Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain
Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain
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DOI：
10.1093/emboj/18.7.1982
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发表时间：
1999-04-01
期刊：
影响因子：
11.4
通讯作者：
Dreyfuss, G
中科院分区：
文献类型：
--
作者：
Nakielny, S;Shaikh, S;Dreyfuss, G
我们利用噬菌体展示系统来寻找与转运蛋白1（TRN 1）相互作用的蛋白质，TRN 1是使具有M9核定位序列（NLS）的hnRNP蛋白穿梭的输入受体，并且在核孔蛋白Nup 153的N-末端内鉴定了与TRN 1结合的短区域，Nup 153位于核孔复合物（NPC）的核质面，在远端篮状结构中，并在mRNA输出中起作用。我们发现Nup 153的输入和输出受体都与Nup 153的几个区域相互作用，以RanGTP调节的方式，RanGTP解离Nup 153-输入受体复合物，但Nup 153-输出受体相互作用需要RanGTP。我们还发现Nup 153是一个RanGDP结合蛋白，并且这种相互作用是由Nup 153的锌指区域介导的，这代表了一个新的RanGDP结合结构域，我们称之为锌指RanGDP结合基序。我们提供了Nup 153穿梭于NPC的核和胞质表面之间的证据，Nup 153中存在M9穿梭结构域，连同其在NPC内移动并与输出受体相互作用的能力，表明该核孔蛋白是将输出货物运送到细胞质的孔的移动的组分。
We employed a phage display system to search for proteins that interact with transportin 1 (TRN1), the import receptor for shuttling hnRNP proteins with an M9 nuclear localization sequence (NLS), and identified a short region within the N-terminus of the nucleoporin Nup153 which binds TRN1, Nup153 is located at the nucleoplasmic face of the nuclear pore complex (NPC), in the distal basket structure, and functions in mRNA export. We show that this Nup153 TRN1-interacting region is an M9 NLS, We found that both import and export receptors interact with several regions of Nup153, in a RanGTP-regulated fashion, RanGTP dissociates Nup153-import receptor complexes, but is required for Nup153-export receptor interactions. We also show that Nup153 is a RanGDP-binding protein, and that the interaction is mediated by the zinc finger region of Nup153, This represents a novel Ran-binding domain, which we term the zinc finger Ran-binding motif, We provide evidence that Nup153 shuttles between the nuclear and cytoplasmic faces of the NPC, The presence of an M9 shuttling domain in Nup153, together with its ability to move within the NPC and to interact with export receptors, suggests that this nucleoporin is a mobile component of the pore which carries export cargos towards the cytoplasm.