Peters Reiner
Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065 , USA.
Bioessays. 2009 Apr;31(4):466-77. doi: 10.1002/bies.200800159.
Transport through the nuclear pore complex (NPC), a keystone of the eukaryotic building plan, is known to involve a large channel and an abundance of phenylalanine-glycine (FG) protein domains serving as binding sites for soluble nuclear transport receptors and their cargo complexes. However, the conformation of the FG domains in vivo, their arrangement in relation to the transport channel and their function(s) in transport are still vividly debated. Here, we revisit a number of representative transport models-specifically Brownian affinity gating, selective phase gating, reversible FG domain collapse, and reduction of dimensionality (ROD)-in the light of new data obtained by optical single transporter recording, optical superresolution microscopy, artificial nanopores, and many other techniques. The analysis suggests that a properly adapted, simplified version of the ROD model accounts well for the available data. This has implications for nucleocytoplasmic transport in general.
通过核孔复合体（NPC）的运输是真核生物构建计划的关键环节，已知其涉及一个大通道以及大量苯丙氨酸-甘氨酸（FG）蛋白结构域，这些结构域作为可溶性核转运受体及其货物复合体的结合位点。然而，FG结构域在体内的构象、它们相对于运输通道的排列以及它们在运输中的功能仍存在激烈争论。在此，我们根据通过光学单转运体记录、光学超分辨率显微镜、人工纳米孔及许多其他技术获得的新数据，重新审视一些具有代表性的运输模型，特别是布朗亲和门控、选择性相门控、可逆FG结构域塌陷和维度降低（ROD）模型。分析表明，经过适当调整的简化版ROD模型能够很好地解释现有数据。这对一般的核质运输具有重要意义。
