ArticleMolecular and cellular biology2000
Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Architecture of the cytoplasmic face of the nuclear pore.Science (New York, N.Y.) · 2022Article
- Non-homologous End Joining-Mediated Insertional Mutagenesis Reveals a Novel Target for Enhancing Fatty Alcohols Production inFrontiers in microbiology · 2022Article
- A short linear motif in scaffold Nup145C connects Y-complex with pre-assembled outer ring Nup82 complex.Nature communications · 2017Article
- A Novel Saccharomyces cerevisiae FG Nucleoporin Mutant Collection for Use in Nuclear Pore Complex Functional Experiments.G3 (Bethesda, Md.) · 2015Article
- Linker Nups connect the nuclear pore complex inner ring with the outer ring and transport channel.Nature structural & molecular biology · 2015Article
- Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulations.Biophysical journal · 2014Article
- Nucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complex.Genetics · 2014Article
- Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata.Proteins · 2012Article
- The yeast nuclear pore complex and transport through it.Genetics · 2012Article
- 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
- Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport.Eukaryotic cell · 2009Review
- Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates.PLoS genetics · 2009Article
- Article
- Degradation of normal mRNA in the nucleus of Saccharomyces cerevisiae.Molecular and cellular biology · 2003Article
- Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes.Molecular biology of the cell · 2003Article
- Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating.Molecular and cellular biology · 2003Article
- In situ analysis of spatial relationships between proteins of the nuclear pore complex.Biophysical journal · 2002Article
- HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins.Molecular biology of the cell · 2001Article
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7 authors.
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Abstract
The yeast Saccharomyces cerevisiae nucleoporin Nup116p serves as a docking site for both nuclear import and export factors. However, the mechanism for assembling Nup116p into the nuclear pore complex (NPC) has not been resolved. By conducting a two-hybrid screen with the carboxy (C)-terminal Nup116p region as bait, we identified Nup82p. The predicted coiled-coil region of Nup82p was not required for Nup116p interaction, making the binding requirements distinct from those for the Nsp1p-Nup82p-Nup159p subcomplex (N. Belgareh, C. Snay-Hodge, F. Pasteau, S. Dagher, C. N. Cole, and V. Doye, Mol. Biol. Cell 9:3475-3492, 1998). Immunoprecipitation experiments using yeast cell lysates resulted in the coisolation of a Nup116p-Nup82p subcomplex. Although the absence of Nup116p had no effect on the NPC localization of Nup82p, overexpression of C-terminal Nup116p in a nup116 null mutant resulted in Nup82p mislocalization. Moreover, NPC localization of Nup116p was specifically diminished in a nup82-Delta108 mutant after growth at 37 degrees C. Immunoelectron microscopy analysis showed Nup116p was localized on both the cytoplasmic and nuclear NPC faces. Its distribution was asymmetric with the majority at the cytoplasmic face. Taken together, these results suggest that Nup82p and Nup116p interact at the cytoplasmic NPC face, with nucleoplasmic Nup116p localization utilizing novel binding partners.
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