Phosphorylation by Cdk1 increases the binding of Eg5 to microtubules in vitro and in Xenopus egg extract spindles.
Phosphorylation by Cdk1 increases the binding of Eg5 to microtubules in vitro and in Xenopus egg extract spindles.
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DOI：
10.1371/journal.pone.0003936
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发表时间：
2008
期刊：
影响因子：
3.7
通讯作者：
Surrey, Thomas
中科院分区：
文献类型：
--
作者：
Cahu, Julie;Olichon, Aurelien;Hentrich, Christian;Schek, Henry;Drinjakovic, Jovana;Zhang, Cunjie;Doherty-Kirby, Amanda;Lajoie, Gilles;Surrey, Thomas
来自驱动蛋白5亚家族的马达蛋白在大多数生物的细胞分裂期间的纺锤体组装中起重要作用。这些马达使纺锤体中的微管交联并滑动。在有丝分裂过程中，驱动蛋白-5马达在保守位点被细胞周期蛋白依赖性激酶1（Cdk 1）磷酸化。非洲爪蟾驱动蛋白-5也被报道在体外被Aurora A磷酸化。我们在这里调查这些磷酸化对非洲爪蟾驱动蛋白-5（Eg 5）的影响。我们发现，磷酸化在苏氨酸937在C-末端尾部的Eg 5由Cdk 1不影响速度的Eg 5，但强烈地增加其结合到微管组装在缓冲液中。同样，这种磷酸化促进Eg 5与非洲爪蟾卵提取物纺锤体中微管的结合。这种结合的增强使纺锤体中Eg 5的量升高到双极纺锤体形成所需的临界水平以上。我们还发现，非洲爪蟾Eg 5的极光A在丝氨酸543在柄的磷酸化是不需要纺锤体的形成。这些结果表明，Cdk 1对Eg 5的磷酸化对该马达与微管的相互作用具有直接影响。在卵提取物中，Cdk 1对Eg 5的磷酸化确保纺锤体中Eg 5的量高于纺锤体形成所需的水平。因此，这种增强的纺锤体靶向似乎是，至少部分地，增强的结合Eg 5微管后，Cdk 1磷酸化的直接后果。这些发现推进了我们对这种必需的有丝分裂运动蛋白的调控的理解。
Motor proteins from the kinesin-5 subfamily play an essential role in spindle assembly during cell division of most organisms. These motors crosslink and slide microtubules in the spindle. Kinesin-5 motors are phosphorylated at a conserved site by Cyclin-dependent kinase 1 (Cdk1) during mitosis. Xenopus laevis kinesin-5 has also been reported to be phosphorylated by Aurora A in vitro. We investigate here the effect of these phosphorylations on kinesin-5 from Xenopus laevis, called Eg5. We find that phosphorylation at threonine 937 in the C-terminal tail of Eg5 by Cdk1 does not affect the velocity of Eg5, but strongly increases its binding to microtubules assembled in buffer. Likewise, this phosphorylation promotes binding of Eg5 to microtubules in Xenopus egg extract spindles. This enhancement of binding elevates the amount of Eg5 in spindles above a critical level required for bipolar spindle formation. We find furthermore that phosphorylation of Xenopus laevis Eg5 by Aurora A at serine 543 in the stalk is not required for spindle formation. These results show that phosphorylation of Eg5 by Cdk1 has a direct effect on the interaction of this motor with microtubules. In egg extract, phosphorylation of Eg5 by Cdk1 ensures that the amount of Eg5 in the spindle is above a level that is required for spindle formation. This enhanced targeting to the spindle appears therefore to be, at least in part, a direct consequence of the enhanced binding of Eg5 to microtubules upon phosphorylation by Cdk1. These findings advance our understanding of the regulation of this essential mitotic motor protein.
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人类TPX2是将极光-A激酶靶向纺锤体所必需的。
影响因子：
7.8
作者：
Kufer, Thomas A;Sillje, Herman H W;Korner, Roman;Gruss, Oliver J;Meraldi, Patrick;Nigg, Erich A
通讯作者：
Nigg, Erich A
DOI：
10.1083/jcb.118.1.109
发表时间：
1992-07
期刊：
The Journal of cell biology
影响因子：
--
作者：
Hoyt MA;He L;Loo KK;Saunders WS
通讯作者：
Saunders WS
影响因子：
9.2
作者：
Goshima, G;Wollman, R;Vale, RD
通讯作者：
Vale, RD
影响因子：
64.8
作者：
Kashina, AS;Baskin, RJ;Scholey, JM
通讯作者：
Scholey, JM
影响因子：
3.3
作者：
Goshima, G;Vale, RD
通讯作者：
Vale, RD