Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly.

Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly.
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DOI:
10.1038/emboj.2012.256
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发表时间:
2012-10-17
期刊:
影响因子:
11.4
通讯作者:
Antonin, Wolfram
Antonin, Wolfram
中科院分区:
生物学1区
文献类型:
--
作者:
Vollmer, Benjamin;Schooley, Allana;Sachdev, Ruchika;Eisenhardt, Nathalie;Schneider, Anna M.;Sieverding, Cornelia;Madlung, Johannes;Gerken, Uwe;Macek, Boris;Antonin, Wolfram

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核孔复合体(NPC)将核膜(NE)的两层膜融合到一个孔中,连接细胞质和核质,并允许这些隔室之间的大分子交换。大多数NPC蛋白不包含完整的膜结构域,因此很大程度上还不清楚NPC是如何嵌入和锚定在NE中的。在这里,我们证明了进化保守的核孔蛋白Nup53独立于其他蛋白质与膜结合,这一性质对于NPC组装至关重要,并且在酵母和脊椎动物之间是保守的。脊椎动物蛋白包括两个膜结合位点,其中C-末端结构域具有膜变形能力,是从头组装NPC并在间期插入完整NE所必需的。Nup53的二聚化有助于其膜相互作用,并对其在NPC组装中的作用至关重要。
Nuclear pore complexes (NPCs) fuse the two membranes of the nuclear envelope (NE) to a pore, connecting cytoplasm and nucleoplasm and allowing exchange of macromolecules between these compartments. Most NPC proteins do not contain integral membrane domains and thus it is largely unclear how NPCs are embedded and anchored in the NE. Here, we show that the evolutionary conserved nuclear pore protein Nup53 binds independently of other proteins to membranes, a property that is crucial for NPC assembly and conserved between yeast and vertebrates. The vertebrate protein comprises two membrane binding sites, of which the C-terminal domain has membrane deforming capabilities, and is specifically required for de novo NPC assembly and insertion into the intact NE during interphase. Dimerization of Nup53 contributes to its membrane interaction and is crucial for its function in NPC assembly.
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