메뉴 건너뛰기




Volumn 10, Issue 6, 1999, Pages 2063-2074

Congruent docking of dimeric kinesin and ncd into three-dimensional electron cryomicroscopy maps of microtubule-motor ADP complexes

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; KINESIN; TUBULIN;

EID: 0344867017     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.6.2063     Document Type: Article
Times cited : (75)

References (43)
  • 1
    • 0032481381 scopus 로고    scopus 로고
    • Proteolytic mapping of kinesin/ncd-microtubule interface: Nucleotide-dependent conformational changes in the loops L8 and L12
    • Alonso, M.C., Vanderkerckhove, J., and Cross, R.A. (1998). Proteolytic mapping of kinesin/ncd-microtubule interface: nucleotide-dependent conformational changes in the loops L8 and L12. EMBO J. 17, 945-951.
    • (1998) EMBO J. , vol.17 , pp. 945-951
    • Alonso, M.C.1    Vanderkerckhove, J.2    Cross, R.A.3
  • 2
    • 0031042321 scopus 로고    scopus 로고
    • The structure of microtubule-motor complexes
    • Amos, L.A., and Hirose, K. (1997). The structure of microtubule-motor complexes. Curr. Opin. Cell Biol. 9, 4-11.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 4-11
    • Amos, L.A.1    Hirose, K.2
  • 3
    • 0030266603 scopus 로고    scopus 로고
    • Three-dimensional structure of functional motor proteins on microtubules
    • Arnal, I., Metoz, F., DeBonis, S., and Wade, R.H. (1996). Three-dimensional structure of functional motor proteins on microtubules. Curr. Biol. 6, 1265-1270.
    • (1996) Curr. Biol. , vol.6 , pp. 1265-1270
    • Arnal, I.1    Metoz, F.2    DeBonis, S.3    Wade, R.H.4
  • 4
    • 0032518489 scopus 로고    scopus 로고
    • Nucleotide-dependent conformations of the kinesin dimer interacting with microtubules
    • Arnal, I., and Wade, R.H. (1998). Nucleotide-dependent conformations of the kinesin dimer interacting with microtubules. Structure 6, 33-38.
    • (1998) Structure , vol.6 , pp. 33-38
    • Arnal, I.1    Wade, R.H.2
  • 5
    • 0029914906 scopus 로고    scopus 로고
    • Weak and strong states of kinesin and ncd
    • Crevel, I.M.-T., Lockhart, A., and Cross, R.A. (1996). Weak and strong states of kinesin and ncd. J. Mol. Biol. 257, 66-76.
    • (1996) J. Mol. Biol. , vol.257 , pp. 66-76
    • Crevel, I.M.-T.1    Lockhart, A.2    Cross, R.A.3
  • 6
    • 0031260456 scopus 로고    scopus 로고
    • Molecular motors: The natural economy of kinesin
    • Cross, R.A. (1997). Molecular motors: the natural economy of kinesin. Curr. Biol. 7, R631-R633.
    • (1997) Curr. Biol. , vol.7
    • Cross, R.A.1
  • 7
    • 0025275327 scopus 로고
    • Mediation of meiotic and early mitotic chromosome segregation in Drosophila by a protein related to kinesin
    • Endow, S.A., Henikoff, S., and Soler Niedziela, L. (1990). Mediation of meiotic and early mitotic chromosome segregation in Drosophila by a protein related to kinesin. Nature 345, 81-83.
    • (1990) Nature , vol.345 , pp. 81-83
    • Endow, S.A.1    Henikoff, S.2    Soler Niedziela, L.3
  • 8
    • 0028985886 scopus 로고
    • Pathway of processive ATP hydrolysis by kinesin
    • Gilbert, S.P., Webb, M.R., Brune, M., and Johnson, K.A. (1995). Pathway of processive ATP hydrolysis by kinesin. Nature 373, 671-676.
    • (1995) Nature , vol.373 , pp. 671-676
    • Gilbert, S.P.1    Webb, M.R.2    Brune, M.3    Johnson, K.A.4
  • 9
    • 0027132479 scopus 로고
    • With apologies to scheherazade - Tails of 1001 kinesin motors
    • Goldstein, L.S.B. (1993). With apologies to Scheherazade - tails of 1001 kinesin motors. Annu. Rev. Genet. 27, 319-351.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 319-351
    • Goldstein, L.S.B.1
  • 10
    • 1542353988 scopus 로고
    • Kinesin ATPase: Rate-limiting ADP release
    • Hackney, D.D. (1988). Kinesin ATPase: rate-limiting ADP release. Proc. Natl. Acad. Sci. USA 85, 6314-6318.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6314-6318
    • Hackney, D.D.1
  • 11
    • 0028341667 scopus 로고
    • The rate-limiting step in microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains occurs while bound to the microtubule
    • Hackney, D.D. (1994). The rate-limiting step in microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains occurs while bound to the microtubule. J. Biol. Chem. 269, 16508-16511.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16508-16511
    • Hackney, D.D.1
  • 12
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa, N. (1998). Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 13
    • 0030930492 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: Structure, polarity and interaction with motor protein
    • Hirose, K., Amos, W.B., Lockhart, A., Cross, R.A., and Amos, L.A. (1997). Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: structure, polarity and interaction with motor protein. J. Struct. Biol. 118, 140-148.
    • (1997) J. Struct. Biol. , vol.118 , pp. 140-148
    • Hirose, K.1    Amos, W.B.2    Lockhart, A.3    Cross, R.A.4    Amos, L.A.5
  • 14
    • 0032079618 scopus 로고    scopus 로고
    • Nucleotide-dependent structural changes in dimeric ncd molecules complexed to microtubules
    • Hirose, K., Cross, R.A., and Amos, L.A. (1998). Nucleotide-dependent structural changes in dimeric ncd molecules complexed to microtubules. J. Mol. Biol. 278, 389-400.
    • (1998) J. Mol. Biol. , vol.278 , pp. 389-400
    • Hirose, K.1    Cross, R.A.2    Amos, L.A.3
  • 15
    • 0028979598 scopus 로고
    • Nucleotide-dependent angular change in kinesin motor domain bound to tubulin
    • Hirose, K., Lockhart, A., Cross, R.A., and Amos, L.A. (1995). Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Nature 376, 277-279.
    • (1995) Nature , vol.376 , pp. 277-279
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 16
    • 0029795642 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules
    • Hirose, K., Lockhart, A., Cross, R.A., and Amos, L.A. (1996). Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules. Proc. Natl. Acad. Sci. USA 93, 9539-9544.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9539-9544
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 17
    • 0031556947 scopus 로고    scopus 로고
    • Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry
    • Hoenger, A., and Milligan, R.A. (1997). Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry. J. Mol. Biol. 265, 553-564.
    • (1997) J. Mol. Biol. , vol.265 , pp. 553-564
    • Hoenger, A.1    Milligan, R.A.2
  • 19
    • 0032550175 scopus 로고    scopus 로고
    • Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with x-ray structure and implications for motility
    • Hoenger, A., Sack, S., Thormählen, M., Marx, A., Müller, J., Gross, H., and Mandelkow, E. (1998). Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: comparison with x-ray structure and implications for motility. J. Cell Biol. 141, 419-430.
    • (1998) J. Cell Biol. , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormählen, M.3    Marx, A.4    Müller, J.5    Gross, H.6    Mandelkow, E.7
  • 20
    • 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
  • 21
    • 0028979606 scopus 로고
    • 3-dimensional structure of the kinesin head-microtubule complex
    • Kikkawa, M., Ishikawa, T., Wakabayashi, T., and Hirokawa, N. (1995). 3-dimensional structure of the kinesin head-microtubule complex. Nature 376, 274-279.
    • (1995) Nature , vol.376 , pp. 274-279
    • Kikkawa, M.1    Ishikawa, T.2    Wakabayashi, T.3    Hirokawa, N.4
  • 22
    • 0032509950 scopus 로고    scopus 로고
    • A model of the microtubule-kinesin complex based on electron cryomicroscopy and x-ray crystallography
    • Kozielski, F., Arnal, I., and Wade, R.H. (1998). A model of the microtubule-kinesin complex based on electron cryomicroscopy and x-ray crystallography. Curr. Biol. 8, 191-198.
    • (1998) Curr. Biol. , vol.8 , pp. 191-198
    • Kozielski, F.1    Arnal, I.2    Wade, R.H.3
  • 24
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). Molscript - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull, F.J., Sablin, E.P., Lau, R., Fletterick, R.J., and Vale, R.D. (1996). Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380, 550-555.
    • (1996) Nature , vol.380 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 26
    • 0029012977 scopus 로고
    • Kinesin and ncd bind through a single head to microtubules and compete for a shared MT binding site
    • Lockhart, A., Crevel, I.M.-T.C., and Cross, R.A. (1995a). Kinesin and ncd bind through a single head to microtubules and compete for a shared MT binding site. J. Mol. Biol. 249, 763-771.
    • (1995) J. Mol. Biol. , vol.249 , pp. 763-771
    • Lockhart, A.1    Crevel, I.M.-T.C.2    Cross, R.A.3
  • 27
    • 0028040295 scopus 로고
    • Origins of reversed directionality in the ncd molecular motor
    • Lockhart, A., and Cross, R.A. (1994). Origins of reversed directionality in the ncd molecular motor. EMBO J. 13, 751-757.
    • (1994) EMBO J. , vol.13 , pp. 751-757
    • Lockhart, A.1    Cross, R.A.2
  • 28
    • 0029148759 scopus 로고
    • ADP release is the rate-limiting step of the MT activated ATPase of nonclaret disjunctional and kinesin
    • Lockhart, A., Cross, RA., and McKillop, D.F.A. (1995b). ADP release is the rate-limiting step of the MT activated ATPase of nonclaret disjunctional and kinesin. FEBS Lett. 368, 531-535.
    • (1995) FEBS Lett. , vol.368 , pp. 531-535
    • Lockhart, A.1    Cross, R.A.2    McKillop, D.F.A.3
  • 29
    • 0032966626 scopus 로고    scopus 로고
    • Structures of kinase and kinesin-microtubule interactions
    • Mandelkow, E., and Hoenger, A. (1999). Structures of kinase and kinesin-microtubule interactions. Curr. Opin. Cell Biol. 11, 34-44.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 34-44
    • Mandelkow, E.1    Hoenger, A.2
  • 30
    • 0030695901 scopus 로고    scopus 로고
    • Kinetic mechanism of monomeric nonclaret disjunctional protein (Ncd) ATPase
    • Pechatnikova, E., and Taylor, E.W. (1997). Kinetic mechanism of monomeric nonclaret disjunctional protein (Ncd) ATPase. J. Biol. Chem. 272, 30735-30740.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30735-30740
    • Pechatnikova, E.1    Taylor, E.W.2
  • 31
    • 0027211908 scopus 로고
    • Kinesin follows the microtubule's protofilament axis
    • Ray, S., Meyhöfer, E., Milligan, R.A., and Howard, J. (1993). Kinesin follows the microtubule's protofilament axis. J. Cell Biol. 121, 1083-1093.
    • (1993) J. Cell Biol. , vol.121 , pp. 1083-1093
    • Ray, S.1    Meyhöfer, E.2    Milligan, R.A.3    Howard, J.4
  • 33
    • 0029878485 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of the kinesin-related motor ncd
    • Sablin, E.P., Kull, F.J., Cooke, R., Vale, R.D., and Fletterick, R.J. (1996). Crystal structure of the motor domain of the kinesin-related motor ncd. Nature 380, 555-559.
    • (1996) Nature , vol.380 , pp. 555-559
    • Sablin, E.P.1    Kull, F.J.2    Cooke, R.3    Vale, R.D.4    Fletterick, R.J.5
  • 35
    • 0026755992 scopus 로고
    • A kinetic study of the kinesin ATPase
    • Sadhu, A., and Taylor, E.W. (1992). A kinetic study of the kinesin ATPase. J. Biol. Chem. 267, 11352-11359.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11352-11359
    • Sadhu, A.1    Taylor, E.W.2
  • 36
    • 0028838570 scopus 로고
    • Expression, purification, ATPase properties, and microtubule-binding properties of the ncd motor domain
    • Shimizu, T., Sablin, E., Vale, R.D., Fletterick, R., Pechatnikova, E., and Taylor, E.W. (1995). Expression, purification, ATPase properties, and microtubule-binding properties of the ncd motor domain. Biochemistry 34, 13259-13266.
    • (1995) Biochemistry , vol.34 , pp. 13259-13266
    • Shimizu, T.1    Sablin, E.2    Vale, R.D.3    Fletterick, R.4    Pechatnikova, E.5    Taylor, E.W.6
  • 37
    • 0028854634 scopus 로고
    • The anatomy of flagellar microtubules: Polarity, seam, junctions, and lattice
    • Song, Y.-H., and Mandelkow, E. (1995). The anatomy of flagellar microtubules: 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
  • 39
    • 0023644892 scopus 로고
    • Three-dimensional structure of the frozen-hydrated flagellar filament. The left-handed filament of Salmonella typhimurium
    • Trachtenberg, S., and DeRosier, D.J. (1987). Three-dimensional structure of the frozen-hydrated flagellar filament. The left-handed filament of Salmonella typhimurium. J. Mol. Biol. 195, 581-601.
    • (1987) J. Mol. Biol. , vol.195 , pp. 581-601
    • Trachtenberg, S.1    DeRosier, D.J.2
  • 41
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale, R.D., Reese, T.S., and Sheetz, M.P. (1985). Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42, 39-50.
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 43
    • 0024550571 scopus 로고
    • A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses
    • Yang, J.T., Laymon, R.A., and Goldstein, L.S.B. (1989). A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses. Cell 56, 879-889.
    • (1989) Cell , vol.56 , pp. 879-889
    • Yang, J.T.1    Laymon, R.A.2    Goldstein, L.S.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.