Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import

被引：94

作者：

Stewart, M ^{[1
]}

Baker, RP ^{[1
]}

Bayliss, R ^{[1
]}

Clayton, L ^{[1
]}

Grant, RP ^{[1
]}

Littlewood, T ^{[1
]}

Matsuura, Y ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

FEBS LETTERS | 2001年 / 498卷 / 2-3期

关键词：

nuclear trafficking; nucleoporin; molecular interaction; cell biology;

D O I：

10.1016/S0014-5793(01)02489-9

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 trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin-beta 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 beta een 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. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B,V, All rights reserved.

引用

页码：145 / 149

页数：5

共 55 条

[1] STRUCTURAL PLASTICITY OF THE NUCLEAR-PORE COMPLEX [J].