Nuclear Import Mechanism of the EJC Component Mago-Y14 Revealed by Structural Studies of Importin 13

被引：53

作者：

Bono, Fulvia ^{[1
,2
]}

Cook, Atlanta G. ^{[1
]}

Gruenwald, Marlene ^{[2
]}

Ebert, Judith ^{[1
]}

Conti, Elena ^{[1
]}

机构：

[1] Max Planck Inst Biochem, Dept Struct Cell Biol, D-82152 Martinsried, Germany

[2] Max Planck Inst Dev Biol, D-72076 Tubingen, Germany

来源：

MOLECULAR CELL | 2010年 / 37卷 / 02期

关键词：

EXON-JUNCTION COMPLEX; CRYSTAL-STRUCTURE; CORE COMPLEX; EXPORT; RNA; RECOGNITION; TRANSPORT; PYM;

D O I：

10.1016/j.molcel.2010.01.007

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：

Mago, and Y14 are core components of the exon junction complex (EJC), an assembly central to nonsense-mediated mRNA decay in humans and mRNA localization in flies. The Mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm, where it functions in translational regulation. The heterodimer is imported back into the nucleus by Importin 13 (Imp13), a member of the karyopherin-beta family of transport factors. We have elucidated the structural basis of the Mago-Y14 nuclear import cycle. The 3.35 angstrom structure of the Drosophila Imp13-Mago-Y14 complex shows that Imp13 forms a ring-like molecule, reminiscent of Crm1, and encircles the Mago-Y14 cargo with a conserved interaction surface. The 2.8 angstrom structure of human Imp13 bound to RanGTP reveals how Mago-Y14 is released in the nucleus by a steric hindrance mechanism. Comparison of the two structures suggests how this unusual karyopherin might function in bidirectional nucleocytoplasmic transport.

引用

页码：211 / 222

页数：12

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