Human mRNA export machinery recruited to the 5′ end of mRNA
Human mRNA export machinery recruited to the 5′ end of mRNA
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DOI：
10.1016/j.cell.2006.10.044
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发表时间：
2006-12-29
期刊：
影响因子：
64.5
通讯作者：
Reed, Robin
中科院分区：
文献类型：
--
作者：
Cheng, Hong;Dufu, Kobina;Reed, Robin
前体mRNA经历剪接以去除内含子，并且剪接的mRNA被输出到细胞质用于翻译。在这里，我们研究了保守的mRNA输出机制（TREX复合物）的mRNA的招聘机制。我们表明，人TREX复合物被募集到mRNA的5'端附近的区域，其中TREX组分Aly最接近5'帽结合。TREX募集和mRNA输出都需要帽，并且帽的这些作用是剪接依赖性的。与帽结合的CBP 80有效地与TREX缔合，并且Aly介导这种相互作用。总之，这些数据表明，CBP 80-Aly相互作用导致TREX募集到mRNA的5'端，在那里它在mRNA输出中起作用。因此，mRNA将通过核孔以5'至3'方向输出，如在巨大Balbiani环mRNP的早期电子显微照片中所观察到的。
Pre-mRNAs undergo splicing to remove introns, and the spliced mRNA is exported to the cytoplasm for translation. Here we investigated the mechanism for recruitment of the conserved mRNA export machinery (TREX complex) to mRNA. We show that the human TREX complex is recruited to a region near the 5' end of mRNA, with the TREX component Aly bound closest to the 5' cap. Both TREX recruitment and mRNA export require the cap, and these roles for the cap are splicing dependent. CBP80, which is bound to the cap, associates efficiently with TREX, and Aly mediates this interaction. Together, these data indicate that the CBP80-Aly interaction results in recruitment of TREX to the 5' end of mRNA, where it functions in mRNA export. As a consequence, the mRNA would be exported in a 5' to 3' direction through the nuclear pore, as observed in early electron micrographs of giant Balbiani ring mRNPs.