The Mechanism of Nucleocytoplasmic Transport through the Nuclear Pore Complex

被引:33
作者
Tetenbaum-Novatt, J. [1 ]
Rout, M. P. [1 ]
机构
[1] Rockefeller Univ, Lab Cellular & Struct Biol, New York, NY 10065 USA
来源
NUCLEAR ORGANIZATION AND FUNCTION | 2010年 / 75卷
基金
美国国家卫生研究院;
关键词
MESSENGER-RNA EXPORT; PHENYLALANINE-GLYCINE NUCLEOPORINS; N-TERMINAL DOMAIN; FG-REPEAT DOMAINS; PROTEIN IMPORT; STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; LOCALIZATION SIGNALS; CRYSTAL-STRUCTURE; FUNCTIONAL-ANALYSIS;
D O I
10.1101/sqb.2010.75.033
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:567 / 584
页数:18
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