Solution NMR assignment of the cryptic sixth TOG domain of mini spindles
Solution NMR assignment of the cryptic sixth TOG domain of mini spindles
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DOI：
10.1007/s12104-015-9620-4
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发表时间：
2015-10-01
影响因子：
0.9
通讯作者：
Pfuhl, Mark
中科院分区：
文献类型：
--
作者：
Burgess, Selena G.;Bayliss, Richard;Pfuhl, Mark
TOG结构域通过其结合微管蛋白的能力有助于微管的组织。它们存在于XMAP215蛋白家族成员中，作为微管聚合酶，在有丝分裂纺锤体的形成和着丝点纤维的组装中发挥重要作用。我们最近在XMAP215家族蛋白中发现了一个神秘的TOG结构域，chTOG及其果蝇同源物迷你纺锤体。这个结构域不是参与微管蛋白聚合的公认的TOG结构域的一部分。相反，它是TACC3家族蛋白结合位点的一部分。这种相互作用是在与网格蛋白的三聚体复合体中装配着丝点桥所必需的。在这里，我们提出了第一个核磁共振分配的第六个TOG结构域从微型纺锤体作为第一步，以阐明其结构和功能。
TOG domains contribute to the organisation of microtubules through their ability to bind tubulin. They are found in members of the XMAP215 family of proteins, which act as microtubule polymerases and fulfill important roles in the formation of the mitotic spindle and in the assembly of kinetochore fibres. We recently identified a cryptic TOG domain in the XMAP215 family proteins, chTOG and its Drosophila homologue, mini spindles. This domain is not part of the well-established array of TOG domains involved in tubulin polymerisation. Instead it forms part of a binding site for TACC3 family proteins. This interaction is required for the assembly of kinetochore bridges in a trimeric complex with clathrin. Here we present the first NMR assignment of a sixth TOG domain from mini spindles as a first step to elucidate its structure and function.