Hood Fiona E, Royle Stephen J
The Physiological Laboratory; University of Liverpool; Liverpool, UK.
Bioarchitecture. 2011 May;1(3):105-109. doi: 10.4161/bioa.1.3.16518.
Transforming acidic coiled coil 3 (TACC3) is a non-motor microtubule-associated protein (MAP) that is important for mitotic spindle stability and organization. The exact mechanism by which TACC3 acts at microtubules to stabilize the spindle has been unclear. However, several recent studies identified that the TACC3 complex at microtubules contains clathrin in addition to its previously identified binding partner, colonic and hepatic tumor overexpressed gene (ch-TOG). In this complex, phosphorylated TACC3 interacts directly with both ch-TOG and clathrin heavy chain, promoting accumulation of all complex members at the mitotic spindle. This complex stabilizes kinetochore fibers within the spindle by forming cross-bridges that link adjacent microtubules in these bundles. So, TACC3 is an adaptor that recruits ch-TOG and clathrin to mitotic microtubules, in an Aurora A kinase-regulated manner. In this mini-review we will describe the recent advances in the understanding of TACC 3 function and present a model that pulls together these new data with previous observations.
转化酸性卷曲螺旋蛋白3（TACC3）是一种非运动性微管相关蛋白（MAP），对有丝分裂纺锤体的稳定性和组织形成至关重要。TACC3在微管上发挥作用以稳定纺锤体的确切机制尚不清楚。然而，最近的几项研究发现，微管上的TACC3复合物除了其先前确定的结合伴侣结肠和肝肿瘤过表达基因（ch-TOG）外，还含有网格蛋白。在这个复合物中，磷酸化的TACC3直接与ch-TOG和网格蛋白重链相互作用，促进所有复合物成员在有丝分裂纺锤体上的积累。该复合物通过形成连接这些束中相邻微管的交叉桥来稳定纺锤体内的动粒纤维。因此，TACC3是一种衔接蛋白，以极光激酶A调节的方式将ch-TOG和网格蛋白募集到有丝分裂微管上。在这篇小型综述中，我们将描述对TACC3功能理解的最新进展，并提出一个将这些新数据与先前观察结果整合在一起的模型。
