, E.B.4    Lowey, S.5    Trybus, K.M.6    Hanein, D.7
  • 37
  • 39
    • 24044527127 scopus 로고    scopus 로고
    • Myosin V from Drosophila Reveals Diversity of Motor Mechanisms within the Myosin V Family
    • J. Toth, M. Kovacs, F. Wang, L. Nyitray, and J.R. Sellers Myosin V from Drosophila Reveals Diversity of Motor Mechanisms within the Myosin V Family J Biol Chem 280 2005 30594 30603
    • (2005) J Biol Chem , vol.280 , pp. 30594-30603
    • Toth, J.1    Kovacs, M.2    Wang, F.3    Nyitray, L.4    Sellers, J.R.5
  • 40
    • 0035947774 scopus 로고    scopus 로고
    • The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin- based motors
    • S.L. Reck-Peterson, M.J. Tyska, P.J. Novick, and M.S. Mooseker The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin- based motors J Cell Biol 153 2001 1121 1126
    • (2001) J Cell Biol , vol.153 , pp. 1121-1126
    • Reck-Peterson, S.L.1    Tyska, M.J.2    Novick, P.J.3    Mooseker, M.S.4
  • 42
    • 0037342115 scopus 로고    scopus 로고
    • A simple kinetic model describes the processivity of myosin-v
    • A.B. Kolomeisky, and M.E. Fisher A simple kinetic model describes the processivity of myosin-v Biophys J 84 2003 1642 1650
    • (2003) Biophys J , vol.84 , pp. 1642-1650
    • Kolomeisky, A.B.1    Fisher, M.E.2
  • 43
    • 22244472947 scopus 로고    scopus 로고
    • Elastic lever-arm model for myosin V
    • A. Vilfan Elastic lever-arm model for myosin V Biophys J 88 2005 3792 3805
    • (2005) Biophys J , vol.88 , pp. 3792-3805
    • Vilfan, A.1
  • 44
    • 21244502885 scopus 로고    scopus 로고
    • Dynamics of myosin-V processivity
    • G. Lan, and S.X. Sun Dynamics of myosin-V processivity Biophys J 88 2005 999 1008
    • (2005) Biophys J , vol.88 , pp. 999-1008
    • Lan, G.1    Sun, S.X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.