Sequential protein recruitment in C. elegans centriole formation
Sequential protein recruitment in C. elegans centriole formation
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DOI：
10.1016/j.cub.2006.07.059
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发表时间：
2006-09-19
期刊：
影响因子：
9.2
通讯作者：
Gonczy, Pierre
中科院分区：
文献类型：
--
作者：
Delattre, Marie;Canard, Coralie;Gonczy, Pierre
基于微管的中心粒的形成是一个知之甚少的过程，其对于中心体的复制至关重要，中心体是动物细胞的主要微管组织中心[1]。已鉴定出五种蛋白质是秀丽隐杆线虫中心粒形成所必需的：激酶ZYG-1，以及卷曲螺旋蛋白SAS-4、SAS-5、SAS-6和SPD-2 [2-9]。这些蛋白质之间的关系还不完全清楚，限制了对它们如何促进中心粒形成的理解。在这项研究中，我们建立了这五种蛋白质被招募到中心粒的顺序，并在早期工作的基础上进行了分子上位性实验。我们发现，SPD-2是加载第一，是需要的中心粒定位的其他四种蛋白质。ZYG-1的募集是必需的，其余三种蛋白定位到中心粒。SAS-5和SAS-6是随后征聘的，需要它们来维持最后纳入的SAS-4。我们的研究结果还表明，SAS-5和SAS-6的存在允许减少中心粒ZYG-1。此外，星状微管出现的中心粒招聘的所有五种蛋白质。这些蛋白质中有几个在其他后生动物中有同源物，我们希望我们的工作所产生的组装途径是保守的。
Formation of the microtubule-based centriole is a poorly understood process that is crucial for duplication of the centrosome, the principal microtubule-organizing center of animal cells [1]. Five proteins have been identified as being essential for centriole formation in Caenorhabditis elegans: the kinase ZYG-1, as well as the coiled-coil proteins SAS-4, SAS-5, SAS-6, and SPD-2 [2-9]. The relationship between these proteins is incompletely understood, limiting understanding of how they contribute to centriole formation. In this study, we established the order in which these five proteins are recruited to centrioles, and we conducted molecular epistasis experiments expanding on earlier work. We find that SPD-2 is loaded first and is needed for the centriolar localization of the four other proteins. ZYG-1 recruitment is required thereafter for the remaining three proteins to localize to centrioles. SAS-5 and SAS-6 are recruited next and are needed for the presence of SAS-4, which is incorporated last. Our results indicate in addition that the presence of SAS-5 and SAS-6 allows diminution of centriolar ZYG-1. Moreover, astral microtubules appear dispensable for the centriolar recruitment of all five proteins. Several of these proteins have homologs in other metazoans, and we expect the assembly pathway that stems from our work to be conserved.