Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import
Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import
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DOI：
10.1016/s0014-5793(01)02489-9
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发表时间：
2001-06
期刊：
影响因子：
3.5
通讯作者：
M. Stewart;R. Baker;R. Bayliss;L. Clayton;R. Grant;T. Littlewood;Y. Matsuura
中科院分区：
文献类型：
--
作者：
M. Stewart;R. Baker;R. Bayliss;L. Clayton;R. Grant;T. Littlewood;Y. Matsuura
大分子通过核孔复合物在细胞质和细胞核之间的运输是由特定的载体分子（例如输入蛋白-β家族的成员）介导的。核孔蛋白（核孔蛋白）经常包含基于 FG 核心的序列重复，并且载体似乎通过在连续的 FG 核心之间跳跃来将其货物移动通过孔。一个主要问题是为什么有些大分子可以运输，而另一些则不能。这种选择性可能是由结合 FG 重复序列的能力、孔通道入口附近载体-货物复合物的局部浓度以及通道中高浓度核孔蛋白产生的空间位阻产生的。
The trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin-β family. Nuclear pore proteins (nucleoporins) frequently contain sequence repeats based on FG cores and carriers appear to move their cargo through the pores by hopping between successive FG cores. A major question is why some macromolecules are transported while others are not. This selectivity may be generated by the ability to bind FG repeats, a local concentration of carrier–cargo complexes near the entrance to the pore channel, and steric hindrance produced by high concentrations of nucleoporins in the channel.