人类PLK4和STIL之间关键的中心粒组装相互作用界面在果蝇中似乎并不保守。
A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies.
作者信息
Cottee Matthew A, Johnson Steven, Raff Jordan W, Lea Susan M
机构信息
Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK
出版信息
Biol Open. 2017 Mar 15;6(3):381-389. doi: 10.1242/bio.024661.
A small number of proteins form a conserved pathway of centriole duplication. In humans and flies, the binding of PLK4/Sak to STIL/Ana2 initiates daughter centriole assembly. In humans, this interaction is mediated by an interaction between the Polo-Box-3 (PB3) domain of PLK4 and the coiled-coil domain of STIL (HsCCD). We showed previously that the Ana2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramer that likely precludes an interaction with PB3. Here, we show that the isolated HsCCD and HsPB3 domains form a mixture of homo-multimers , but these readily dissociate when mixed to form the previously described 1:1 HsCCD:HsPB3 complex. In contrast, although PB3 (DmPB3) adopts a canonical polo-box fold, it does not detectably interact with DmCCD Thus, surprisingly, a key centriole assembly interaction interface appears to differ between humans and flies.
少数蛋白质构成了一个保守的中心粒复制途径。在人类和果蝇中，PLK4/Sak与STIL/Ana2的结合启动了子中心粒的组装。在人类中，这种相互作用是由PLK4的Polo-Box-3（PB3）结构域与STIL的卷曲螺旋结构域（HsCCD）之间的相互作用介导的。我们之前表明，Ana2卷曲螺旋结构域（DmCCD）对中心粒组装至关重要，但它形成了一个紧密的平行四聚体，这可能排除了与PB3的相互作用。在这里，我们表明，分离的HsCCD和HsPB3结构域形成了同多聚体的混合物，但当混合形成先前描述的1:1 HsCCD:HsPB3复合物时，它们很容易解离。相比之下，尽管PB3（DmPB3）采用了典型的polo-box折叠，但它与DmCCD没有可检测到的相互作用。因此，令人惊讶的是，人类和果蝇之间一个关键的中心粒组装相互作用界面似乎有所不同。
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