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首页> 外文期刊>Journal of Molecular Biology >Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex
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Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex

机译：原蛋白Nup98锚定到核孔复合体的细胞质表面的分子基础

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The cytoplasmic filament nucleoporins of the nuclear pore complex (NPC) are critically involved in nuclear export and remodeling of mRNA ribonucleoprotein particles and are associated with various human malignancies. Here, we report the crystal structure of the Nup98 C-terminal autoproteolytic domain, frequently missing from leukemogenic forms of the protein, in complex with the N-terminal domain of Nup82 and the C-terminal tail fragment of Nup159. The Nup82 β propeller serves as a noncooperative binding platform for both binding partners. Interaction of Nup98 with Nup82 occurs through a reciprocal exchange of loop structures. Strikingly, the same Nup98 groove promiscuously interacts with Nup82 and Nup96 in a mutually excusive fashion. Simultaneous disruption of both Nup82 interactions in yeast causes severe defects in mRNA export, while the severing of a single interaction is tolerated. Thus, the cytoplasmic filament network of the NPC is robust, consistent with its essential function in nucleocytoplasmic transport.
机译：核孔复合体（NPC）的胞质细丝核孔蛋白与mRNA核糖核蛋白颗粒的核输出和重塑密切相关，并且与各种人类恶性肿瘤相关。在这里，我们报道了Nup98 C端自蛋白水解域的晶体结构，该蛋白经常从蛋白质的致白血病形式中缺失，与Nup82的N端域和Nup159的C端尾部片段复合。 Nup82β螺旋桨是两个结合伴侣的非合作结合平台。 Nup98与Nup82的相互作用通过相互交换环结构而发生。引人注目的是，同一Nup98凹槽以相互排斥的方式与Nup82和Nup96混杂地相互作用。酵母中两个Nup82相互作用的同时破坏会导致mRNA输出的严重缺陷，同时允许单个相互作用的切断。因此，NPC的细胞质细丝网络很健壮，与其在核质运输中的基本功能相一致。

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