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通过核孔复合体进行核质运输的机制。

The mechanism of nucleocytoplasmic transport through the nuclear pore complex.

作者信息

Tetenbaum-Novatt J, Rout M P

机构信息

Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065, USA.

出版信息

Cold Spring Harb Symp Quant Biol. 2010;75:567-84. doi: 10.1101/sqb.2010.75.033. Epub 2011 Mar 29.

Abstract

The nuclear pore complex (NPC) mediates all transport between the nucleus and cytoplasm. Passage through the NPC is highly selective, yet the same channel must allow rapid specific transport of a wide range of cargoes. This chapter focuses mainly on the phenylalanine-glycine (FG) nucleoporins (nups), proteins carrying natively unfolded regions that are thought to form the selectively permeable barrier within the NPC. The physical properties of the FG nup barrier remain unclear. The high selectivity and rapidity of transport observed in vivo may be explained, in part, by competition for binding and space between transport factors and nontransported proteins. Future studies of FG nups will therefore also examine their interactions between FG nups and other proteins in their surroundings.

摘要

核孔复合体(NPC)介导细胞核与细胞质之间的所有物质运输。通过NPC的过程具有高度选择性,但同一通道必须允许多种货物进行快速且特定的运输。本章主要聚焦于苯丙氨酸-甘氨酸(FG)核孔蛋白(nups),这些蛋白质带有天然未折叠区域,被认为在NPC内形成选择性通透屏障。FG核孔蛋白屏障的物理性质仍不清楚。在体内观察到的运输的高选择性和快速性,部分可以通过运输因子与非运输蛋白之间对结合和空间的竞争来解释。因此,未来对FG核孔蛋白的研究也将考察它们与周围其他蛋白质之间的相互作用。

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