A second tubulin binding site on the kinesin-13 motor head domain is important during mitosis.
A second tubulin binding site on the kinesin-13 motor head domain is important during mitosis.
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DOI：
10.1371/journal.pone.0073075
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Sosa H
中科院分区：
文献类型：
--
作者：
Zhang D;Asenjo AB;Greenbaum M;Xie L;Sharp DJ;Sosa H
驱动蛋白-13是微管（MT）解聚酶，不同于沿着MT移动的大多数其他驱动蛋白。与其他驱动蛋白一样，它们具有包含微管蛋白和ATP结合位点的运动或头部结构域（HD）。有趣的是，驱动蛋白-13在HD的相对侧具有另外的结合位点（Kin-Tub-2），其含有几个家族保守的带正电荷的残基。该位点在驱动蛋白-13功能中的作用尚不清楚。为了解决这一问题，我们研究了突变Kin-Tub-2家族保守残基对果蝇驱动蛋白13（KLP 10A）的体外和体内影响。我们发现Kin-Tub-2位点在体外增强了KLP 10A的微管蛋白交联和MT捆绑特性。破坏Kin-Tub-2位点，尽管对MT解聚没有有害影响，但在果蝇S2细胞有丝分裂期间导致异常的有丝分裂纺锤体和落后的染色体。结果表明，额外的Kin-Tub-2微管蛋白结合位点在体内起着直接的MT附着作用。
Kinesin-13s are microtubule (MT) depolymerases different from most other kinesins that move along MTs. Like other kinesins, they have a motor or head domain (HD) containing a tubulin and an ATP binding site. Interestingly, kinesin-13s have an additional binding site (Kin-Tub-2) on the opposite side of the HD that contains several family conserved positively charged residues. The role of this site in kinesin-13 function is not clear. To address this issue, we investigated the in-vitro and in-vivo effects of mutating Kin-Tub-2 family conserved residues on the Drosophila melanogaster kinesin-13, KLP10A. We show that the Kin-Tub-2 site enhances tubulin cross-linking and MT bundling properties of KLP10A in-vitro. Disruption of the Kin-Tub-2 site, despite not having a deleterious effect on MT depolymerization, results in abnormal mitotic spindles and lagging chromosomes during mitosis in Drosophila S2 cells. The results suggest that the additional Kin-Tub-2 tubulin biding site plays a direct MT attachment role in-vivo.
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