메뉴 건너뛰기




Volumn 110, Issue 43, 2013, Pages

Design principles governing the motility of myosin v

Author keywords

Architectural basis; Functional robustness; Polymer physics; Stall force expression

Indexed keywords

MYOSIN V;

EID: 84886427888     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1312393110     Document Type: Article
Times cited : (40)

References (55)
  • 1
    • 75149128079 scopus 로고    scopus 로고
    • Myosin VI: An innovative motor that challenged the swinging lever arm hypothesis
    • Spudich JA, Sivaramakrishnan S (2010) Myosin VI: An innovative motor that challenged the swinging lever arm hypothesis. Nat Rev Mol Cell Biol 11(2):128-137.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.2 , pp. 128-137
    • Spudich, J.A.1    Sivaramakrishnan, S.2
  • 3
    • 79955506649 scopus 로고    scopus 로고
    • Direct observation of the myosin Va recovery stroke that contributes to unidirectional stepping along actin
    • Shiroguchi K, et al. (2011) Direct observation of the myosin Va recovery stroke that contributes to unidirectional stepping along actin. PLoS Biol 9(4):e1001031.
    • (2011) PLoS Biol , vol.9 , Issue.4
    • Shiroguchi, K.1
  • 4
    • 0033527043 scopus 로고    scopus 로고
    • Myosin-V is a processive actin-based motor
    • Mehta AD, et al. (1999) Myosin-V is a processive actin-based motor. Nature 400(6744): 590-593.
    • (1999) Nature , vol.400 , Issue.6744 , pp. 590-593
    • Mehta, A.D.1
  • 5
    • 0034662912 scopus 로고    scopus 로고
    • Myosin-V stepping kinetics: A molecular model for processivity
    • Rief M, et al. (2000) Myosin-V stepping kinetics: A molecular model for processivity. Proc Natl Acad Sci USA 97(17):9482-9486.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.17 , pp. 9482-9486
    • Rief, M.1
  • 6
    • 0034616649 scopus 로고    scopus 로고
    • Direct observation of processive movement by individual myosin v molecules
    • Sakamoto T, Amitani I, Yokota E, Ando T (2000) Direct observation of processive movement by individual myosin V molecules. Biochem Biophys Res Commun 272(2): 586-590.
    • (2000) Biochem Biophys Res Commun , vol.272 , Issue.2 , pp. 586-590
    • Sakamoto, T.1    Amitani, I.2    Yokota, E.3    Ando, T.4
  • 7
    • 0037832404 scopus 로고    scopus 로고
    • Myosin v walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • Yildiz A, et al. (2003) Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization. Science 300(5628):2061-2065.
    • (2003) Science , vol.300 , Issue.5628 , pp. 2061-2065
    • Yildiz, A.1
  • 8
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin v by single-molecule fluorescence polarization
    • Forkey JN, Quinlan ME, Shaw MA, Corrie JET, Goldman YE (2003) Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization. Nature 422(6930):399-404.
    • (2003) Nature , vol.422 , Issue.6930 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.T.4    Goldman, Y.E.5
  • 9
    • 51349088578 scopus 로고    scopus 로고
    • Direct observation of the mechanochemical coupling in myosin Va during processive movement
    • Sakamoto T, Webb MR, Forgacs E, White HD, Sellers JR (2008) Direct observation of the mechanochemical coupling in myosin Va during processive movement. Nature 455(7209):128-132.
    • (2008) Nature , vol.455 , Issue.7209 , pp. 128-132
    • Sakamoto, T.1    Webb, M.R.2    Forgacs, E.3    White, H.D.4    Sellers, J.R.5
  • 10
    • 1842681965 scopus 로고    scopus 로고
    • Myosin v processivity: Multiple kinetic pathways for head-tohead coordination
    • Baker JE, et al. (2004) Myosin V processivity: Multiple kinetic pathways for head-tohead coordination. Proc Natl Acad Sci USA 101(15):5542-5546.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.15 , pp. 5542-5546
    • Baker, J.E.1
  • 11
    • 68049143191 scopus 로고    scopus 로고
    • Velocity, processivity, and individual steps of single myosin v molecules in live cells
    • Pierobon P, et al. (2009) Velocity, processivity, and individual steps of single myosin V molecules in live cells. Biophys J 96(10):4268-4275.
    • (2009) Biophys J , vol.96 , Issue.10 , pp. 4268-4275
    • Pierobon, P.1
  • 13
    • 4544232738 scopus 로고    scopus 로고
    • A model of myosin v processivity
    • Rosenfeld SS, Sweeney HL (2004) A model of myosin V processivity. J Biol Chem 279(38):40100-40111.
    • (2004) J Biol Chem , vol.279 , Issue.38 , pp. 40100-40111
    • Rosenfeld, S.S.1    Sweeney, H.L.2
  • 14
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • Veigel C, Schmitz S, Wang F, Sellers JR (2005) Load-dependent kinetics of myosin-V can explain its high processivity. Nat Cell Biol 7(9):861-869.
    • (2005) Nat Cell Biol , vol.7 , Issue.9 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 15
    • 25444437003 scopus 로고    scopus 로고
    • A force-dependent state controls the coordination of processive myosin v
    • Purcell TJ, Sweeney HL, Spudich JA (2005) A force-dependent state controls the coordination of processive myosin V. Proc Natl Acad Sci USA 102(39):13873-13878.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.39 , pp. 13873-13878
    • Purcell, T.J.1    Sweeney, H.L.2    Spudich, J.A.3
  • 16
    • 47749142424 scopus 로고    scopus 로고
    • Load and Pi control flux through the branched kinetic cycle of myosin v
    • Kad NM, Trybus KM, Warshaw DM (2008) Load and Pi control flux through the branched kinetic cycle of myosin V. J Biol Chem 283(25):17477-17484.
    • (2008) J Biol Chem , vol.283 , Issue.25 , pp. 17477-17484
    • Kad, N.M.1    Trybus, K.M.2    Warshaw, D.M.3
  • 19
    • 34848923743 scopus 로고    scopus 로고
    • Myosin v stepping mechanism
    • Cappello G, et al. (2007) Myosin V stepping mechanism. Proc Natl Acad Sci USA 104(39):15328-15333.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.39 , pp. 15328-15333
    • Cappello, G.1
  • 20
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin v by high-speed atomic force microscopy
    • Kodera N, Yamamoto D, Ishikawa R, Ando T (2010) Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 468(7320):72-76.
    • (2010) Nature , vol.468 , Issue.7320 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ishikawa, R.3    Ando, T.4
  • 21
    • 33646568493 scopus 로고    scopus 로고
    • Adaptability of myosin v studied by simultaneous detection of position and orientation
    • Syed S, Snyder GE, Franzini-Armstrong C, Selvin PR, Goldman YE (2006) Adaptability of myosin V studied by simultaneous detection of position and orientation. EMBO J 25(9):1795-1803.
    • (2006) EMBO J , vol.25 , Issue.9 , pp. 1795-1803
    • Syed, S.1    Snyder, G.E.2    Franzini-Armstrong, C.3    Selvin, P.R.4    Goldman, Y.E.5
  • 22
    • 84877083700 scopus 로고    scopus 로고
    • Tilting and wobble of myosin v by high-speed single-molecule polarized fluorescence microscopy
    • Beausang JF, Shroder DY, Nelson PC, Goldman YE (2013) Tilting and wobble of myosin V by high-speed single-molecule polarized fluorescence microscopy. Biophys J 104(6): 1263-1273.
    • (2013) Biophys J , vol.104 , Issue.6 , pp. 1263-1273
    • Beausang, J.F.1    Shroder, D.Y.2    Nelson, P.C.3    Goldman, Y.E.4
  • 23
    • 33847680889 scopus 로고    scopus 로고
    • Dynamics of the unbound head during myosin v processive translocation
    • Dunn AR, Spudich JA (2007) Dynamics of the unbound head during myosin V processive translocation. Nat Struct Mol Biol 14(3):246-248.
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.3 , pp. 246-248
    • Dunn, A.R.1    Spudich, J.A.2
  • 24
    • 34249948276 scopus 로고    scopus 로고
    • Myosin v walks by lever action and Brownian motion
    • Shiroguchi K, Kinosita K, Jr. (2007) Myosin V walks by lever action and Brownian motion. Science 316(5828):1208-1212.
    • (2007) Science , vol.316 , Issue.5828 , pp. 1208-1212
    • Shiroguchi, K.1    Kinosita Jr., K.2
  • 25
    • 34948867142 scopus 로고    scopus 로고
    • Myosin-V makes two brownian 90 degrees rotations per 36-nm step
    • Komori Y, Iwane AH, Yanagida T (2007) Myosin-V makes two brownian 90 degrees rotations per 36-nm step. Nat Struct Mol Biol 14(10):968-973.
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.10 , pp. 968-973
    • Komori, Y.1    Iwane, A.H.2    Yanagida, T.3
  • 26
    • 0030606512 scopus 로고    scopus 로고
    • Is the lever arm of myosin a molecular elastic element?
    • Howard J, Spudich JA (1996) Is the lever arm of myosin a molecular elastic element? Proc Natl Acad Sci USA 93(9):4462-4464.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.9 , pp. 4462-4464
    • Howard, J.1    Spudich, J.A.2
  • 28
    • 22244472947 scopus 로고    scopus 로고
    • Elastic lever-arm model for myosin v
    • Vilfan A (2005) Elastic lever-arm model for myosin V. Biophys J 88(6):3792-3805.
    • (2005) Biophys J , vol.88 , Issue.6 , pp. 3792-3805
    • Vilfan, A.1
  • 29
    • 0037342115 scopus 로고    scopus 로고
    • A simple kinetic model describes the processivity of myosin-v
    • Kolomeisky AB, Fisher ME (2003) A simple kinetic model describes the processivity of myosin-v. Biophys J 84(3):1642-1650.
    • (2003) Biophys J , vol.84 , Issue.3 , pp. 1642-1650
    • Kolomeisky, A.B.1    Fisher, M.E.2
  • 30
    • 21244502885 scopus 로고    scopus 로고
    • Dynamics of myosin-V processivity
    • Lan GH, Sun SX (2005) Dynamics of myosin-V processivity. Biophys J 88(2):999-1008.
    • (2005) Biophys J , vol.88 , Issue.2 , pp. 999-1008
    • Lan, G.H.1    Sun, S.X.2
  • 31
    • 33749435355 scopus 로고    scopus 로고
    • A kinetic model describing the processivity of myosin-V
    • Skau KI, Hoyle RB, Turner MS (2006) A kinetic model describing the processivity of myosin-V. Biophys J 91(7):2475-2489.
    • (2006) Biophys J , vol.91 , Issue.7 , pp. 2475-2489
    • Skau, K.I.1    Hoyle, R.B.2    Turner, M.S.3
  • 32
    • 37749044426 scopus 로고    scopus 로고
    • Mechanoenzymes under superstall and large assisting loads reveal structural features
    • Tsygankov D, Fisher ME (2007) Mechanoenzymes under superstall and large assisting loads reveal structural features. Proc Natl Acad Sci USA 104(49):19321-19326.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.49 , pp. 19321-19326
    • Tsygankov, D.1    Fisher, M.E.2
  • 33
    • 73649091759 scopus 로고    scopus 로고
    • Comprehensive physical mechanism of two-headed biomotor myosin v
    • Xu YZ, Wang ZS (2009) Comprehensive physical mechanism of two-headed biomotor myosin V. J Chem Phys 131(24):245104.
    • (2009) J Chem Phys , vol.131 , Issue.24 , pp. 245104
    • Xu, Y.Z.1    Wang, Z.S.2
  • 34
    • 79959673675 scopus 로고    scopus 로고
    • Chemomechanical coupling and motor cycles of myosin v
    • Bierbaum V, Lipowsky R (2011) Chemomechanical coupling and motor cycles of myosin V. Biophys J 100(7):1747-1755.
    • (2011) Biophys J , vol.100 , Issue.7 , pp. 1747-1755
    • Bierbaum, V.1    Lipowsky, R.2
  • 35
    • 70849119718 scopus 로고    scopus 로고
    • Mechanochemical model for myosin v
    • Craig EM, Linke H (2009) Mechanochemical model for myosin V. Proc Natl Acad Sci USA 106(43):18261-18266.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.43 , pp. 18261-18266
    • Craig, E.M.1    Linke, H.2
  • 36
    • 22244474260 scopus 로고    scopus 로고
    • Force-dependent stepping kinetics of myosin-V
    • Clemen AEM, et al. (2005) Force-dependent stepping kinetics of myosin-V. Biophys J 88(6):4402-4410.
    • (2005) Biophys J , vol.88 , Issue.6 , pp. 4402-4410
    • Clemen, A.E.M.1
  • 37
    • 0034660532 scopus 로고    scopus 로고
    • Two-headed binding of a processive myosin to F-actin
    • Walker ML, et al. (2000) Two-headed binding of a processive myosin to F-actin. Nature 405(6788):804-807.
    • (2000) Nature , vol.405 , Issue.6788 , pp. 804-807
    • Walker, M.L.1
  • 39
    • 77951978236 scopus 로고    scopus 로고
    • Direct observation of the myosin-Va power stroke and its reversal
    • Sellers JR, Veigel C (2010) Direct observation of the myosin-Va power stroke and its reversal. Nat Struct Mol Biol 17(5):590-595.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.5 , pp. 590-595
    • Sellers, J.R.1    Veigel, C.2
  • 40
    • 80052470762 scopus 로고    scopus 로고
    • Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models
    • Ortega A, Amorós D, García de la Torre J (2011) Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models. Biophys J 101(4):892-898.
    • (2011) Biophys J , vol.101 , Issue.4 , pp. 892-898
    • Ortega, A.1    Amorós, D.2    García De La Torre, J.3
  • 41
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin v structures delineate essential features of chemo-mechanical transduction
    • Coureux PD, Sweeney HL, Houdusse A (2004) Three myosin V structures delineate essential features of chemo-mechanical transduction. EMBO J 23(23):4527-4537.
    • (2004) EMBO J , vol.23 , Issue.23 , pp. 4527-4537
    • Coureux, P.D.1    Sweeney, H.L.2    Houdusse, A.3
  • 43
    • 0034700284 scopus 로고    scopus 로고
    • Actin and light chain isoform dependence of myosin v kinetics
    • De La Cruz EM, Wells AL, Sweeney HL, Ostap EM (2000) Actin and light chain isoform dependence of myosin V kinetics. Biochemistry 39(46):14196-14202.
    • (2000) Biochemistry , vol.39 , Issue.46 , pp. 14196-14202
    • De La Cruz, E.M.1    Wells, A.L.2    Sweeney, H.L.3    Ostap, E.M.4
  • 44
    • 0032425057 scopus 로고    scopus 로고
    • Estimation of cross-bridge stiffness from maximum thermodynamic efficiency
    • Barclay CJ (1998) Estimation of cross-bridge stiffness from maximum thermodynamic efficiency. J Muscle Res Cell Motil 19(8):855-864.
    • (1998) J Muscle Res Cell Motil , vol.19 , Issue.8 , pp. 855-864
    • Barclay, C.J.1
  • 45
    • 25444456675 scopus 로고    scopus 로고
    • Effect of temperature on the working stroke of muscle myosin
    • Decostre V, Bianco P, Lombardi V, Piazzesi G (2005) Effect of temperature on the working stroke of muscle myosin. Proc Natl Acad Sci USA 102(39):13927-13932.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.39 , pp. 13927-13932
    • Decostre, V.1    Bianco, P.2    Lombardi, V.3    Piazzesi, G.4
  • 46
    • 44049094435 scopus 로고    scopus 로고
    • Single-molecule measurement of the stiffness of the rigor myosin head
    • Lewalle A, Steffen W, Stevenson O, Ouyang Z, Sleep J (2008) Single-molecule measurement of the stiffness of the rigor myosin head. Biophys J 94(6):2160-2169.
    • (2008) Biophys J , vol.94 , Issue.6 , pp. 2160-2169
    • Lewalle, A.1    Steffen, W.2    Stevenson, O.3    Ouyang, Z.4    Sleep, J.5
  • 47
    • 80052429807 scopus 로고    scopus 로고
    • Lever-arm mechanics of processive myosins
    • Sun YJ, Goldman YE (2011) Lever-arm mechanics of processive myosins. Biophys J 101(1):1-11.
    • (2011) Biophys J , vol.101 , Issue.1 , pp. 1-11
    • Sun, Y.J.1    Goldman, Y.E.2
  • 48
    • 44849116355 scopus 로고    scopus 로고
    • Long single alpha-helical tail domains bridge the gap between structure and function of myosin VI
    • Spink BJ, Sivaramakrishnan S, Lipfert J, Doniach S, Spudich JA (2008) Long single alpha-helical tail domains bridge the gap between structure and function of myosin VI. Nat Struct Mol Biol 15(6):591-597.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.6 , pp. 591-597
    • Spink, B.J.1    Sivaramakrishnan, S.2    Lipfert, J.3    Doniach, S.4    Spudich, J.A.5
  • 49
    • 68349146394 scopus 로고    scopus 로고
    • Myosin VI dimerization triggers an unfolding of a threehelix bundle in order to extend its reach
    • Mukherjea M, et al. (2009) Myosin VI dimerization triggers an unfolding of a threehelix bundle in order to extend its reach. Mol Cell 35(3):305-315.
    • (2009) Mol Cell , vol.35 , Issue.3 , pp. 305-315
    • Mukherjea, M.1
  • 50
    • 78149433174 scopus 로고    scopus 로고
    • Myosin VI: How do charged tails exert control?
    • Thirumalai D, Zhang ZC (2010) Myosin VI: How do charged tails exert control? Structure 18(11):1393-1394.
    • (2010) Structure , vol.18 , Issue.11 , pp. 1393-1394
    • Thirumalai, D.1    Zhang, Z.C.2
  • 52
    • 36749114331 scopus 로고
    • Diffusion-controlled intrachain reactions of polymers. 1. Theory
    • Wilemski G, Fixman M (1974) Diffusion-controlled intrachain reactions of polymers. 1. Theory. J Chem Phys 60(3):866-877.
    • (1974) J Chem Phys , vol.60 , Issue.3 , pp. 866-877
    • Wilemski, G.1    Fixman, M.2
  • 54
    • 0001604770 scopus 로고
    • Statistical mechanical theory of stiff chains
    • Saito N, Takahashi W, Yunoki Y (1967) Statistical mechanical theory of stiff chains. J Phys Soc Jpn 22:219-226.
    • (1967) J Phys Soc Jpn , vol.22 , pp. 219-226
    • Saito, N.1    Takahashi, W.2    Yunoki, Y.3
  • 55
    • 34547925924 scopus 로고    scopus 로고
    • Kinetics of interior loop formation in semiflexible chains
    • Hyeon C, Thirumalai D (2006) Kinetics of interior loop formation in semiflexible chains. J Chem Phys 124(10):104905.
    • (2006) J Chem Phys , vol.124 , Issue.10 , pp. 104905
    • Hyeon, C.1    Thirumalai, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.