Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.
Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.
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DOI：
10.1083/jcb.200110082
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发表时间：
2002-01-07
期刊：
影响因子：
--
通讯作者：
Macara IG
中科院分区：
文献类型：
--
作者：
Brownawell AM;Macara IG
我们已经鉴定了一个新的人karyopherin（Kap）β家族成员，其与人Crm 1和酿酒酵母蛋白Msn 5 p/Kap 142 p相关。与其他已知的转运受体一样，这种Kap特异性结合RanGTP，与核孔蛋白相互作用，并在细胞核和细胞质区室之间穿梭。我们报告说，白细胞介素增强子结合因子（ILF）3，双链RNA结合蛋白，与此KAP在RanGTP依赖的方式，其双链RNA结合结构域（dsRBD）是这种相互作用所需的限制序列。重要的是，Kap与其他几种蛋白质中发现的dsRBD相互作用，并且结合被双链RNA阻断。我们发现ILF 3的dsRBD在完整细胞中作为一种新的核输出序列（内斯）发挥作用，并且其作为内斯的能力依赖于Kap的表达。在毛地黄皂苷透化的细胞中，Kap而不是Crm 1刺激ILF 3的核输出。基于该Kap介导dsRNA结合蛋白输出的能力，我们将该蛋白质命名为exportin-5。我们认为exportin-5不是RNA输出因子，而是参与dsRBD蛋白向细胞质的调节性易位，在细胞质中它们与靶mRNA相互作用。
We have identified a novel human karyopherin (Kap)β family member that is related to human Crm1 and the Saccharomyces cerevisiae protein, Msn5p/Kap142p. Like other known transport receptors, this Kap binds specifically to RanGTP, interacts with nucleoporins, and shuttles between the nuclear and cytoplasmic compartments. We report that interleukin enhancer binding factor (ILF)3, a double-stranded RNA binding protein, associates with this Kap in a RanGTP-dependent manner and that its double-stranded RNA binding domain (dsRBD) is the limiting sequence required for this interaction. Importantly, the Kap interacts with dsRBDs found in several other proteins and binding is blocked by double-stranded RNA. We find that the dsRBD of ILF3 functions as a novel nuclear export sequence (NES) in intact cells, and its ability to serve as an NES is dependent on the expression of the Kap. In digitonin-permeabilized cells, the Kap but not Crm1 stimulated nuclear export of ILF3. Based on the ability of this Kap to mediate the export of dsRNA binding proteins, we named the protein exportin-5. We propose that exportin-5 is not an RNA export factor but instead participates in the regulated translocation of dsRBD proteins to the cytoplasm where they interact with target mRNAs.
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