Kinesin and dynein superfamily proteins in organelle transport and cell division

Current Opinion in Cell Biology

Volumn 10, Issue 1, 1998, Pages 60-73

  Hirokawa, Nobutaka ^a   Noda, Yasuko ^a   Okada, Yasushi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; MICROTUBULE ASSOCIATED PROTEIN; MONOMER;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; CARBOXY TERMINAL SEQUENCE; CELL DIVISION; CELL ORGANELLE; CENTROSOME; CONTROLLED STUDY; GENETIC ENGINEERING; INTRACELLULAR TRANSPORT; MITOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN STRUCTURE; PROTEIN TRANSPORT; REVIEW;

ANIMALIA;

EID: 0032005975     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80087-2     Document Type: Article

References (98)

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76. Ma YZ, Taylor EW. Kinetic mechanism of a monomeric kinesin construct. of outstanding interest J Biol Chem. 272:1997;717-773 This article reports detailed analyses of the kinetics of a monomeric kinesin construct, which will be important as a basis for the interpretation of the kinetics of the dimeric kinesin holoenzyme.
77. Jiang W, Hackney DD. Monomeric kinesin head domains hydrolyze multiple ATP molecules before release from a microtubule. of outstanding interest J Biol Chem. 272:1997;5616-5621 The authors investigated transient kinetics of a monomeric kinesin construct similar to [76]. Unlike myosin, even monomeric kinesin showed weak processivity. A monomeric kinesin head was shown to hydrolyze 2-4 ATP molecules before dissociating from a microtubule by diffusion.
78. Ma YZ, Taylor EW. Interacting head mechanism of microtubule-kinesin ATPase. of special interest J Biol Chem. 272:1997;724-730 This paper reports the comparison of kinetic and equilibrium parameters of monomeric as compared to dimeric kinesin constructs. The main difference between the two was that the two heads of the dimer are not equivalent in their interaction with microtubules and substrates, which the authors consider to provide biochemical support for the 'walking model' of kinesin processivity.
79. bi(ratio), a parameter that refects the processivity, of monomeric and dimeric constructs were significantly different. The value of this parameter being more than 12-fold greater for dimers. This reflects a much stronger processivity of the dimeric form.
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87. Kull FJ, Sablin EP, Lau R, Fletterick RJ, Vale RD. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. of outstanding interest Nature. 380:1996;550-555 Here the authors report the crystal structure of the motor domain of conventional kinesin. Unexpectedly, it resembles that of myosin and G proteins. This structural similarity suggests that these molecules share common structural mechanisms.
88. Sablin EP, Kull FJ, Cooke R, Vale RD, Fletterick RJ. Crystal structure of the motor domain of the kinesin-related motor ncd. of outstanding interest Nature. 380:1996;555-559 This paper reports the determination of crystal structure of the motor domain of Ncd. Comparison of the crystal structures of Ncd and kinesin motor domains was expected to answer the question of why the two move in opposite directions. Quite unexpectedly, however, the two structures were almost identical. This suggests that all KIF motor domains could be, structurally, almost identical, and that the differences in their motile properties arise from domains outside the motor domain or from very small differences within the motor domain.
89. Wolf SG, Nogales E, Kikkawa M, Gratziner D, Hirokawa N, Downing KH. Interpreting a medium-resolution model of tubulin: comparison of zinc-sheet and microtubule structure. J Mol Biol. 262:1996;485-501.
90. Sosa H, Dias DP, Hoenger A, Whittaker M, Wilson-Kubalek E, Sablin E, Fletterick RJ, Vale RD, Milligan RA. A model for the microtubule-ncd motor protein complex obtained by cryoelectron microscopy and image analysis. Cell. 90:1997;217-224.
91. Woehike G, Ruby AK, Hart CL, Ly B, Hombooher N, Vale RD. Microtubule interaction site of the kinesin motor. of outstanding interest Cell. 90:1997;207-216 Using alanine scanning mutagenesis of the kinesin motor domain, the authors have found that amino acid residues which interact with microtubules are located in three loops that cluster in a patch on the motor surface (especially in the highly conserved loop and helix L12/α5). The critical residues are primarily positively charged, which is consistent with a primarily electrostatic interaction with the negatively charged domain(s) of the tubulin molecule.
92. Holmes KC. The swinging lever-arm hypothesis of muscle contraction. Curr Biol. 7:1997;R112-R118.
93. Vale RD. Switches, latches and amplifiers: common themes of G proteins and molecular motors. J Cell Biol. 135:1996;291-302.
94. Coppin CM, Pierce DW, Hsu L, Vale RD. The load dependence of kinesin's mechanical cycle. of special interest Proc Natl Acad Sci USA. 94:1997;8539-8544 The response of kinesin's motile behavior to the external force was measured in this study with a high-resolution optical trapping microscope. Kinesin does not go backwards under reverse loads up to 13pN (2-3 times greater than the stall load), while forward loads accelerate kinesin movement up to threefold.
95. Lockhart A, Cross RA. Origins of reversed directionality in the ncd molecular motor. EMBO J. 13:1994;751-757.
96. Case RB, Pierce DW, Hom-Booher N, Hart CL, Vale RD. The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain. of outstanding interest Cell. 98:1997;959-966 In this study, the motor domain of human conventional kinesin (β1-α6) was replaced with the corresponding domain of Ncd. This chimera showed a polarity characteristic of kinesin, while the velocity and the processivity were more reminiscent of Ncd.
97. Henningsen U, Schliwa M. Reversal in the direction of movement of a molecular motor. of outstanding interest Nature. 389:1997;93-96 This study is similar to that above [96], but the authors used Neurospora kinesin instead of human kinesin.
98. Stewart RJ, Thaler JP, Goldstein LS. Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein. Proc Natl Acad Sci USA. 90:1993;5209-5213.