Leucine-rich nuclear-export signals:: born to be weak
Leucine-rich nuclear-export signals:: born to be weak
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DOI：
10.1016/j.tcb.2005.01.005
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发表时间：
2005-03-01
影响因子：
19
通讯作者：
Güttinger, S
中科院分区：
文献类型：
--
作者：
Kutay, U;Güttinger, S
CRM 1介导暴露富含亮氨酸的核输出信号（NES）的蛋白质的核输出。大多数NES以相对较低的亲和力与CRM 1结合。最近，从15-mer随机肽库中选择了更高亲和力的NES。出乎意料的是，高亲和力NES和CRM 1之间的复合物在核孔复合物（NPC）的细胞质丝处积累。这一发现表明，高亲和力的内斯结合CRM 1损害了输出复合物从NPC的有效释放，解释了为什么富含亮氨酸的NES已经进化为弱。
CRM1 mediates the nuclear export of proteins exposing leucine-rich nuclear-export signals (NESs). Most NESs bind to CRM1 with relatively low affinity. Recently, higher-affinity NESs were selected from a 15-mer random peptide library. Unexpectedly, complexes between high-affinity NESs and CRM1 accumulate at the cytoplasmic filaments of the nuclear pore complex (NPC). This finding suggests that high-affinity NES binding to CRM1 impairs the efficient release of export complexes from the NPC, explaining why leucine-rich NESs have evolved to be weak.