How Dynein Moves Along Microtubules

被引:109
作者
Bhabha, Gira [1 ,2 ]
Johnson, Graham T. [3 ,4 ]
Schroeder, Courtney M. [1 ,2 ]
Vale, Ronald D. [1 ,2 ]
机构
[1] Univ Calif San Francisco, Dept Cellular & Mol Pharmacol, San Francisco, CA 94143 USA
[2] Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94143 USA
[3] Univ Calif San Francisco, Dept Bioengn & Therapeut Sci, San Francisco, CA 94143 USA
[4] Univ Calif San Francisco, Calif Inst Quantitat Biosci QB3, San Francisco, CA 94143 USA
关键词
AAA PLUS RING; CRYSTAL-STRUCTURE; MITOTIC SPINDLE; MOTOR PROTEIN; COILED-COIL; MYOSIN-V; KINESIN; BINDING; DOMAIN; MECHANISM;
D O I
10.1016/j.tibs.2015.11.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cytoplasmic dynein, a member of the AAA (ATPases Associated with diverse cellular Activities) family of proteins, drives the processive movement of numerous intracellular cargos towards the minus end of microtubules. Here, we summarize the structural and motile properties of dynein and highlight features that distinguish this motor from kinesin-1 and myosin V, two well-studied transport motors. Integrating information from recent crystal and cryoelectron microscopy structures, as well as high-resolution single-molecule studies, we also discuss models for how dynein biases its movement in one direction along a microtubule track, and present a movie that illustrates these principles.
引用
收藏
页码:94 / 105
页数:12
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