Dynein and kinesin share an overlapping microtubule-binding site
Dynein and kinesin share an overlapping microtubule-binding site
复制标题
DOI：
10.1038/sj.emboj.7600240
复制
发表时间：
2004-07-07
期刊：
影响因子：
11.4
通讯作者：
Kikkawa, M
中科院分区：
文献类型：
--
作者：
Mizuno, N;Toba, S;Kikkawa, M
Dyneins and kinesins move in opposite directions on microtubules. The question of how the same-track microtubules are able to support movement in two directions remains unanswered due to the absence of details on dynein-microtubule interactions. To address this issue, we studied dynein-microtubule interactions using the tip of the microtubule-binding stalk, the dynein stalk head (DSH), which directly interacts with microtubules upon receiving conformational change from the ATPase domain. Biochemical and cryo-electron microscopic studies revealed that DSH bound to tubulin dimers with a periodicity of 80 A, corresponding to the step size of dyneins. The DSH molecule was observed as a globular corn grain-like shape that bound the same region as kinesin. Biochemical crosslinking experiments and image analyses of the DSH-kinesin head-microtubule complex revealed competition between DSH and the kinesin head for microtubule binding. Our results demonstrate that dynein and kinesin share an overlapping microtubule-binding site, and imply that binding at this site has an essential role for these motor proteins.
