期刊
EMBO JOURNAL
卷 29, 期 20, 页码 3437-3447出版社
WILEY
DOI: 10.1038/emboj.2010.220
关键词
cryo-electron microscopy; crystallography; cytoskeleton regulation; kinesin; microtubule
资金
- BBSRC [BB/D008921]
- Wellcome Trust
- BBSRC [BB/D008921/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D008921/1] Funding Source: researchfish
Members of the kinesin-8 motor class have the remarkable ability to both walk towards microtubule plus-ends and depolymerise these ends on arrival, thereby regulating microtubule length. To analyse how kinesin-8 multitasks, we studied the structure and function of the kinesin-8 motor domain. We determined the first crystal structure of a kinesin-8 and used cryo-electron microscopy to calculate the structure of the microtubule-bound motor. Microtubule-bound kinesin-8 reveals a new conformation compared with the crystal structure, including a bent conformation of the alpha 4 relay helix and ordering of functionally important loops. The kinesin-8 motor domain does not depolymerise stabilised microtubules with ATP but does form tubulin rings in the presence of a non-hydro-lysable ATP analogue. This shows that, by collaborating, kinesin-8 motor domain molecules can release tubulin from microtubules, and that they have a similar mechanical effect on microtubule ends as kinesin-13, which enables depolymerisation. Our data reveal aspects of the molecular mechanism of kinesin-8 motors that contribute to their unique dual motile and depolymerising functions, which are adapted to control microtubule length. The EMBO Journal (2010) 29, 3437-3447. doi:10.1038/emboj.2010.220; Published online 3 September 2010 Subject Categories: cell & tissue architecture; structural biology
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据