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Reconstitution of a microtubule plus-end tracking system in vitro

机译：体外微管末端追踪系统的重建

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The microtubule cytoskeleton is essential to cell morphogenesis. Growing microtubule plus ends have emerged as dynamic regulatory sites in which specialized proteins, called plus-end-binding proteins (+TIPs), bind and regulate the proper functioning of microtubules. However, the molecular mechanism of plus-end association by +TIPs and their ability to track the growing end are not well understood. Here we report the in vitro reconstitution of a minimal plus-end tracking system consisting of the three fission yeast proteins Mal3, Tipl and the kinesin Tea2. Using time-lapse total internal reflection fluorescence microscopy, we show that the EB1 homologue Mal3 has an enhanced affinity for growing microtubule end structures as opposed to the microtubule lattice. This allows it to track growing microtubule ends autonomously by an end recognition mechanism. In addition, Mal3 acts as a factor that mediates loading of the processive motor Tea2 and its cargo, the Clip 170 homologue Tipl, onto the microtubule lattice. The interaction of all three proteins is required for the selective tracking of growing microtubule plus ends by both Tea2 and Tip1. Our results dissect the collective interactions of the constituents of this plus-end tracking system and show how these interactions lead to the emergence of its dynamic behaviour. We expect that such in vitro reconstitutions will also be essential for the mechanistic dissection of other plus-end tracking systems.
机译：微管细胞骨架对细胞形态发生至关重要。越来越多的微管正末端已成为动态调控位点，在该位点，称为正末端结合蛋白（+ TIP）的特殊蛋白质会结合并调控微管的正常功能。然而，人们还不太了解+ TIP进行正向末端缔合的分子机制及其追踪生长末端的能力。在这里，我们报告了由三个裂变酵母蛋白Mal3，Tip1和驱动蛋白Tea2组成的最小末端追踪系统的体外重组。使用延时全内反射荧光显微镜，我们显示EB1同源Mal3具有增强的亲和力，与微管晶格相反，用于生长微管末端结构。这允许它通过末端识别机制自动跟踪生长的微管末端。此外，Mal3充当介导过程马达Tea2及其货物Clip 170同源物Tipl加载到微管网格上的因素。 Tea2和Tip1选择性跟踪生长中的微管和末端需要这三种蛋白质的相互作用。我们的研究结果剖析了这种高端跟踪系统的组成部分的集体相互作用，并显示了这些相互作用如何导致其动态行为的出现。我们期望这种体外重构对于其他正负追踪系统的机械解剖也必不可少。

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