ArticleMolecular and cellular biology2004
The fission yeast Nup107-120 complex functionally interacts with the small GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution, and proper cell division.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 85 citations in OpenAlex.
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- Comprehensive pan-cancer evaluation of NUP85 prognosis, immune infiltration response, and validation in prostate cancer.Discover oncology · 2025Article
- Nucleoporin 107 is a prognostic biomarker in hepatocellular carcinoma associated with immune infiltration.Cancer medicine · 2023Article
- Quantitative analysis of nuclear pore complex organization inLife science alliance · 2022Article
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- Heh2/Man1 may be an evolutionarily conserved sensor of NPC assembly state.Molecular biology of the cell · 2021Article
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- Nucleoporin 160 Regulates Flowering through Anchoring HOS1 for Destabilizing CO inPlant communications · 2020Article
- Spatiotemporal control of spindle disassembly in fission yeast.Cellular and molecular life sciences : CMLS · 2019Review
- Asymmetrical localization of Nup107-160 subcomplex components within the nuclear pore complex in fission yeast.PLoS genetics · 2019Article
- Breaking the Y.PLoS genetics · 2019Article
- Systematic analysis reveals the prevalence and principles of bypassable gene essentiality.Nature communications · 2019Article
- A systematic genetic screen identifies essential factors involved in nuclear size control.PLoS genetics · 2019Article
- Nucleoporin 107 facilitates the nuclear export of Scn5a mRNA to regulate cardiac bioelectricity.Journal of cellular and molecular medicine · 2019Article
- Article
- Article
- Release of condensin from mitotic chromosomes requires the Ran-GTP gradient in the reorganized nucleus.Biology open · 2017Article
- Virtual Nuclear Envelope Breakdown and Its Regulators in Fission Yeast Meiosis.Frontiers in cell and developmental biology · 2016Review
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Authors and funding
7 authors at 3 institutions in 2 countries.
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Abstract
We have characterized Schizosaccharomyces pombe open reading frames encoding potential orthologues of constituents of the evolutionarily conserved Saccharomyces cerevisiae Nup84 vertebrate Nup107-160 nuclear pore subcomplex, namely Nup133a, Nup133b, Nup120, Nup107, Nup85, and Seh1. In spite of rather weak sequence conservation, in vivo analyses demonstrated that these S. pombe proteins are localized at the nuclear envelope. Biochemical data confirmed the organization of these nucleoporins within conserved complexes. Although examination of the S. cerevisiae and S. pombe deletion mutants revealed different viability phenotypes, functional studies indicated that the involvement of this complex in nuclear pore distribution and mRNA export has been conserved between these highly divergent yeasts. Unexpectedly, microscopic analyses of some of the S. pombe mutants revealed cell division defects at the restrictive temperature (abnormal septa and mitotic spindles and chromosome missegregation) that were reminiscent of defects occurring in several S. pombe GTPase Ran (Ran(Sp))/Spi1 cycle mutants. Furthermore, deletion of nup120 moderately altered the nuclear location of Ran(Sp)/Spi1, whereas overexpression of a nonfunctional Ran(Sp)/Spi1-GFP allele was specifically toxic in the Deltanup120 and Deltanup133b mutant strains, indicating a functional and genetic link between constituents of the S. pombe Nup107-120 complex and of the Ran(Sp)/Spi1 pathway.
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