Structure and Assembly of the Nuclear Pore Complex

被引:174
|
作者
Hampoelz, Bernhard [1 ]
Andres-Pons, Amparo [1 ,2 ]
Kastritis, Panagiotis [1 ,3 ]
Beck, Martin [1 ,4 ,5 ]
机构
[1] European Mol Biol Lab, Struct & Computat Biol Unit, D-69117 Heidelberg, Germany
[2] Friedrich Miescher Inst Biomed Res, CH-4058 Basel, Switzerland
[3] Martin Luther Univ Halle Wittenberg, ZIK HALOmem, D-06120 Halle, Saale, Germany
[4] European Mol Biol Lab, Cell Biol & Biophys Unit, D-69117 Heidelberg, Germany
[5] Max Planck Inst Biophys, D-60438 Frankfurt, Germany
来源
ANNUAL REVIEW OF BIOPHYSICS, VOL 48 | 2019年 / 48卷
基金
欧盟地平线“2020”; 欧洲研究理事会;
关键词
nuclear pore complex; NPC; nucleoporin; nuclear transport; NPC architecture; NPC assembly; MESSENGER-RNA; NUP107-160; COMPLEX; ATOMIC-STRUCTURE; GENE-REGULATION; INNER RING; DE-NOVO; ENVELOPE; PROTEIN; TRANSPORT; MEMBRANE;
D O I
10.1146/annurev-biophys-052118-115308
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Nuclear pore complexes (NPCs) mediate nucleocytoplasmic exchange. They are exceptionally large protein complexes that fuse the inner and outer nuclear membranes to form channels across the nuclear envelope. About 30 different protein components, termed nucleoporins, assemble in multiple copies into an intricate cylindrical architecture. Here, we review our current knowledge of the structure of nucleoporins and how those come together in situ. We delineate architectural principles on several hierarchical organization levels, including isoforms, posttranslational modifications, nucleoporins, and higher-order oligomerization of nucleoporin subcomplexes. We discuss how cells exploit this modularity to faithfully assemble NPCs.
引用
收藏
页码:515 / 536
页数:22
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