ArticleNucleus (Austin, Tex.)2014
Structural characterization of altered nucleoporin Nup153 expression in human cells by thin-section electron microscopy.
Article in Nucleus (Austin, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Quantifying 3D live-cell membrane dynamics using dynamic metal-induced energy transfer spectroscopy (dynaMIET).Science advances · 2026Article
- Proviral NUP153 binding to viral proteins and RNA regulates structural-nonstructural protein ratios in orthoflavivirus infection.Nature communications · 2026Article
- Nup153 and TPR/Megator Interact with TREX-2 Subunits and Are Essential for TREX-2-Dependent Nuclear Export ofInternational journal of molecular sciences · 2025Article
- Cul3 substrate adaptor SPOP targets Nup153 for degradation.Molecular biology of the cell · 2025Article
- The nucleoporin Nup153 is the anchor for Kif1a during basal nuclear migration in brain progenitor cells.Cell reports · 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
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Evolutionary, structural and functional insights in nuclear organisation and nucleocytoplasmic transport in trypanosomes.FEBS letters · 2023Review
- An evolutionarily conserved bimodular domain anchors ZC3HC1 and its yeast homologue Pml39p to the nuclear basket.Molecular biology of the cell · 2023Article
- Nup50 plays more than one instrument.Cell cycle (Georgetown, Tex.) · 2022Article
- ZC3HC1 is a structural element of the nuclear basket effecting interlinkage of TPR polypeptides.Molecular biology of the cell · 2022Article
- An anaphase surveillance mechanism prevents micronuclei formation from frequent chromosome segregation errors.Cell reports · 2021Article
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- Article
- Computational analyses reveal spatial relationships between nuclear pore complexes and specific lamins.The Journal of cell biology · 2021Article
- ATR is essential for preservation of cell mechanics and nuclear integrity during interstitial migration.Nature communications · 2020Article
- Nucleoporin TPR is an integral component of the TREX-2 mRNA export pathway.Nature communications · 2020Article
- Phosphoproteomic characterization of the signaling network resulting from activation of the chemokine receptor CCR2.The Journal of biological chemistry · 2020Article
- Viral protein X unlocks the nuclear pore complex through a human Nup153-dependent pathway to promote nuclear translocation of the lentiviral genome.Molecular biology of the cell · 2020Article
- Rescue of DNA damage after constricted migration reveals a mechano-regulated threshold for cell cycle.The Journal of cell biology · 2019Article
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Authors and funding
5 authors.
Funding
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Abstract
Nuclear pore complexes (NPCs) span the 2 membranes of the nuclear envelope (NE) and facilitate nucleocytoplasmic exchange of macromolecules. NPCs have a roughly tripartite structural organization with the so-called nuclear basket emanating from the NPC scaffold into the nucleoplasm. The nuclear basket is composed of the 3 nucleoporins Nup153, Nup50, and Tpr, but their specific role for the structural organization of this NPC substructure is, however, not well established. In this study, we have used thin-section transmission electron microscopy to determine the structural consequences of altering the expression of Nup153 in human cells. We show that the assembly and integrity of the nuclear basket is not affected by Nup153 depletion, whereas its integrity is perturbed in cells expressing high concentrations of the zinc-finger domain of Nup153. Moreover, even mild over-expression of Nup153 is coinciding with massive changes in nuclear organization and it is the excess of the zinc-finger domain of Nup153 that is sufficient to induce these rearrangements. Our data indicate a central function of Nup153 in the organization of the nucleus, not only at the periphery, but throughout the entire nuclear interior.
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