Dissemin is shutting down on January 1st, 2025

Published in

Rockefeller University Press, Journal of Cell Biology, 3(208), p. 283-297, 2015

DOI: 10.1083/jcb.201411003

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 2015 by Monika Gaik ORCID, Dirk Flemming, Alexander von Appen, Panagiotis Kastritis ORCID, Norbert Mücke, Jessica Fischer, Philipp Stelter, Alessandro Ori ORCID, Khanh Huy Bui ORCID, Bui Kh, Jochen Baßler, Elisar Barbar, Martin Beck ORCID, Ed Hurt
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Red circle
Postprint: archiving forbidden
Green circle
Published version: archiving allowed
Upload
Policy details
Data provided by SHERPA/RoMEO

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.