Abstract：
SUMMARYCilia and the nucleus were two defining features of the last eukaryotic common ancestor. In early eukaryotic evolution, these structures evolved through the diversification of a common membrane-coating ancestor, the protocoatomer. While in cilia, the descendants of this protein complex evolved into parts of the intraflagellar transport complexes and BBSome, the nucleus gained its selectivity by recruiting protocoatomer-like proteins to the nuclear envelope to form the selective nuclear pore complexes. Recent studies show a growing number of proteins shared between the proteomes of the respective organelles, and it is currently unknown how ciliary transport proteins could acquire nuclear functions and vice versa. The nuclear functions of ciliary proteins are still observable today and remain relevant for the understanding of the disease mechanisms behind ciliopathies. In this work, we review the evolutionary history of cilia and nucleus and their respective defining proteins and integrate current knowledge into theories for early eukaryotic evolution. We postulate a scenario where both compartments co-evolved and that fits current models of eukaryotic evolution, explaining how ciliary proteins and nucleoporins acquired their dual functions.
摘要：
SUMNARYCilia和细胞核是最后一个真核共同祖先的两个定义特征。在早期的真核生物进化中,这些结构是通过共同的膜涂层祖先的多样化进化而来的，原型涂料。在纤毛中，这种蛋白质复合物的后代进化成步行内运输复合物和BBSome的一部分，核通过向核包膜募集原涂层体样蛋白以形成选择性核孔复合物来获得其选择性。最近的研究表明，越来越多的蛋白质在各个细胞器的蛋白质组之间共享，目前尚不清楚纤毛转运蛋白如何获得核功能，反之亦然。纤毛蛋白的核功能今天仍然可以观察到，并且仍然与了解纤毛病背后的疾病机制有关。在这项工作中,我们回顾了纤毛和细胞核的进化史以及它们各自定义的蛋白质，并将现有知识整合到早期真核生物进化的理论中。我们假设两个隔室共同进化并符合当前真核生物进化模型的情景，解释纤毛蛋白和核孔蛋白如何获得其双重功能。
