Co-translational assembly and localized translation of nucleoporins in nuclear pore complex biogenesis
Co-translational assembly and localized translation of nucleoporins in nuclear pore complex biogenesis
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DOI：
10.1016/j.molcel.2021.03.030
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发表时间：
2021-06-03
期刊：
影响因子：
16
通讯作者：
Palancade, Benoit
中科院分区：
文献类型：
--
作者：
Lautier, Ophelie;Penzo, Arianna;Palancade, Benoit
mRNA的翻译与细胞质中的多蛋白复合物组装或蛋白质递送到细胞内隔室有关。在这里，通过结合酵母中系统的RNA免疫沉淀和单分子RNA成像，我们已经提供了一个完整的描述，涉及一个大的多蛋白组装，核孔复合物（NPC）的生物发生的共翻译事件。我们报道在翻译过程中，在细胞质中可以建立NPC亚基之间的二元相互作用。引人注目的是，核孔蛋白Nup1/Nup2与许多核蛋白一起，通过一种涉及其新生n端和核转运受体之间相互作用的机制，在核孔中进行翻译。解耦这种共翻译招募进一步触发了未组装多肽的细胞质灶的形成。总之，我们的数据表明，不同的、空间分离的共翻译相互作用模式促进了NPC亚基的有序组装，并且局部翻译可以确保蛋白质正确地递送到孔和细胞核。
mRNA translation is coupled to multiprotein complex assembly in the cytoplasm or to protein delivery into intracellular compartments. Here, by combining systematic RNA immunoprecipitation and single-molecule RNA imaging in yeast, we have provided a complete depiction of the co-translational events involved in the biogenesis of a large multiprotein assembly, the nuclear pore complex (NPC). We report that binary interactions between NPC subunits can be established during translation, in the cytoplasm. Strikingly, the nucleoporins Nup1/Nup2, together with a number of nuclear proteins, are instead translated at nuclear pores, through a mechanism involving interactions between their nascent N-termini and nuclear transport receptors. Uncoupling this co-translational recruitment further triggers the formation of cytoplasmic foci of unassembled polypeptides. Altogether, our data reveal that distinct, spatially segregated modes of co-translational interactions foster the ordered assembly of NPC subunits and that localized translation can ensure the proper delivery of proteins to the pore and the nucleus.