ArticleThe Journal of cell biology2009
Role of the Ndc1 interaction network in yeast nuclear pore complex assembly and maintenance.
Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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Who cites it
88 citing papers in PubMed, 155 citations in OpenAlex.
- Synaptonemal complex SUMOylation is maintained by Nup60-dependent docking of Ulp1 at the nuclear periphery.Cell reports · 2026Article
- The nuclear envelope protein TMEM209 is an integral component of the nuclear pore complex and interacts with Nup210.Journal of cell science · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Continuous nuclear envelope surveillance is required for DNA double strand break repair.Communications biology · 2025Article
- Cytoplasmic nucleoporin assemblage: the cellular artwork in physiology and disease.Nucleus (Austin, Tex.) · 2024Review
- Implications of a multiscale structure of the yeast nuclear pore complex.Molecular cell · 2023Article
- Article
- Nucleoporin foci are stress-sensitive condensates dispensable for C. elegans nuclear pore assembly.The EMBO journal · 2023Article
- Distinct domains in Ndc1 mediate its interaction with the Nup84 complex and the nuclear membrane.The Journal of cell biology · 2023Article
- Meiotic nuclear pore complex remodeling provides key insights into nuclear basket organization.The Journal of cell biology · 2023Article
- Uip4p modulates nuclear pore complex function inNucleus (Austin, Tex.) · 2022Article
- Article
- Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Review
- Co-translational assembly orchestrates competing biogenesis pathways.Nature communications · 2022Article
- Unexplored Cdc42 functions at the budding yeast nucleus suggested by subcellular localization.Small GTPases · 2022Article
- Review
- Characterization of nuclear pore complex targeting domains in Pom152 in Saccharomyces cerevisiae.Biology open · 2021Article
- One Ring to Rule them All? Structural and Functional Diversity in the Nuclear Pore Complex.Trends in biochemical sciences · 2021Review
28 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The nuclear pore complex (NPC) mediates all nucleocytoplasmic transport, yet its structure and biogenesis remain poorly understood. In this study, we have functionally characterized interaction partners of the yeast transmembrane nucleoporin Ndc1. Ndc1 forms a distinct complex with the transmembrane proteins Pom152 and Pom34 and two alternative complexes with the soluble nucleoporins Nup53 and Nup59, which in turn bind to Nup170 and Nup157. The transmembrane and soluble Ndc1-binding partners have redundant functions at the NPC, and disruption of both groups of interactions causes defects in Ndc1 targeting and in NPC structure accompanied by significant pore dilation. Using photoconvertible fluorescent protein fusions, we further show that the depletion of Pom34 in cells that lack NUP53 and NUP59 blocks new NPC assembly and leads to the reversible accumulation of newly made nucleoporins in cytoplasmic foci. Therefore, Ndc1 together with its interaction partners are collectively essential for the biosynthesis and structural integrity of yeast NPCs.
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