메뉴 건너뛰기




Volumn 11, Issue 1, 2000, Pages 161-169

Evidence for a novel affinity mechanism of motor-assisted transport along microtubules

Author keywords

[No Author keywords available]

Indexed keywords

BETA TUBULIN; DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN;

EID: 0033978565     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.1.161     Document Type: Article
Times cited : (10)

References (27)
  • 2
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules. Studied with optical tweezers
    • Block, S.M., Goldstein, L.S.B., and Schnapp, B.J. (1990). Bead movement by single kinesin molecules. Studied with optical tweezers. Nature 348, 348-352.
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.B.2    Schnapp, B.J.3
  • 3
    • 0029887264 scopus 로고    scopus 로고
    • Microtubule minus ends can be labeled with a phage display antibody specific to alpha-tubulin
    • Fan, J., Griffiths, A.D., Lockhar, A., Cross, R.A., and Amos, L.A. (1996). Microtubule minus ends can be labeled with a phage display antibody specific to alpha-tubulin. J. Mol. Biol. 259, 325-330.
    • (1996) J. Mol. Biol. , vol.259 , pp. 325-330
    • Fan, J.1    Griffiths, A.D.2    Lockhar, A.3    Cross, R.A.4    Amos, L.A.5
  • 4
    • 0003051583 scopus 로고
    • Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions
    • Frens, G. (1973). Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions. Nature 241, 20-22.
    • (1973) Nature , vol.241 , pp. 20-22
    • Frens, G.1
  • 5
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill, S.R., Schroer, T.A., Szilak, I., Steuer, E.R., Sheetz, M.P., and Cleveland, D.W. (1991). Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol. 175, 1639-1650.
    • (1991) J. Cell Biol. , vol.175 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 6
    • 0020118942 scopus 로고
    • Monoclonal antibodies that recognize discrete forms of tubulin
    • Gozes, I., and Barnstable, C.J. (1982). Monoclonal antibodies that recognize discrete forms of tubulin. Proc. Natl. Acad. Sci. USA 79, 2579-2583.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2579-2583
    • Gozes, I.1    Barnstable, C.J.2
  • 7
    • 0032554803 scopus 로고    scopus 로고
    • Chromosome movement: Kinetochores motor along
    • Grancell, A., and Sorger, P.K. (1998). Chromosome movement: kinetochores motor along. Curr. Biol. 8, R382-R385.
    • (1998) Curr. Biol. , vol.8
    • Grancell, A.1    Sorger, P.K.2
  • 9
    • 0025881253 scopus 로고
    • A cAMP-stimulated phosphorylation of an axonemal polypeptide that copurifies with the 22S dynein arm regulates microtubule translocation velocity and swimming speed in Paramecium
    • Hamasaki, T., Barkalow, K., Richmond, J., and Satir, P. (1991). A cAMP-stimulated phosphorylation of an axonemal polypeptide that copurifies with the 22S dynein arm regulates microtubule translocation velocity and swimming speed in Paramecium. Proc. Natl. Acad. Sci. USA 88, 7918-7922.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7918-7922
    • Hamasaki, T.1    Barkalow, K.2    Richmond, J.3    Satir, P.4
  • 10
    • 0028876063 scopus 로고
    • Mechanochemical aspects of axonemal dynein activity studied by in vitro microtubule translocation
    • Hamasaki, T., Holwill, M.E.J., Barkalow, K., and Satir, P. (1995). Mechanochemical aspects of axonemal dynein activity studied by in vitro microtubule translocation. Biophys. J. 69, 2569-2579.
    • (1995) Biophys. J. , vol.69 , pp. 2569-2579
    • Hamasaki, T.1    Holwill, M.E.J.2    Barkalow, K.3    Satir, P.4
  • 11
    • 0032559822 scopus 로고    scopus 로고
    • Processivity of the motor protein kinesin requires two heads
    • Hancock, W.O., and Howard, J. (1998). Processivity of the motor protein kinesin requires two heads. J. Cell Biol. 140, 1395-1405.
    • (1998) J. Cell Biol. , vol.140 , pp. 1395-1405
    • Hancock, W.O.1    Howard, J.2
  • 12
    • 0029039829 scopus 로고
    • Three-dimensional structure of a tubulin-motor-protein complex
    • Hoenger, A., Sablin, E.P., Vale, R.D., Fletterick, R.J., and Milligan, R.A. (1995). Three-dimensional structure of a tubulin-motor-protein complex. Nature 376, 271-274.
    • (1995) Nature , vol.376 , pp. 271-274
    • Hoenger, A.1    Sablin, E.P.2    Vale, R.D.3    Fletterick, R.J.4    Milligan, R.A.5
  • 13
    • 0031004867 scopus 로고    scopus 로고
    • Influence of the kinesin neck domain on dimerization and ATPase kinetics
    • Jiang, W., Stock, M.F., Li, X., and Hackney, D.D. (1997). Influence of the kinesin neck domain on dimerization and ATPase kinetics. J. Biol. Chem. 272, 7626-7632.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7626-7632
    • Jiang, W.1    Stock, M.F.2    Li, X.3    Hackney, D.D.4
  • 14
    • 0023837441 scopus 로고
    • Polewards chromosome movement driven by microtubule depolymerization in vitro
    • Koshland, D.E., Mitchison, T.J., and Kirschner, M.W. (1988). Polewards chromosome movement driven by microtubule depolymerization in vitro. Nature 331, 499-504.
    • (1988) Nature , vol.331 , pp. 499-504
    • Koshland, D.E.1    Mitchison, T.J.2    Kirschner, M.W.3
  • 15
    • 0023389780 scopus 로고
    • Identification of an acetylation site of Chlamydomonas α-tubulin
    • LeDizet, M., and Piperno, G. (1987). Identification of an acetylation site of Chlamydomonas α-tubulin. Proc. Natl. Acad. Sci. USA 84, 5720-5724.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5720-5724
    • LeDizet, M.1    Piperno, G.2
  • 17
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S.G., and Downing, K.H. (1998). Structure of the αβ tubulin dimer by electron crystallography. Nature 391, 199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 18
    • 0033582814 scopus 로고    scopus 로고
    • A processive single-headed motor: Kinesin superfamily protein KIF1A
    • Okada, Y., and 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
  • 19
    • 0032146974 scopus 로고    scopus 로고
    • The vertebrate cell kinetochore and its roles during mitosis
    • Rieder, C.L., and Salmon, E.D. (1998). The vertebrate cell kinetochore and its roles during mitosis. Trends Cell Biol. 8, 310-317.
    • (1998) Trends Cell Biol. , vol.8 , pp. 310-317
    • Rieder, C.L.1    Salmon, E.D.2
  • 20
    • 0028854634 scopus 로고
    • The anatomy of flagellar MTs: Polarity, seam, junctions, and lattice
    • Song, Y.H., and Mandelkow, E. (1995). The anatomy of flagellar MTs: polarity, seam, junctions, and lattice. J. Cell Biol. 128, 81-94.
    • (1995) J. Cell Biol. , vol.128 , pp. 81-94
    • Song, Y.H.1    Mandelkow, E.2
  • 21
    • 0024991350 scopus 로고
    • Myosin step size estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • Uyeda, T.Q.P., Kron, S.J., and Spudich, J.A. (1990). Myosin step size estimation from slow sliding movement of actin over low densities of heavy meromyosin. J. Mol. Biol. 214, 699-710.
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 22
    • 0027070849 scopus 로고
    • Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motors
    • Vale, R.D., Malik, F., and Brown, D. (1992). Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motors. J. Cell Biol. 119, 1589-1596.
    • (1992) J. Cell Biol. , vol.119 , pp. 1589-1596
    • Vale, R.D.1    Malik, F.2    Brown, D.3
  • 23
    • 0024805563 scopus 로고
    • One-dimensional diffusion of microtubules bound to flagellar dynein
    • Vale, R.D., Soll, D.R., and Gibbons, I.R. (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
  • 24
    • 0024687692 scopus 로고
    • Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia
    • Vale, R.D., and Toyoshima, Y.Y. (1989). Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia. J. Cell Biol. 108, 2327-2334.
    • (1989) J. Cell Biol. , vol.108 , pp. 2327-2334
    • Vale, R.D.1    Toyoshima, Y.Y.2
  • 25
    • 0029563632 scopus 로고
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
    • Vaughan, K.T., and Vallee, R.B. (1995). Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued. J. Cell Biol. 131, 1507-1516.
    • (1995) J. Cell Biol. , vol.131 , pp. 1507-1516
    • Vaughan, K.T.1    Vallee, R.B.2
  • 26
    • 0031055639 scopus 로고    scopus 로고
    • Microtubule structure and dynamics
    • Wade, R.H., and Hyman, A.A. (1997). Microtubule structure and dynamics. Curr. Opin. Cell Biol. 9, 12-17.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 12-17
    • Wade, R.H.1    Hyman, A.A.2
  • 27
    • 0020009818 scopus 로고
    • Preparation of tubulin from brain
    • Williams, R.C., and Lee, J.C. (1982). Preparation of tubulin from brain. Methods Enzymol. 85, 376-381.
    • (1982) Methods Enzymol. , vol.85 , pp. 376-381
    • Williams, R.C.1    Lee, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.