Evidence map›Paper›PMID 22479148›Full record

ArticlePLoS biology2012

NUP-1 Is a large coiled-coil nucleoskeletal protein in trypanosomes with lamin-like functions.

Kelly N DuBois, Sam Alsford, Jennifer M Holden, Johanna Buisson, Michal Swiderski, Jean-Mathieu Bart, Alexander V Ratushny, Yakun Wan, Philippe Bastin, J David Barry and 5 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
7.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

78 citing papers in PubMed, 118 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Lamins as structural nuclear elements through evolution.Current opinion in cell biology · 2023
    Review
  10. Lessons from the deep: mechanisms behind diversification of eukaryotic protein complexes.Biological reviews of the Cambridge Philosophical Society · 2023
    Article
  11. Article
  12. RAD51-mediated R-loop formation acts to repair transcription-associated DNA breaks driving antigenic variation inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 9 institutions in 4 countries.

Kelly N DuBoisDepartment of Pathology, University of Cambridge, Cambridge, United Kingdom.
Sam Alsford
Jennifer M Holden
Johanna Buisson
Michal Swiderski
Jean-Mathieu Bart
Alexander V Ratushny
Yakun Wan
Philippe Bastin
J David Barry
Miguel Navarro
David Horn
John D Aitchison
Michael P Rout
Mark C Field
Institute for Systems Biology · USUniversity of Cambridge · GBInstitut Pasteur · FRUniversity of London · GBConsejo Superior de Investigaciones Científicas · ESInstituto de Parasitología y Biomedicina "López - Neyra" · ESRockefeller University · USUniversity of Glasgow · GBWellcome Centre for Molecular Parasitology · GB

Funding

Quantitative Systems BiologyP50GM076547 · NIGMS · INSTITUTE FOR SYSTEMS BIOLOGY · PI BALIGA, NITIN S · 2006 to 2016
$30.6M
NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
NCRR NIH HHS U54 RR022220NIGMS NIH HHS P50 GM076547Wellcome TrustWellcome Trust 055558Wellcome Trust 082813Wellcome Trust 085349Wellcome Trust 093010
6 · The paper itself

Abstract

A unifying feature of eukaryotic nuclear organization is genome segregation into transcriptionally active euchromatin and transcriptionally repressed heterochromatin. In metazoa, lamin proteins preserve nuclear integrity and higher order heterochromatin organization at the nuclear periphery, but no non-metazoan lamin orthologues have been identified, despite the likely presence of nucleoskeletal elements in many lineages. This suggests a metazoan-specific origin for lamins, and therefore that distinct protein elements must compose the nucleoskeleton in other lineages. The trypanosomatids are highly divergent organisms and possess well-documented but remarkably distinct mechanisms for control of gene expression, including polycistronic transcription and trans-splicing. NUP-1 is a large protein localizing to the nuclear periphery of Trypanosoma brucei and a candidate nucleoskeletal component. We sought to determine if NUP-1 mediates heterochromatin organization and gene regulation at the nuclear periphery by examining the influence of NUP-1 knockdown on morphology, chromatin positioning, and transcription. We demonstrate that NUP-1 is essential and part of a stable network at the inner face of the trypanosome nuclear envelope, since knockdown cells have abnormally shaped nuclei with compromised structural integrity. NUP-1 knockdown also disrupts organization of nuclear pore complexes and chromosomes. Most significantly, we find that NUP-1 is required to maintain the silenced state of developmentally regulated genes at the nuclear periphery; NUP-1 knockdown results in highly specific mis-regulation of telomere-proximal silenced variant surface glycoprotein (VSG) expression sites and procyclin loci, indicating a disruption to normal chromatin organization essential to life-cycle progression. Further, NUP-1 depletion leads to increased VSG switching and therefore appears to have a role in control of antigenic variation. Thus, analogous to vertebrate lamins, NUP-1 is a major component of the nucleoskeleton with key roles in organization of the nuclear periphery, heterochromatin, and epigenetic control of developmentally regulated loci.

Indexed as

Gene Expression RegulationAntigenic VariationCell NucleusChromosomesGene Knockdown TechniquesGenes, ProtozoanGenetic LociHeterochromatinLaminsMicroscopy, Electron, TransmissionMitosisNuclear EnvelopeNuclear Pore Complex ProteinsNuclear ProteinsProtein ConformationProtein TransportHeterochromatinLaminsNuclear Pore Complex ProteinsNuclear ProteinsProtozoan ProteinsVariant Surface Glycoproteins, Trypanosoma

Identifiers

PMID22479148
PMCPMC3313915
OpenAlexW2014619760

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.