Functions and mechanics of dynein motor proteins

被引:390
作者
Roberts, Anthony J. [1 ,2 ]
Kon, Takahide [3 ,4 ]
Knight, Peter J. [1 ]
Sutoh, Kazuo [5 ]
Burgess, Stan A. [1 ]
机构
[1] Univ Leeds, Fac Biol Sci, Sch Mol & Cellular Biol, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England
[2] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
[3] Hosei Univ, Fac Biosci & Appl Chem, Dept Frontier Biosci, Koganei, Tokyo 1848584, Japan
[4] Japan Sci & Technol Agcy, PRESTO, Kawaguchi, Saitama 3320012, Japan
[5] Waseda Univ, Fac Sci & Engn, Shinjuku Ku, Tokyo 1698555, Japan
基金
英国惠康基金; 英国生物技术与生命科学研究理事会; 日本科学技术振兴机构;
关键词
CYTOPLASMIC DYNEIN; MICROTUBULE-BINDING; MOLECULAR MOTORS; COILED-COIL; INTRAFLAGELLAR TRANSPORT; CONFORMATIONAL-CHANGES; KINETOCHORE DYNEIN; PROCESSIVE MOTION; CRYSTAL-STRUCTURE; ATPASE ACTIVITY;
D O I
10.1038/nrm3667
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division and intracellular transport. The large mass and complexity of dynein motors have made elucidating their mechanisms a sizable task. Yet, through a combination of approaches, including X-ray crystallography, cryo-electron microscopy, single-molecule assays and biochemical experiments, important progress has been made towards understanding how these giant motor proteins work. From these studies, a model for the mechanochemical cycle of dynein is emerging, in which nucleotide-driven flexing motions within the AAA+ ring of dynein alter the affinity of its microtubule-binding stalk and reshape its mechanical element to generate movement.
引用
收藏
页码:713 / 726
页数:14
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