Dissociation of nuclear import cargo complexes by the protein Ran: a fluorescence correlation spectroscopy study

被引:10
作者
Fradin, C
Zbaida, D
Elbaum, M
机构
[1] Dept Phys & Astron, Hamilton, ON L8S 4M1, Canada
[2] Dept Biochem & Biomed Sci, Hamilton, ON L8S 4M1, Canada
[3] Weizmann Inst Sci, Dept Mat & Interfaces, IL-76100 Rehovot, Israel
基金
加拿大自然科学与工程研究理事会; 以色列科学基金会;
关键词
nucleocytoplasmic transport; nuclear import; karyopherins; importins; nuclear localization signal; NLS; Ran; RanGTP; RanGDP; FCS;
D O I
10.1016/j.crvi.2005.10.003
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
In nucleated cells, proteins designed for nuclear import form complexes with soluble nuclear transport receptors prior to translocation across the nuclear envelope. The directionality of transport is due to the asymmetric distribution of the protein Ran, which dissociates import cargo complexes only in its nuclear RanGTP form. Using fluorescence correlation spectroscopy, we have studied the stability of cargo complexes in solution in the presence and in the absence of RanGTP. We find that RanGTP has a higher affinity for the major import receptor, the importin alpha/beta heterodimer, when importin alpha does not carry a cargo, suggesting that some nuclear transport targets might be preferentially released.
引用
收藏
页码:1073 / 1082
页数:10
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