ArticleJournal of cell science2021
A hub-and-spoke nuclear lamina architecture in trypanosomes.
Article in Journal of cell science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Enhanced Detection of Homology Using Artificial Intelligence in Euglenids.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The subcellular architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Strange Case of the Noncanonical Lamina: Deep Divisions in Nuclear Organisation?Sub-cellular biochemistry · 2025Review
- Structural Diversity and Distribution of Nuclear Matrix Constituent Protein Class Nuclear Lamina Proteins in Streptophytic Algae.Genome biology and evolution · 2024Article
- Lamins as structural nuclear elements through evolution.Current opinion in cell biology · 2023Review
- Evolutionary, structural and functional insights in nuclear organisation and nucleocytoplasmic transport in trypanosomes.FEBS letters · 2023Review
- Evolution and diversification of the nuclear envelope.Nucleus (Austin, Tex.) · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The nuclear lamina supports many functions, including maintaining nuclear structure and gene expression control, and correct spatio-temporal assembly is vital to meet these activities. Recently, multiple lamina systems have been described that, despite independent evolutionary origins, share analogous functions. In trypanosomatids the two known lamina proteins, NUP-1 and NUP-2, have molecular masses of 450 and 170 kDa, respectively, which demands a distinct architecture from the ∼60 kDa lamin-based system of metazoa and other lineages. To uncover organizational principles for the trypanosome lamina we generated NUP-1 deletion mutants to identify domains and their arrangements responsible for oligomerization. We found that both the N- and C-termini act as interaction hubs, and that perturbation of these interactions impacts additional components of the lamina and nuclear envelope. Furthermore, the assembly of NUP-1 terminal domains suggests intrinsic organizational capacity. Remarkably, there is little impact on silencing of telomeric variant surface glycoprotein genes. We suggest that both terminal domains of NUP-1 have roles in assembling the trypanosome lamina and propose a novel architecture based on a hub-and-spoke configuration.
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Registered trials
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