ArticleProceedings of the National Academy of Sciences of the United States of America2018
Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed, 90 citations in OpenAlex.
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- Super-Resolution Imaging of Nuclear Pore Responses to Mechanical Stress and Energy Depletion.Viruses · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Kap-centric Nsp1-mediated nuclear transport at full amino acid resolution.Nature communications · 2025Article
- CHMP2B promotes CHMP7 mediated nuclear pore complex injury in sporadic ALS.Acta neuropathologica communications · 2024Article
- Nuclear pore and nucleocytoplasmic transport impairment in oxidative stress-induced neurodegeneration: relevance to molecular mechanisms in Pathogenesis of Parkinson's and other related neurodegenerative diseases.Molecular neurodegeneration · 2024Review
- Docking a flexible basket onto the core of the nuclear pore complex.Nature cell biology · 2024Article
- The nuclear pore Y-complex functions as a platform for transcriptional regulation of FLOWERING LOCUS C in Arabidopsis.The Plant cell · 2024Article
- Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.Nature communications · 2024Article
- Nuclear pore complexes mediate subtelomeric gene silencing by regulating PCNA levels on chromatin.The Journal of cell biology · 2023Article
- Intracellular Amyloid-β Detection from Human Brain Sections Using a Microfluidic Immunoassay in Tandem with MALDI-MS.Analytical chemistry · 2023Article
- Digital nanoreactors to control absolute stoichiometry and spatiotemporal behavior of DNA receptors within lipid bilayers.Nature communications · 2023Article
- Improving the secretion of designed protein assemblies through negative design of cryptic transmembrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A library of sensitive position-specific scoring matrices for high-throughput identification of nuclear pore complex subunits.NAR genomics and bioinformatics · 2023Article
- Uip4p modulates nuclear pore complex function inNucleus (Austin, Tex.) · 2022Article
- Article
- Nuclear mRNA metabolism drives selective basket assembly on a subset of nuclear pore complexes in budding yeast.Molecular cell · 2022Article
- Percolation transition prescribes protein size-specific barrier to passive transport through the nuclear pore complex.Nature communications · 2022Article
- Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear pore complex (NPC) is an eightfold symmetrical channel providing selective transport of biomolecules across the nuclear envelope. Each NPC consists of ∼30 different nuclear pore proteins (Nups) all present in multiple copies per NPC. Significant progress has recently been made in the characterization of the vertebrate NPC structure. However, because of the estimated size differences between the vertebrate and yeast NPC, it has been unclear whether the NPC architecture is conserved between species. Here, we have developed a quantitative image analysis pipeline, termed nuclear rim intensity measurement (NuRIM), to precisely determine copy numbers for almost all Nups within native NPCs of budding yeast cells. Our analysis demonstrates that the majority of yeast Nups are present at most in 16 copies per NPC. This reveals a dramatic difference to the stoichiometry determined for the human NPC, suggesting that despite a high degree of individual Nup conservation, the yeast and human NPC architecture is significantly different. Furthermore, using NuRIM, we examined the effects of mutations on NPC stoichiometry. We demonstrate for two paralog pairs of key scaffold Nups, Nup170/Nup157 and Nup192/Nup188, that their altered expression leads to significant changes in the NPC stoichiometry inducing either voids in the NPC structure or substitution of one paralog by the other. Thus, our results not only provide accurate stoichiometry information for the intact yeast NPC but also reveal an intriguing compositional plasticity of the NPC architecture, which may explain how differences in NPC composition could arise in the course of evolution.
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