TACC3-ch-TOG track the growing tips of microtubules independently of clathrin and Aurora-A phosphorylation.
TACC3-ch-TOG track the growing tips of microtubules independently of clathrin and Aurora-A phosphorylation.
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DOI：
10.1242/bio.201410843
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发表时间：
2015-01-16
期刊：
影响因子：
2.4
通讯作者：
Royle SJ
中科院分区：
文献类型：
--
作者：
Gutiérrez-Caballero C;Burgess SG;Bayliss R;Royle SJ
TACC 3（转化酸性卷曲螺旋蛋白3）和微管聚合酶ch-TOG（结肠，肝肿瘤过表达基因）之间的相互作用在进化上是保守的。将TACC 3-ch-TOG加载到有丝分裂纺锤体微管上需要TACC 3被Aurora-A激酶磷酸化，以及随后TACC 3与网格蛋白的相互作用以形成微管结合表面。最近的研究表明，TACC 3可以跟踪微管的正末端，并通过与ch-TOG的相互作用调节非分裂细胞中的微管动力学。在人类细胞中是否存在独立于网格蛋白的TACC 3-ch-TOG库，以及该库的功能是什么，都是悬而未决的问题。在这里，我们描述了TACC 3和ch-TOG之间的分子相互作用，允许TACC 3招聘到微管的正端。该TACC 3-ch-TOG库不依赖于EB 1、EB 3、Aurora-A磷酸化和与网格蛋白的结合。我们还描述了TACC 3，ch-TOG和网格蛋白的不同组合的亚细胞池。TACC 3通常被描述为一个中心体蛋白，但我们发现，有没有显着的人口TACC 3在中心体。不同蛋白池的描绘揭示了这些蛋白如何通过翻译后修饰来组织和控制的简化视图。
The interaction between TACC3 (transforming acidic coiled coil protein 3) and the microtubule polymerase ch-TOG (colonic, hepatic tumor overexpressed gene) is evolutionarily conserved. Loading of TACC3–ch-TOG onto mitotic spindle microtubules requires the phosphorylation of TACC3 by Aurora-A kinase and the subsequent interaction of TACC3 with clathrin to form a microtubule-binding surface. Recent work indicates that TACC3 can track the plus-ends of microtubules and modulate microtubule dynamics in non-dividing cells via its interaction with ch-TOG. Whether there is a pool of TACC3–ch-TOG that is independent of clathrin in human cells, and what is the function of this pool, are open questions. Here, we describe the molecular interaction between TACC3 and ch-TOG that permits TACC3 recruitment to the plus-ends of microtubules. This TACC3–ch-TOG pool is independent of EB1, EB3, Aurora-A phosphorylation and binding to clathrin. We also describe the distinct combinatorial subcellular pools of TACC3, ch-TOG and clathrin. TACC3 is often described as a centrosomal protein, but we show that there is no significant population of TACC3 at centrosomes. The delineation of distinct protein pools reveals a simplified view of how these proteins are organized and controlled by post-translational modification.