Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains

被引：34

作者：

Kuersten, S ^{[1
]}

Arts, GJ ^{[1
]}

Walther, TC ^{[1
]}

Englmeier, L ^{[1
]}

Mattaj, IW ^{[1
]}

机构：

[1] European Mol Biol Lab, Gene Express Programme, D-69117 Heidelberg, Germany

来源：

MOLECULAR AND CELLULAR BIOLOGY | 2002年 / 22卷 / 16期

关键词：

D O I：

10.1128/MCB.22.16.5708-5720.2002

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：

Vertebrate tRNA export receptor exportin-t (Xpo-t) binds to RanGTP and mature tRNAs cooperatively to form a nuclear export complex. Xpo-t shuttles bidirectionally through nuclear pore complexes (NPCs) but is mainly nuclear at steady state. The steady-state distribution of Xpo-t is shown to depend on its interaction with RanGTP. Two distinct Xpo-t NPC interaction domains that bind differentially to peripherally localized nucleoporins in vitro are identified. The N terminus binds to both Nup153 and RanBP2/Nup358 in a RanGTP-dependent manner, while the C terminus binds to CAN/Nup214 independently of Ran. We propose that these interactions increase the concentration of tRNA export complexes and of empty Xpo-t in the vicinity of NPCs and thus increase the efficiency of the Xpo-t transport cycle.

引用

页码：5708 / 5720

页数：13

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