Structure and Functional Role of Dynein's Microtubule-Binding Domain

被引：178

作者：

Carter, Andrew P. ^{[1
,2
]}

Garbarino, Joan E. ^{[3
]}

Wilson-Kubalek, Elizabeth M. ^{[4
]}

Shipley, Wesley E. ^{[3
]}

Cho, Carol ^{[1
,2
]}

Milligan, Ronald A. ^{[4
]}

Vale, Ronald D. ^{[1
,2
]}

Gibbons, I. R. ^{[3
]}

机构：

[1] Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94158 USA

[2] Univ Calif San Francisco, Dept Cellular & Mol Pharmacol, San Francisco, CA 94158 USA

[3] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[4] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA

来源：

SCIENCE | 2008年 / 322卷 / 5908期

关键词：

D O I：

10.1126/science.1164424

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule- binding domain ( MTBD) is separated from its ring- shaped AAA+ adenosine triphosphatase ( ATPase) domain by a 15- nanometer coiled- coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility.

引用

页码：1691 / 1695

页数：5

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