Davis L I
Department of Genetics, Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA.
Annu Rev Biochem. 1995;64:865-96. doi: 10.1146/annurev.bi.64.070195.004245.
The nuclear pore complex (NPC) creates an aqueous channel across the nuclear envelope through which macromolecular transport between nucleus and cytoplasm occurs. Nucleocytoplasmic traffic is bidirectional and involves diverse substrates, including protein and RNA. It is unclear whether import and export are mechanistically similar, but evidence suggests that numerous pathways may be involved. The discovery of filaments that extend out from each side of the NPC suggests that the NPC may also have a structural role, perhaps providing a connection between cytoskeletal elements of the nucleus and cytoplasm. If this suggestion is valid, it remains to be determined whether this aspect of NPC function is related to its role in nuclear transport. This review discusses recent developments regarding the structure of the NPC, characterization of its constituent proteins (nucleoporins), the mechanism by which transport occurs, the function of individual nucleoporins, and the pathway of NPC assembly and disassembly.
核孔复合体（NPC）在核膜上形成一个水性通道，通过该通道在细胞核和细胞质之间进行大分子运输。核质运输是双向的，涉及多种底物，包括蛋白质和RNA。目前尚不清楚输入和输出在机制上是否相似，但有证据表明可能涉及众多途径。从NPC两侧伸出的细丝的发现表明，NPC可能还具有结构作用，也许在细胞核和细胞质的细胞骨架成分之间提供连接。如果这一推测成立，NPC功能的这一方面是否与其在核运输中的作用相关仍有待确定。本综述讨论了关于NPC结构、其组成蛋白（核孔蛋白）的特性、运输发生的机制、单个核孔蛋白的功能以及NPC组装和拆卸途径的最新进展。
