RanBP3 influences interactions between CRM1 and its nuclear protein export substrates

被引：84

作者：

Englmeier, L

Fornerod, M

Bischoff, FR

Petosa, C

Mattaj, IW

Kutay, U

机构：

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

[2] German Canc Res Ctr, Div Mol Biol Mitosis, D-69120 Heidelberg, Germany

[3] European Mol Biol Lab, Grenoble Outstn, F-38042 Grenoble, France

[4] Swiss Fed Inst Technol, Inst Biochem, CH-8092 Zurich, Switzerland

来源：

EMBO REPORTS | 2001年 / 2卷 / 10期

关键词：

D O I：

10.1093/embo-reports/kve200

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：

We investigated the role of RanBP3, a nuclear member of the Ran-binding protein 1 family, in CRM1-mediated protein export in higher eukaryotes. RanBP3 interacts directly with CRM1 and also forms a trimeric complex with CRM1 and RanGTP. However, RanBP3 does not bind to CRM1 like an export substrate. Instead, it can stabilize CRM1-export substrate interaction. Nuclear RanBP3 stimulates CRM1-dependent protein export in permeabilized cells. These data indicate that RanBP3 functions by a novel mechanism as a cofactor in recognition and export of certain CRM1 substrates. In vitro, RanBP3 binding to CRM1 affects the relative affinity of CRM1 for different substrates.

引用

页码：926 / 932

页数：7

共 32 条

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