ArticleThe Journal of cell biology2015
Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.
Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- RNA export through the nuclear pore complex: pathways, mechanisms, and imaging strategies.RNA biology · 2026Review
- Cooperative multivalency converts disorder into rods, resolving a paradox in cellular architecture.bioRxiv : the preprint server for biology · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- NUP214 in Acute Myeloid Leukemia.Cells · 2025Review
- Article
- Dynamic interactions of dimeric hub proteins underlie their diverse functions and structures: A comparative analysis of 14-3-3 and LC8.The Journal of biological chemistry · 2025Review
- Article
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- The Molecular Architecture of the Nuclear Basket.bioRxiv : the preprint server for biology · 2024Article
- Exploring Cellular Gateways: Unraveling the Secrets of Disordered Proteins within Live Nuclear Pores.Research square · 2024Article
- Implications of a multiscale structure of the yeast nuclear pore complex.Molecular cell · 2023Article
- Characterization of a novel interaction of the Nup159 nucleoporin with asymmetrically localized spindle pole body proteins and its link with autophagy.PLoS biology · 2023Article
- Cryo-EM structure of the fully assembled Elongator complex.Nucleic acids research · 2023Article
- Insights into the role of Nup62 and Nup93 in assembling cytoplasmic ring and central transport channel of the nuclear pore complex.Molecular biology of the cell · 2022Article
- 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.Protein & cell · 2022Article
- Architecture of the cytoplasmic face of the nuclear pore.Science (New York, N.Y.) · 2022Article
- Continuum dynamics and statistical correction of compositional heterogeneity in multivalent IDP oligomers resolved by single-particle EM.Journal of molecular biology · 2022Article
- Near-atomic structure of the inner ring of the Saccharomyces cerevisiae nuclear pore complex.Cell research · 2022Article
- Co-translational assembly orchestrates competing biogenesis pathways.Nature communications · 2022Article
- Article
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Authors and funding
13 authors.
Funding
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.
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