Evidence map›Paper›PMID 11309407›Full record

ArticleThe Journal of cell biology2001

Nuclear import of histone H2A and H2B is mediated by a network of karyopherins.

N Mosammaparast, K R Jackson, Y Guo, C J Brame, J Shabanowitz, D F Hunt, L F Pemberton

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 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

85 citing papers in PubMed, 178 citations in OpenAlex.

  1. Article
  2. Article
  3. Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Dinochromosome Heterotermini with Telosomal Anchorages.International journal of molecular sciences · 2024
    Article
  8. Article
  9. Article
  10. Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 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 1 institution in 1 country.

N MosammaparastCenter for Cell Signaling, Department of Microbiology, Health Sciences Center, University of Virginia, 22908, USA.
K R Jackson
Y Guo
C J Brame
J Shabanowitz
D F Hunt
L F Pemberton
University of Virginia · US

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
NIGMS NIH HHS GM-37537NIGMS NIH HHS R01 GM037537
6 · The paper itself

Abstract

The first step in the assembly of new chromatin is the cell cycle-regulated synthesis and nuclear import of core histones. The core histones include H2A and H2B, which are assembled into nucleosomes as heterodimers. We show here that the import of histone H2A and H2B is mediated by several members of the karyopherin (Kap; importin) family. An abundant complex of H2A, H2B, and Kap114p was detected in cytosol. In addition, two other Kaps, Kap121p and Kap123p, and the histone chaperone Nap1p were isolated with H2A and H2B. Nap1p is not necessary for the formation of the Kap114p-H2A/H2B complex or for import of H2A and H2B. We demonstrate that both histones contain a nuclear localization sequence (NLS) in the amino-terminal tail. Fusions of the NLSs to green fluorescent protein were specifically mislocalized to the cytoplasm in kap mutant strains. In addition, we detected a specific mislocalization in a kap95 temperature-sensitive strain, suggesting that this Kap is also involved in the import of H2A and H2B in vivo. Importantly, we show that Kap114p, Kap121p, and Kap95 interact directly with both histone NLSs and that RanGTP inhibits this association. These data suggest that the import of H2A and H2B is mediated by a network of Kaps, in which Kap114p may play the major role.

Indexed as

Saccharomyces cerevisiae ProteinsActive Transport, Cell Nucleusbeta KaryopherinsCell Cycle ProteinsCell NucleusGenes, ReporterHistonesHumansImmunoblottingMacromolecular SubstancesMicroscopy, FluorescenceMolecular ChaperonesNuclear Localization SignalsNuclear ProteinsNucleosome Assembly Protein 1Protein Bindingbeta KaryopherinsCell Cycle ProteinsHistonesKAP114 protein, S cerevisiaeMacromolecular SubstancesMolecular ChaperonesNAP1L1 protein, humanNAP1 protein, S cerevisiaeNuclear Localization SignalsNuclear ProteinsNucleosome Assembly Protein 1ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID11309407
PMCPMC2169462
OpenAlexW2013165066

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.