Geometry of antiparallel microtubule bundles regulates relative sliding and stalling by PRC1 and Kif4A
Geometry of antiparallel microtubule bundles regulates relative sliding and stalling by PRC1 and Kif4A
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DOI：
10.7554/elife.32595
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发表时间：
2018-10-24
期刊：
影响因子：
7.7
通讯作者：
Subramanian, Radhika
中科院分区：
文献类型：
--
作者：
Wijeratne, Sithara;Subramanian, Radhika
马达和非马达交联蛋白在决定微管结构的大小和稳定性方面起着关键作用。目前，我们对微管阵列的几何性质如何反过来调节交联蛋白的输出的了解有限。在这里，我们在微管滑动的背景下研究这个问题，两个相互作用的蛋白质：非运动交联剂PRC1和Kinesin Kif4A。PRC1和Kif4A的集体活性也导致它们在微管正端(‘end-tag’)积累。当反平行微管上的末端标签碰撞时，滑动失速，形成稳定的重叠。有趣的是，我们发现初始阵列的结构属性通过PRC1-Kif4A调节微管组织。首先，滑动速度随初始微管重叠长度的增加而增大。其次，最终重叠的宽度随着微管长度的增加而变化。我们的分析揭示了反平行微管的微米级几何特征如何调节纳米级蛋白质的活性，以定义基于微管的结构和机制。
Motor and non-motor crosslinking proteins play critical roles in determining the size and stability of microtubule-based architectures. Currently, we have a limited understanding of how geometrical properties of microtubule arrays, in turn, regulate the output of crosslinking proteins. Here we investigate this problem in the context of microtubule sliding by two interacting proteins: the non-motor crosslinker PRC1 and the kinesin Kif4A. The collective activity of PRC1 and Kif4A also results in their accumulation at microtubule plus-ends ('end-tag'). Sliding stalls when the end-tags on antiparallel microtubules collide, forming a stable overlap. Interestingly, we find that structural properties of the initial array regulate microtubule organization by PRC1-Kif4A. First, sliding velocity scales with initial microtubule-overlap length. Second, the width of the final overlap scales with microtubule lengths. Our analyses reveal how micron-scale geometrical features of antiparallel microtubules can regulate the activity of nanometer-sized proteins to define the structure and mechanics of microtubule-based architectures.