Evidence map›Paper›PMID 11425876›Full record

ArticleThe Journal of cell biology2001

Nup2p dynamically associates with the distal regions of the yeast nuclear pore complex.

D J Dilworth, A Suprapto, J C Padovan, B T Chait, R W Wozniak, M P Rout, J D Aitchison

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

86 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
  2. Article
  3. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Nup50 plays more than one instrument.Cell cycle (Georgetown, Tex.) · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

26 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

7 authors at 3 institutions in 2 countries.

D J DilworthInstitute for Systems Biology, Seattle, Washington, 98105, USA.
A Suprapto
J C Padovan
B T Chait
R W Wozniak
M P Rout
J D Aitchison
Rockefeller University · USUniversity of Alberta · CAInstitute for Systems Biology · US

Funding

YNG1 PHD BINDING TO H3 3METHYL AT K4 PROMOTES TRANSCRIPTION AT TARGETED ORFSP41RR000862 · NCRR · ROCKEFELLER UNIVERSITY · PI DARNELL, JAMES E · 1985 to 2011
$16.1M
NCRR NIH HHS P41 RR000862NCRR NIH HHS RR 00862
6 · The paper itself

Abstract

Nucleocytoplasmic transport is mediated by the interplay between soluble transport factors and nucleoporins resident within the nuclear pore complex (NPC). Understanding this process demands knowledge of components of both the soluble and stationary phases and the interface between them. Here, we provide evidence that Nup2p, previously considered to be a typical yeast nucleoporin that binds import- and export-bound karyopherins, dynamically associates with the NPC in a Ran-facilitated manner. When bound to the NPC, Nup2p associates with regions corresponding to the nuclear basket and cytoplasmic fibrils. On the nucleoplasmic face, where the Ran--GTP levels are predicted to be high, Nup2p binds to Nup60p. Deletion of NUP60 renders Nup2p nucleoplasmic and compromises Nup2p-mediated recycling of Kap60p/Srp1p. Depletion of Ran--GTP by metabolic poisoning, disruption of the Ran cycle, or in vitro by cell lysis, results in a shift of Nup2p from the nucleoplasm to the cytoplasmic face of the NPC. This mobility of Nup2p was also detected using heterokaryons where, unlike nucleoporins, Nup2p was observed to move from one nucleus to the other. Together, our data support a model in which Nup2p movement facilitates the transition between the import and export phases of nucleocytoplasmic transport.

Indexed as

Nuclear Pore Complex ProteinsSaccharomyces cerevisiae Proteinsbeta KaryopherinsBinding SitesCell NucleusCytoplasmDeoxyglucoseFungal ProteinsGreen Fluorescent ProteinsGuanosine TriphosphateHeat-Shock ProteinsLuminescent ProteinsNuclear PoreNuclear ProteinsPorinsProtein Bindingbeta KaryopherinsDeoxyglucoseFungal ProteinsGreen Fluorescent ProteinsGuanosine TriphosphateHeat-Shock ProteinsLuminescent ProteinsNuclear Pore Complex ProteinsNuclear ProteinsNUP2 protein, S cerevisiaePorinsran GTP-Binding ProteinRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSodium AzideTIR1 protein, S cerevisiae

Identifiers

PMID11425876
PMCPMC2150724
OpenAlexW2143432207

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.