Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end-binding microtubule destabilizer.
Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end-binding microtubule destabilizer.
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DOI：
10.1083/jcb.200211097
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发表时间：
2003-04-28
期刊：
影响因子：
--
通讯作者：
Hyman A
中科院分区：
文献类型：
--
作者：
van Breugel M;Drechsel D;Hyman A
从酵母到哺乳动物都保守的微管相关蛋白 Dis1/XMAP215 家族对于细胞分裂至关重要。 XMAP215 是该家族的非洲爪蟾成员，已被证明可以在体外稳定微管，但该家族的其他成员尚未得到生化特征。在这里，我们研究了酿酒酵母同源物 Stu2p 的体外特性。令人惊讶的是，Stu2p 是一种微管去稳定剂，优先与微管正端结合。微管动力学的定量分析表明，Stu2p 通过空间干扰微管蛋白添加到微管末端而引发微管灾难。这些结果揭示了 Dis1/XMAP215 家族成员的新生化活性和微管不稳定的新机制。
The Dis1/XMAP215 family of microtubule-associated proteins conserved from yeast to mammals is essential for cell division. XMAP215, the Xenopus member of this family, has been shown to stabilize microtubules in vitro, but other members of this family have not been biochemically characterized. Here we investigate the properties of the Saccharomyces cerevisiae homologue Stu2p in vitro. Surprisingly, Stu2p is a microtubule destabilizer that binds preferentially to microtubule plus ends. Quantitative analysis of microtubule dynamics suggests that Stu2p induces microtubule catastrophes by sterically interfering with tubulin addition to microtubule ends. These results reveal both a new biochemical activity for a Dis1/XMAP215 family member and a novel mechanism for microtubule destabilization.
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