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J Cell Biol. 2015 Feb 2;208(3):283-97. doi: 10.1083/jcb.201411003.

Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.

Author information

1
Biochemistry Center of Heidelberg University, D-69120 Heidelberg, Germany.
2
Structural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.
3
Division of Biophysics of Macromolecules, German Center Research Center, D-69120 Heidelberg, Germany.
4
Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331.
5
Structural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany ed.hurt@bzh.uni-heidelberg.de martin.beck@embl.de.
6
Biochemistry Center of Heidelberg University, D-69120 Heidelberg, Germany ed.hurt@bzh.uni-heidelberg.de martin.beck@embl.de.

Abstract

Nuclear pore complexes (NPCs) are huge assemblies formed from ∼30 different nucleoporins, typically organized in subcomplexes. One module, the conserved Nup82 complex at the cytoplasmic face of NPCs, is crucial to terminate mRNA export. To gain insight into the structure, assembly, and function of the cytoplasmic pore filaments, we reconstituted in yeast the Nup82-Nup159-Nsp1-Dyn2 complex, which was suitable for biochemical, biophysical, and electron microscopy analyses. Our integrative approach revealed that the yeast Nup82 complex forms an unusual asymmetric structure with a dimeric array of subunits. Based on all these data, we developed a three-dimensional structural model of the Nup82 complex that depicts how this module might be anchored to the NPC scaffold and concomitantly can interact with the soluble nucleocytoplasmic transport machinery.

PMID:
25646085
PMCID:
PMC4315244
DOI:
10.1083/jcb.201411003
[Indexed for MEDLINE]
Free PMC Article

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