ArticleThe Journal of cell biology1995
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
60 citing papers in PubMed.
- Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.PLoS biology · 2025Article
- Overexpressed Nup88 stabilized through interaction with Nup62 promotes NF-κB dependent pathways in cancer.Frontiers in oncology · 2023Article
- Architecture of the cytoplasmic face of the nuclear pore.Science (New York, N.Y.) · 2022Article
- Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold.Science (New York, N.Y.) · 2022Article
- The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021Review
- Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis.Cell research · 2020Article
- Review
- A short linear motif in scaffold Nup145C connects Y-complex with pre-assembled outer ring Nup82 complex.Nature communications · 2017Article
- Systematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex.Molecular & cellular proteomics : MCP · 2016Article
- The Structure Inventory of the Nuclear Pore Complex.Journal of molecular biology · 2016Review
- Interactome Mapping Reveals the Evolutionary History of the Nuclear Pore Complex.PLoS biology · 2016Article
- Linker Nups connect the nuclear pore complex inner ring with the outer ring and transport channel.Nature structural & molecular biology · 2015Article
- Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.The Journal of cell biology · 2015Article
- Review
- The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Molecular biology of the cell · 2014Article
- The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1.The Journal of cell biology · 2013Article
- Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex.Journal of molecular biology · 2012Article
- The yeast nuclear pore complex and transport through it.Genetics · 2012Article
- Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex.The Journal of cell biology · 2011Article
- Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nsp1p interacts with nuclear pore proteins Nup49p, Nup57p and Nic96p in a stable complex which participates in nucleocytoplasmic transport. An additional p80 component is associated with Nsp1p, but does not co-purify with tagged Nup57p, Nup49p and Nic96p. The p80 gene was cloned and encodes a novel essential nuclear pore protein named Nup82p. Immunoprecipitation of tagged Nup82p reveals that it is physically associated with a fraction of Nsp1p which is distinct from Nsp1p found in a complex with Nup57p, Nic96p and Nup49p. The Nup82 protein can be divided into at least two different domains both required for the essential function, but it is only the carboxy-terminal domain, exhibiting heptad repeats, which binds to Nsp1p. Yeast cells depleted of Nup82p stop cell growth and concomitantly show a defect in poly(A)+RNA export, but no major alterations of nuclear envelope structure and nuclear pore density are seen by EM. This shows that Nsp1p participates in multiple interactions at the NPC and thus has the capability to physically interact with different NPC structures.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.