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Volumn 10, Issue 10, 2009, Pages 1429-1438

Diffusive movement of processive kinesin-1 on microtubules

Author keywords

Diffusion; Kinesin; Microtubules; Motor proteins; Quantum dot

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID; KINESIN; KINESIN 1; QUANTUM DOT; SODIUM CHLORIDE;

EID: 70350425612     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2009.00964.x     Document Type: Article
Times cited : (38)

References (37)
  • 1
    • 33646950699 scopus 로고    scopus 로고
    • The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends
    • Helenius J, Brouhard G, Kalaidzidis Y, Diez S, Howard J. The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends. Nature 2006, 441:115-119.
    • (2006) Nature , vol.441 , pp. 115-119
    • Helenius, J.1    Brouhard, G.2    Kalaidzidis, Y.3    Diez, S.4    Howard, J.5
  • 2
    • 33846429185 scopus 로고    scopus 로고
    • Microtubule polymerases and depolymerases
    • Howard J, Hyman AA. Microtubule polymerases and depolymerases. Curr Opin Cell Biol 2007, 19:31-35.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 31-35
    • Howard, J.1    Hyman, A.A.2
  • 5
    • 61349122738 scopus 로고    scopus 로고
    • Diffusion and directed movement: in vitro motile properties of fission yeast kinesin-14 Pkl1
    • Furuta K, Edamatsu M, Maeda Y, Toyoshima YY. Diffusion and directed movement: in vitro motile properties of fission yeast kinesin-14 Pkl1. J Biol Chem 2008, 283:36465-36473.
    • (2008) J Biol Chem , vol.283 , pp. 36465-36473
    • Furuta, K.1    Edamatsu, M.2    Maeda, Y.3    Toyoshima, Y.Y.4
  • 6
    • 33845993250 scopus 로고    scopus 로고
    • Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells
    • Cai D, Hoppe AD, Swanson JA, Verhey KJ. Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells. J Cell Biol 2007, 176:51-63.
    • (2007) J Cell Biol , vol.176 , pp. 51-63
    • Cai, D.1    Hoppe, A.D.2    Swanson, J.A.3    Verhey, K.J.4
  • 7
    • 0033195492 scopus 로고    scopus 로고
    • Single-molecule analysis of kinesin motility reveals regulation by the cargo-binding tail domain
    • Friedman DS, Vale RD. Single-molecule analysis of kinesin motility reveals regulation by the cargo-binding tail domain. Nat Cell Biol 1999, 1:293-297.
    • (1999) Nat Cell Biol , vol.1 , pp. 293-297
    • Friedman, D.S.1    Vale, R.D.2
  • 8
    • 0034079578 scopus 로고    scopus 로고
    • The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity
    • Wang Z, Sheetz MP. The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity. Biophys J 2000, 78:1955-1964.
    • (2000) Biophys J , vol.78 , pp. 1955-1964
    • Wang, Z.1    Sheetz, M.P.2
  • 9
    • 27744552948 scopus 로고    scopus 로고
    • The E-hook of tubulin interacts with kinesin's head to increase processivity and speed
    • Lakamper S, Meyhofer E. The E-hook of tubulin interacts with kinesin's head to increase processivity and speed. Biophys J 2005, 89:3223-3234.
    • (2005) Biophys J , vol.89 , pp. 3223-3234
    • Lakamper, S.1    Meyhofer, E.2
  • 10
    • 0026705754 scopus 로고
    • Kinesin undergoes a 9 S to 6 S conformational transition
    • Hackney DD, Levitt JD, Suhan J. Kinesin undergoes a 9 S to 6 S conformational transition. J Biol Chem 1992, 267:8696-8701.
    • (1992) J Biol Chem , vol.267 , pp. 8696-8701
    • Hackney, D.D.1    Levitt, J.D.2    Suhan, J.3
  • 11
    • 0033771901 scopus 로고    scopus 로고
    • Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release
    • Hackney DD, Stock MF. Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release. Nat Cell Biol 2000, 2:257-260.
    • (2000) Nat Cell Biol , vol.2 , pp. 257-260
    • Hackney, D.D.1    Stock, M.F.2
  • 12
    • 0842277818 scopus 로고    scopus 로고
    • Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism
    • Schief WR, Clark RH, Crevenna AH, Howard J. Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism. Proc Natl Acad Sci U S A 2004, 101:1183-1188.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1183-1188
    • Schief, W.R.1    Clark, R.H.2    Crevenna, A.H.3    Howard, J.4
  • 13
    • 0037133038 scopus 로고    scopus 로고
    • Direct long-term observation of kinesin processivity at low load
    • Yajima J, Alonso MC, Cross RA, Toyoshima YY. Direct long-term observation of kinesin processivity at low load. Curr Biol 2002, 12:301-306.
    • (2002) Curr Biol , vol.12 , pp. 301-306
    • Yajima, J.1    Alonso, M.C.2    Cross, R.A.3    Toyoshima, Y.Y.4
  • 14
    • 0034722388 scopus 로고    scopus 로고
    • Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change.
    • Tomishige M, Vale RD. Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change. J Cell Biol 2000, 151:1081-1092.
    • (2000) J Cell Biol , vol.151 , pp. 1081-1092
    • Tomishige, M.1    Vale, R.D.2
  • 15
    • 0034765827 scopus 로고    scopus 로고
    • Motility of single one-headed kinesin molecules along microtubules
    • Inoue Y, Iwane AH, Miyai T, Muto E, Yanagida T. Motility of single one-headed kinesin molecules along microtubules. Biophys J 2001, 81:2838-2850.
    • (2001) Biophys J , vol.81 , pp. 2838-2850
    • Inoue, Y.1    Iwane, A.H.2    Miyai, T.3    Muto, E.4    Yanagida, T.5
  • 17
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn KS, Ubersax JA, Vale RD. Engineering the processive run length of the kinesin motor. J Cell Biol 2000, 151:1093-1100.
    • (2000) J Cell Biol , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 19
    • 1542353988 scopus 로고
    • Kinesin ATPase: rate-limiting ADP release
    • Hackney DD. Kinesin ATPase: rate-limiting ADP release. Proc Natl Acad Sci U S A 1988, 85:6314-6318.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 6314-6318
    • Hackney, D.D.1
  • 20
    • 3242776257 scopus 로고    scopus 로고
    • The kinetic mechanism of kinesin
    • Cross RA. The kinetic mechanism of kinesin. Trends Biochem Sci 2004, 29:301-309.
    • (2004) Trends Biochem Sci , vol.29 , pp. 301-309
    • Cross, R.A.1
  • 21
    • 0031021473 scopus 로고    scopus 로고
    • Interacting head mechanism of microtubule-kinesin ATPase
    • Ma YZ, Taylor EW. Interacting head mechanism of microtubule-kinesin ATPase. J Biol Chem 1997, 272:724-730.
    • (1997) J Biol Chem , vol.272 , pp. 724-730
    • Ma, Y.Z.1    Taylor, E.W.2
  • 22
    • 0028355574 scopus 로고
    • Pre-steady-state kinetics of the microtubule-kinesin ATPase
    • Gilbert SP, Johnson KA. Pre-steady-state kinetics of the microtubule-kinesin ATPase. Biochemistry 1994, 33:1951-1960.
    • (1994) Biochemistry , vol.33 , pp. 1951-1960
    • Gilbert, S.P.1    Johnson, K.A.2
  • 23
    • 0034681137 scopus 로고    scopus 로고
    • Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin
    • Okada Y, Hirokawa N. Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin. Proc Natl Acad Sci U S A 2000, 97:640-645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 24
    • 65949119126 scopus 로고    scopus 로고
    • Mammalian kinesin-3 motors are dimeric in vivo and move by processive motility upon release of autoinhibition
    • Hammond JW, Cai D, Blasius TL, Li Z, Jiang Y, Jih GT, Meyhofer E, Verhey KJ. Mammalian kinesin-3 motors are dimeric in vivo and move by processive motility upon release of autoinhibition. PLoS Biol 2009, 7:e1000072.
    • (2009) PLoS Biol , vol.7
    • Hammond, J.W.1    Cai, D.2    Blasius, T.L.3    Li, Z.4    Jiang, Y.5    Jih, G.T.6    Meyhofer, E.7    Verhey, K.J.8
  • 25
    • 43149106486 scopus 로고    scopus 로고
    • CENP-E combines a slow, processive motor and a flexible coiled coil to produce an essential motile kinetochore tether
    • Kim Y, Heuser JE, Waterman CM, Cleveland DW. CENP-E combines a slow, processive motor and a flexible coiled coil to produce an essential motile kinetochore tether. J Cell Biol 2008, 181:411-419.
    • (2008) J Cell Biol , vol.181 , pp. 411-419
    • Kim, Y.1    Heuser, J.E.2    Waterman, C.M.3    Cleveland, D.W.4
  • 26
    • 38349076942 scopus 로고    scopus 로고
    • Minus-end-directed motor Ncd exhibits processive movement that is enhanced by microtubule bundling in vitro
    • Furuta K, Toyoshima YY. Minus-end-directed motor Ncd exhibits processive movement that is enhanced by microtubule bundling in vitro. Curr Biol 2008, 18:152-157.
    • (2008) Curr Biol , vol.18 , pp. 152-157
    • Furuta, K.1    Toyoshima, Y.Y.2
  • 27
    • 49749149177 scopus 로고    scopus 로고
    • Activation of mitotic kinesin by microtubule bundling
    • Tomishige M. Activation of mitotic kinesin by microtubule bundling. J Cell Biol 2008, 182:417-419.
    • (2008) J Cell Biol , vol.182 , pp. 417-419
    • Tomishige, M.1
  • 28
    • 0030824684 scopus 로고    scopus 로고
    • Mechanics of single kinesin molecules measured by optical trapping nanometry
    • Kojima H, Muto E, Higuchi H, Yanagida T. Mechanics of single kinesin molecules measured by optical trapping nanometry. Biophys J 1997, 73:2012-2022.
    • (1997) Biophys J , vol.73 , pp. 2012-2022
    • Kojima, H.1    Muto, E.2    Higuchi, H.3    Yanagida, T.4
  • 29
    • 0035069744 scopus 로고    scopus 로고
    • Substeps within the 8-nm step of the ATPase cycle of single kinesin molecules
    • Nishiyama M, Muto E, Inoue Y, Yanagida T, Higuchi H. Substeps within the 8-nm step of the ATPase cycle of single kinesin molecules. Nat Cell Biol 2001, 3:425-428.
    • (2001) Nat Cell Biol , vol.3 , pp. 425-428
    • Nishiyama, M.1    Muto, E.2    Inoue, Y.3    Yanagida, T.4    Higuchi, H.5
  • 30
    • 33845967100 scopus 로고    scopus 로고
    • Two binding partners cooperate to activate the molecular motor Kinesin-1
    • Blasius TL, Cai D, Jih GT, Toret CP, Verhey KJ. Two binding partners cooperate to activate the molecular motor Kinesin-1. J Cell Biol 2007, 176:11-17.
    • (2007) J Cell Biol , vol.176 , pp. 11-17
    • Blasius, T.L.1    Cai, D.2    Jih, G.T.3    Toret, C.P.4    Verhey, K.J.5
  • 31
    • 84922523364 scopus 로고    scopus 로고
    • Intracellular imaging of targeted proteins labeled with quantum dots
    • Yoo J, Kambara T, Gonda K, Higuchi H. Intracellular imaging of targeted proteins labeled with quantum dots. Exp Cell Res 2008, 314:3563-3569.
    • (2008) Exp Cell Res , vol.314 , pp. 3563-3569
    • Yoo, J.1    Kambara, T.2    Gonda, K.3    Higuchi, H.4
  • 32
    • 34250372604 scopus 로고    scopus 로고
    • Tracking single kinesin molecules in the cytoplasm of mammalian cells
    • Cai D, Verhey KJ, Meyhöfer E. Tracking single kinesin molecules in the cytoplasm of mammalian cells. Biophysical Journal 2007, 92:4137-4144.
    • (2007) Biophysical Journal , vol.92 , pp. 4137-4144
    • Cai, D.1    Verhey, K.J.2    Meyhöfer, E.3
  • 33
    • 33746871112 scopus 로고    scopus 로고
    • Tracking individual kinesin motors in living cells using single quantum-dot imaging
    • Courty S, Luccardini C, Bellaiche Y, Cappello G, Dahan M. Tracking individual kinesin motors in living cells using single quantum-dot imaging. Nano Lett 2006, 6:1491-1495.
    • (2006) Nano Lett , vol.6 , pp. 1491-1495
    • Courty, S.1    Luccardini, C.2    Bellaiche, Y.3    Cappello, G.4    Dahan, M.5
  • 34
    • 60749102596 scopus 로고    scopus 로고
    • The diffusive interaction of microtubule binding proteins
    • Cooper JR, Wordeman L. The diffusive interaction of microtubule binding proteins. Curr Opin Cell Biol 2009, 21:68-73.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 68-73
    • Cooper, J.R.1    Wordeman, L.2
  • 35
    • 34848896360 scopus 로고    scopus 로고
    • Engineering the processive run length of myosin V
    • Hodges AR, Krementsova EB, Trybus KM. Engineering the processive run length of myosin V. J Biol Chem 2007, 282:27192-27197.
    • (2007) J Biol Chem , vol.282 , pp. 27192-27197
    • Hodges, A.R.1    Krementsova, E.B.2    Trybus, K.M.3
  • 37
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization.
    • Yildiz A, Forkey JN, McKinney SA, Ha T, Goldman YE, Selvin PR. Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 2003, 300:2061-2065.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.