ArticlePLoS genetics2019
Asymmetrical localization of Nup107-160 subcomplex components within the nuclear pore complex in fission yeast.
Article in PLoS genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Proximity-based proteomic profiling uncovers distinct interactome of human RAG1 and RAG2.Acta biochimica et biophysica Sinica · 2026Article
- In situ architecture of the nuclear pore complex of the higher plant Arabidopsis thaliana.Nature plants · 2025Article
- Ulp1 association with nuclear pore complexes is required for the maintenance of global SUMOylation.Molecular biology of the cell · 2025Article
- SUMO protease and proteasome recruitment at the nuclear periphery differently affect replication dynamics at arrested forks.Nucleic acids research · 2024Article
- Combining single-molecule and expansion microscopy in fission yeast to visualize protein structures at the nanostructural level.Open biology · 2024Article
- Fission yeast essential nuclear pore protein Nup211 regulates the expression of genes involved in cytokinesis.PloS one · 2024Article
- Evolutionary, structural and functional insights in nuclear organisation and nucleocytoplasmic transport in trypanosomes.FEBS letters · 2023Review
- Implications of a multiscale structure of the yeast nuclear pore complex.Molecular cell · 2023Article
- Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022Review
- Function of Nuclear Pore Complexes in Regulation of Plant Defense Signaling.International journal of molecular sciences · 2022Review
- The function of Nucleoporin 37 on mouse oocyte maturation and preimplantation embryo development.Journal of assisted reproduction and genetics · 2022Article
- Review
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- Heh2/Man1 may be an evolutionarily conserved sensor of NPC assembly state.Molecular biology of the cell · 2021Article
- One Ring to Rule them All? Structural and Functional Diversity in the Nuclear Pore Complex.Trends in biochemical sciences · 2021Review
- The nuclear pore primes recombination-dependent DNA synthesis at arrested forks by promoting SUMO removal.Nature communications · 2020Article
- Article
- Nuclear Envelope Proteins Modulating the Heterochromatin Formation and Functions in Fission Yeast.Cells · 2020Review
- Lem2 and Lnp1 maintain the membrane boundary between the nuclear envelope and endoplasmic reticulum.Communications biology · 2020Article
- Breaking the Y.PLoS genetics · 2019Article
Corrections and comments
- Commented on byBreaking the Y.2019
Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear pore complex (NPC) forms a gateway for nucleocytoplasmic transport. The outer ring protein complex of the NPC (the Nup107-160 subcomplex in humans) is a key component for building the NPC. Nup107-160 subcomplexes are believed to be symmetrically localized on the nuclear and cytoplasmic sides of the NPC. However, in S. pombe immunoelectron and fluorescence microscopic analyses revealed that the homologous components of the human Nup107-160 subcomplex had an asymmetrical localization: constituent proteins spNup132 and spNup107 were present only on the nuclear side (designated the spNup132 subcomplex), while spNup131, spNup120, spNup85, spNup96, spNup37, spEly5 and spSeh1 were localized only on the cytoplasmic side (designated the spNup120 subcomplex), suggesting the complex was split into two pieces at the interface between spNup96 and spNup107. This contrasts with the symmetrical localization reported in other organisms. Fusion of spNup96 (cytoplasmic localization) with spNup107 (nuclear localization) caused cytoplasmic relocalization of spNup107. In this strain, half of the spNup132 proteins, which interact with spNup107, changed their localization to the cytoplasmic side of the NPC, leading to defects in mitotic and meiotic progression similar to an spNup132 deletion strain. These observations suggest the asymmetrical localization of the outer ring spNup132 and spNup120 subcomplexes of the NPC is necessary for normal cell cycle progression in fission yeast.
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