End-binding proteins (EBs) are widely viewed as master regulators of microtubule dynamics and function. Here, we show that while EB1 mediates the dynamic microtubule capture of herpes simplex virus type 1 (HSV-1) in fibroblasts, in neuronal cells, infection occurs independently of EBs through stable microtubules. Prompted by this, we find that transforming acid coiled-coil protein 3 (TACC3), widely studied in mitotic spindle formation, regulates the cytoplasmic localization of the microtubule polymerizing factor chTOG and influences microtubule plus-end dynamics during interphase to control infection in distinct cell types. Furthermore, perturbing TACC3 function in neuronal cells resulted in the formation of disorganized stable, detyrosinated microtubule networks and changes in cellular morphology, as well as impaired trafficking of both HSV-1 and transferrin. These trafficking defects in TACC3-depleted cells were reversed by the depletion of kinesin-1 heavy chains. As such, TACC3 is a critical regulator of interphase microtubule dynamics and stability that influences kinesin-1-based cargo trafficking.

中文翻译：

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TACC3调节相间细胞中微管的末端动力学和货物运输。

末端结合蛋白（EBs）被广泛视为微管动力学和功能的主要调节剂。在这里，我们显示，虽然EB1介导成纤维细胞中1型单纯疱疹病毒（HSV-1）的动态微管捕获，但在神经元细胞中，感染通过稳定的微管独立于EB发生。由此提示，我们发现在有丝分裂纺锤体形成中广泛研究的转化酸性卷曲螺旋蛋白3（TACC3）调节微管聚合因子chTOG的胞质定位并影响微管聚合反应的中期，以控制不同细胞中的感染类型。此外，扰动神经元细胞中的TACC3功能会导致杂乱无章的，稳定的，去酪氨酸化的微管网络的形成以及细胞形态的变化，以及HSV-1和转铁蛋白的贩运受损。TACC3耗尽的细胞中的这些运输缺陷被kinesin-1重链的消耗所逆转。因此，TACC3是相间微管动力学和稳定性的关键调节剂，会影响基于驱动蛋白1的货物运输。