Promoting microtubule assembly: A hypothesis for the functional significance of the plus TIP network
Promoting microtubule assembly: A hypothesis for the functional significance of the plus TIP network
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DOI：
10.1002/bies.201400029
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发表时间：
2014-09-01
期刊：
影响因子：
4
通讯作者：
Goodson, Holly V.
中科院分区：
文献类型：
--
作者：
Gupta, Kamlesh K.;Alberico, Emily O.;Goodson, Holly V.
微管（MT）动力学的调节是许多细胞过程中必不可少的，但控制MT动力学的机制仍然知之甚少。MT+末端跟踪蛋白（+TIP）是一组MT相关蛋白，其动态跟踪生长的MT末端，并且独特地定位以控制MT动态。+ TIP在分子间和分子内相互作用的复杂阵列中相互关联，称为+TIP网络。为什么这么多+TIP绑定到其他+TIP？典型的答案包括这些相互作用将蛋白质定位在需要的地方，将蛋白质传递到皮层，和/或创建调节途径。我们提出了一个额外的和更机械的假设：+TIPs相互结合，以创建一个超结构，促进MT组装通过约束的MT尖端的结构波动，从而作为一个聚合伴侣。
Regulation of microtubule (MT) dynamics is essential for many cellular processes, but the machinery that controls MT dynamics remains poorly understood. MT plus-end tracking proteins (+TIPs) are a set of MT-associated proteins that dynamically track growing MT ends and are uniquely positioned to govern MT dynamics. +TIPs associate with each other in a complex array of inter-and intra-molecular interactions known as the +TIP network. Why do so many +TIPs bind to other +TIPs? Typical answers include the ideas that these interactions localize proteins where they are needed, deliver proteins to the cortex, and/or create regulatory pathways. We propose an additional and more mechanistic hypothesis: that +TIPs bind each other to create a superstructure that promotes MT assembly by constraining the structural fluctuations of the MT tip, thus acting as a polymerization chaperone.