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Volumn 6, Issue 9, 2011, Pages

Diffusion of myosin v on microtubules: A fine-tuned interaction for which e-hooks are dispensable

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; KINESIN; MYOSIN V; ACTIN;

EID: 80053154678     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025473     Document Type: Article
Times cited : (10)

References (54)
  • 2
    • 70349973366 scopus 로고    scopus 로고
    • Anomalous Dynamics of Melanosomes Driven by Myosin-V in Xenopus laevis Melanophores
    • Brunstein M, Bruno L, Desposito M, Levi V, (2009) Anomalous Dynamics of Melanosomes Driven by Myosin-V in Xenopus laevis Melanophores. Biophysical Journal 97: 1548-1557.
    • (2009) Biophysical Journal , vol.97 , pp. 1548-1557
    • Brunstein, M.1    Bruno, L.2    Desposito, M.3    Levi, V.4
  • 3
    • 9244232349 scopus 로고    scopus 로고
    • Molecular motors: Strategies to get along
    • Mallik R, Gross SP, (2004) Molecular motors: Strategies to get along. Current Biology 14: R971-R982.
    • (2004) Current Biology , vol.14
    • Mallik, R.1    Gross, S.P.2
  • 4
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale RD, (2003) The molecular motor toolbox for intracellular transport. Cell 112: 467-480.
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 5
    • 34250362299 scopus 로고    scopus 로고
    • Cargo transport: two motors are sometimes better than one
    • Gross SP, Vershinin M, Shubeita GT, (2007) Cargo transport: two motors are sometimes better than one. Curr Biol 17: R478-486.
    • (2007) Curr Biol , vol.17
    • Gross, S.P.1    Vershinin, M.2    Shubeita, G.T.3
  • 6
    • 33845315084 scopus 로고    scopus 로고
    • Powering membrane traffic in endocytosis and recycling
    • Soldati T, Schliwa M, (2006) Powering membrane traffic in endocytosis and recycling. Nat Rev Mol Cell Biol 7: 897-908.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 897-908
    • Soldati, T.1    Schliwa, M.2
  • 7
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm
    • Kuznetsov SA, Langford GM, Weiss DG, (1992) Actin-dependent organelle movement in squid axoplasm. Nature 356: 722-725.
    • (1992) Nature , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, G.M.2    Weiss, D.G.3
  • 8
    • 0033588979 scopus 로고    scopus 로고
    • Regulation of melanosome movement in the cell cycle by reversible association with myosin V
    • Rogers SL, Karcher RL, Roland JT, Minin AA, Steffen W, et al. (1999) Regulation of melanosome movement in the cell cycle by reversible association with myosin V. J Cell Biol 146: 1265-1276.
    • (1999) J Cell Biol , vol.146 , pp. 1265-1276
    • Rogers, S.L.1    Karcher, R.L.2    Roland, J.T.3    Minin, A.A.4    Steffen, W.5
  • 9
    • 0032517764 scopus 로고    scopus 로고
    • Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores
    • Tuma MC, Zill A, Le Bot N, Vernos I, Gelfand V, (1998) Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores. J Cell Biol 143: 1547-1558.
    • (1998) J Cell Biol , vol.143 , pp. 1547-1558
    • Tuma, M.C.1    Zill, A.2    Le Bot, N.3    Vernos, I.4    Gelfand, V.5
  • 10
    • 0036898465 scopus 로고    scopus 로고
    • Myosin-V, a versatile motor for short-range vesicle transport
    • Langford GM, (2002) Myosin-V, a versatile motor for short-range vesicle transport. Traffic 3: 859-865.
    • (2002) Traffic , vol.3 , pp. 859-865
    • Langford, G.M.1
  • 11
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo
    • Wu XF, Bowers B, Rao K, Wei Q, Hammer JA, (1998) Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo. Journal of Cell Biology 143: 1899-1918.
    • (1998) Journal of Cell Biology , vol.143 , pp. 1899-1918
    • Wu, X.F.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer, J.A.5
  • 13
    • 34848896360 scopus 로고    scopus 로고
    • Engineering the processive run length of Myosin V
    • Hodges AR, Krementsova EB, Trybus KM, (2007) Engineering the processive run length of Myosin V. J Biol Chem 282: 27192-27197.
    • (2007) J Biol Chem , vol.282 , pp. 27192-27197
    • Hodges, A.R.1    Krementsova, E.B.2    Trybus, K.M.3
  • 14
    • 1542267772 scopus 로고    scopus 로고
    • Functional role of loop 2 in myosin V
    • Yengo CM, Sweeney HL, (2004) Functional role of loop 2 in myosin V. Biochemistry 43: 2605-2612.
    • (2004) Biochemistry , vol.43 , pp. 2605-2612
    • Yengo, C.M.1    Sweeney, H.L.2
  • 15
    • 0042165822 scopus 로고    scopus 로고
    • Addition of lysines to the 50/20 kDa junction of myosin strengthens weak binding to actin without affecting the maximum ATPase activity
    • Joel PB, Sweeney HL, Trybus KM, (2003) Addition of lysines to the 50/20 kDa junction of myosin strengthens weak binding to actin without affecting the maximum ATPase activity. Biochemistry 42: 9160-9166.
    • (2003) Biochemistry , vol.42 , pp. 9160-9166
    • Joel, P.B.1    Sweeney, H.L.2    Trybus, K.M.3
  • 17
    • 27744552948 scopus 로고    scopus 로고
    • The E-hook of tubulin interacts with kinesin's head to increase processivity and speed
    • Lakamper S, Meyhofer E, (2005) The E-hook of tubulin interacts with kinesin's head to increase processivity and speed. Biophysical Journal 89: 3223-3234.
    • (2005) Biophysical Journal , vol.89 , pp. 3223-3234
    • Lakamper, S.1    Meyhofer, E.2
  • 18
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn KS, Ubersax JA, Vale RD, (2000) Engineering the processive run length of the kinesin motor. Journal of Cell Biology 151: 1093-1100.
    • (2000) Journal of Cell Biology , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 19
    • 0033582814 scopus 로고    scopus 로고
    • A processive single-headed motor: Kinesin superfamily protein KIF1A
    • Okada Y, Hirokawa N, (1999) A processive single-headed motor: Kinesin superfamily protein KIF1A. Science 283: 1152-1157.
    • (1999) Science , vol.283 , pp. 1152-1157
    • Okada, Y.1    Hirokawa, N.2
  • 20
    • 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, (2006) The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends. Nature 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
  • 21
    • 0030755709 scopus 로고    scopus 로고
    • Microtubule interaction site of the kinesin motor
    • Woehlke G, Ruby AK, Hart CL, Ly B, HomBooher N, et al. (1997) Microtubule interaction site of the kinesin motor. Cell 90: 207-216.
    • (1997) Cell , vol.90 , pp. 207-216
    • Woehlke, G.1    Ruby, A.K.2    Hart, C.L.3    Ly, B.4    HomBooher, N.5
  • 22
    • 0032481381 scopus 로고    scopus 로고
    • Proteolytic mapping of kinesin/ncd-microtubule interface: nucleotide-dependent conformational changes in the loops L8 and L12
    • Alonso MC, van Damme J, Vandekerckhove J, Cross RA, (1998) Proteolytic mapping of kinesin/ncd-microtubule interface: nucleotide-dependent conformational changes in the loops L8 and L12. Embo Journal 17: 945-951.
    • (1998) Embo Journal , vol.17 , pp. 945-951
    • Alonso, M.C.1    van Damme, J.2    Vandekerckhove, J.3    Cross, R.A.4
  • 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, (2000) Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin. Proceedings of the National Academy of Sciences of the United States of America 97: 640-645.
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 24
    • 0027934789 scopus 로고
    • Developmental regulation of polyglutamylated alpha-tubulin and beta-tubulin in mouse-brain neurons
    • Audebert S, Koulakoff A, Berwaldnetter Y, Gros F, Denoulet P, et al. (1994) Developmental regulation of polyglutamylated alpha-tubulin and beta-tubulin in mouse-brain neurons. Journal of Cell Science 107: 2313-2322.
    • (1994) Journal of Cell Science , vol.107 , pp. 2313-2322
    • Audebert, S.1    Koulakoff, A.2    Berwaldnetter, Y.3    Gros, F.4    Denoulet, P.5
  • 26
    • 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, et al. (2003) Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 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
  • 27
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale RD, Milligan RA, (2000) The way things move: Looking under the hood of molecular motor proteins. Science 288: 88-95.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 29
    • 26844512070 scopus 로고    scopus 로고
    • Molecular dynamics simulations of tubulin structure and calculations of electrostatic properties of microtubules
    • Tuszynski JA, Brown JA, Crawford E, Carpenter EJ, Nip MLA, et al. (2005) Molecular dynamics simulations of tubulin structure and calculations of electrostatic properties of microtubules. Mathematical and Computer Modelling 41: 1055-1070.
    • (2005) Mathematical and Computer Modelling , vol.41 , pp. 1055-1070
    • Tuszynski, J.A.1    Brown, J.A.2    Crawford, E.3    Carpenter, E.J.4    Nip, M.L.A.5
  • 34
    • 77951558010 scopus 로고    scopus 로고
    • One-Dimensional Brownian Motion of Charged Nanoparticles along Microtubules: A Model System for Weak Binding Interactions
    • Minoura I, Katayama E, Sekimoto K, Muto E, (2010) One-Dimensional Brownian Motion of Charged Nanoparticles along Microtubules: A Model System for Weak Binding Interactions. Biophysical Journal 98: 1589-1597.
    • (2010) Biophysical Journal , vol.98 , pp. 1589-1597
    • Minoura, I.1    Katayama, E.2    Sekimoto, K.3    Muto, E.4
  • 35
    • 60749102596 scopus 로고    scopus 로고
    • The diffusive interaction of microtubule binding proteins
    • Cooper JR, Wordeman L, (2009) The diffusive interaction of microtubule binding proteins. Current Opinion in Cell Biology 21: 68-73.
    • (2009) Current Opinion in Cell Biology , vol.21 , pp. 68-73
    • Cooper, J.R.1    Wordeman, L.2
  • 36
    • 0024805563 scopus 로고
    • One dimensional diffusion of microtubules bound to flagellar dynein
    • Vale RD, Soll DR, Gibbons IR, (1989) One dimensional diffusion of microtubules bound to flagellar dynein. Cell 59: 915-925.
    • (1989) Cell , vol.59 , pp. 915-925
    • Vale, R.D.1    Soll, D.R.2    Gibbons, I.R.3
  • 37
    • 0032737402 scopus 로고    scopus 로고
    • One-dimensional diffusion on microtubules of particles coated with cytoplasmic dynein an immunoglobulins
    • Wang ZH, Sheetz MP, (1999) One-dimensional diffusion on microtubules of particles coated with cytoplasmic dynein an immunoglobulins. Cell Structure and Function 24: 373-383.
    • (1999) Cell Structure and Function , vol.24 , pp. 373-383
    • Wang, Z.H.1    Sheetz, M.P.2
  • 38
    • 84859748023 scopus 로고    scopus 로고
    • Mechanism of the single-headed processivity: Diffusional anchoring between "K-loop" of kinesin and the C-terminal of tubulin
    • Okada Y, Hirokawa N, (1999) Mechanism of the single-headed processivity: Diffusional anchoring between "K-loop" of kinesin and the C-terminal of tubulin. Molecular Biology of the Cell 10: 1366.
    • (1999) Molecular Biology of the Cell , vol.10 , pp. 1366
    • Okada, Y.1    Hirokawa, N.2
  • 41
    • 33644747344 scopus 로고    scopus 로고
    • A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules
    • Culver-Hanlon TL, Lex SA, Stephens AD, Quintyne NJ, King SJ, (2006) A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules. Nature Cell Biology 8: 264-270.
    • (2006) Nature Cell Biology , vol.8 , pp. 264-270
    • Culver-Hanlon, T.L.1    Lex, S.A.2    Stephens, A.D.3    Quintyne, N.J.4    King, S.J.5
  • 43
  • 44
    • 77449158973 scopus 로고    scopus 로고
    • Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK
    • Cooper JR, Wagenbach M, Asbury CL, Wordeman L, (2010) Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK. Nature Structural & Molecular Biology 17: 77-U98.
    • (2010) Nature Structural & Molecular Biology , vol.17
    • Cooper, J.R.1    Wagenbach, M.2    Asbury, C.L.3    Wordeman, L.4
  • 45
    • 68949208665 scopus 로고    scopus 로고
    • Protein Friction Limits Diffusive and Directed Movements of Kinesin Motors on Microtubules
    • Bormuth V, Varga V, Howard J, Schaffer E, (2009) Protein Friction Limits Diffusive and Directed Movements of Kinesin Motors on Microtubules. Science 325: 870-873.
    • (2009) Science , vol.325 , pp. 870-873
    • Bormuth, V.1    Varga, V.2    Howard, J.3    Schaffer, E.4
  • 46
    • 13444292841 scopus 로고    scopus 로고
    • Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time
    • Churchman LS, Okten Z, Rock RS, Dawson JF, Spudich JA, (2005) Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time. Proc Natl Acad Sci U S A 102: 1419-1423.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1419-1423
    • Churchman, L.S.1    Okten, Z.2    Rock, R.S.3    Dawson, J.F.4    Spudich, J.A.5
  • 47
    • 0032513032 scopus 로고    scopus 로고
    • Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket
    • Sweeney HL, Rosenfeld SS, Brown F, Faust L, Smith J, et al. (1998) Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket. J Biol Chem 273: 6262-6270.
    • (1998) J Biol Chem , vol.273 , pp. 6262-6270
    • Sweeney, H.L.1    Rosenfeld, S.S.2    Brown, F.3    Faust, L.4    Smith, J.5
  • 48
    • 0022178476 scopus 로고
    • Tubulin domains probed by limited proteolysis and subunit-specific antibodies
    • Mandelkow EM, Herrmann M, Ruhl U, (1985) Tubulin domains probed by limited proteolysis and subunit-specific antibodies. J Mol Biol 185: 311-327.
    • (1985) J Mol Biol , vol.185 , pp. 311-327
    • Mandelkow, E.M.1    Herrmann, M.2    Ruhl, U.3
  • 50
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S, (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246: 4866-4871.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 51
    • 0018427133 scopus 로고
    • N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions
    • Meeusen RL, Cande WZ, (1979) N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions. J Cell Biol 82: 57-65.
    • (1979) J Cell Biol , vol.82 , pp. 57-65
    • Meeusen, R.L.1    Cande, W.Z.2
  • 52
    • 0028363764 scopus 로고
    • Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization
    • Huang TG, Hackney DD, (1994) Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization. J Biol Chem 269: 16493-16501.
    • (1994) J Biol Chem , vol.269 , pp. 16493-16501
    • Huang, T.G.1    Hackney, D.D.2
  • 53
    • 33846011437 scopus 로고    scopus 로고
    • Kinetic and mechanistic basis of the nonprocessive Kinesin-3 motor NcKin3
    • Adio S, Bloemink M, Hartel M, Leier S, Geeves MA, et al. (2006) Kinetic and mechanistic basis of the nonprocessive Kinesin-3 motor NcKin3. J Biol Chem 281: 37782-37793.
    • (2006) J Biol Chem , vol.281 , pp. 37782-37793
    • Adio, S.1    Bloemink, M.2    Hartel, M.3    Leier, S.4    Geeves, M.A.5
  • 54
    • 52949084351 scopus 로고    scopus 로고
    • Fluctuation analysis of mechanochemical coupling depending on the type of biomolecular motors
    • Nishikawa M, Takagi H, Shibata T, Iwane AH, Yanagida T, (2008) Fluctuation analysis of mechanochemical coupling depending on the type of biomolecular motors. Phys Rev Lett 101: 128103.
    • (2008) Phys Rev Lett , vol.101 , pp. 128103
    • Nishikawa, M.1    Takagi, H.2    Shibata, T.3    Iwane, A.H.4    Yanagida, T.5


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