期刊
CELL
卷 138, 期 2, 页码 366-376出版社
CELL PRESS
DOI: 10.1016/j.cell.2009.04.065
关键词
-
资金
- Swiss National Science Foundation
- Netherlands Organization for Scientific Research
- Fundacao para a Ciencia e a Tecnologia
- FEBS
- ETH Zurich through the NCCR Structural Biology''
Microtubules are filamentous polymers essential for cell viability. Microtubule plus-end tracking proteins (+TIPs) associate with growing microtubule plus ends and control microtubule dynamics and interactions with different cellular structures during cell division, migration, and morphogenesis. EB1 and its homologs are highly conserved proteins that play an important role in the targeting of +TIPs to microtubule ends, but the underlying molecular mechanism remains elusive. By using live cell experiments and in vitro reconstitution assays, we demonstrate that a short polypeptide motif, Ser-x-Ile-Pro (SxIP), is used by numerous +TIPs, including the tumor suppressor APC, the transmembrane protein STIM1, and the kinesin MCAK, for localization to microtubule tips in an EB1-dependent manner. Structural and biochemical data reveal the molecular basis of the EB1-SxIP interaction and explain its negative regulation by phosphorylation. Our findings establish a general microtubule tip localization signal'' (MtLS) and delineate a unifying mechanism for this subcellular protein targeting process.
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