Nuclear pore complexes (NPCs) are very large proteinaceous assemblies that consist of more than 500 individual proteins1,2. NPCs are essential for nucleocytoplasmic transport of different cellular components, and disruption of the integrity of NPCs has been linked to aging, cancer and neurodegenerative diseases3-7. However, the mechanism by which membrane-embedded NPCs are turned over is currently unknown. Here we show that, after nitrogen starvation or genetic interference with the architecture of NPCs, nucleoporins are rapidly degraded in the budding yeast Saccharomyces cerevisiae. We demonstrate that NPC turnover involves vacuolar proteases and the core autophagy machinery. Autophagic degradation is mediated by the cytoplasmically exposed Nup159, which serves as intrinsic cargo receptor and directly binds to the autophagy marker protein Atg8. Autophagic degradation of NPCs is therefore inducible, enabling the removal of individual NPCs from the nuclear envelope.

中文翻译：

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选择性自噬可降解核孔复合物。

核孔复合物（NPC）是非常大的蛋白质组装体，由500多种单独的蛋白质1,2组成。NPC对于不同细胞成分的核质运输至关重要，NPC完整性的破坏与衰老，癌症和神经退行性疾病[3-7]有关。但是，目前还不清楚膜嵌入NPC翻转的机制。在这里，我们表明，在氮饥饿或遗传干扰NPC的结构后，核孢菌素在发芽酵母酿酒酵母中迅速降解。我们证明，全国人大营业额涉及液泡蛋白酶和核心自噬机制。自噬降解是由细胞质暴露的Nup159介导的，Nup159充当固有的货物受体，并直接结合自噬标记蛋白Atg8。