Evidence map›Paper›PMID 30177573›Full record

ArticleThe EMBO journal2018

Evidence for the nuclear import of histones H3.1 and H4 as monomers.

Michael James Apta-Smith, Juan Ramon Hernandez-Fernaud, Andrew James Bowman

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

36 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
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  15. Article
  16. Review
  17. Article
  18. Article
  19. The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023
    Article
  20. Article
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

3 authors at 1 institution in 1 country.

Michael James Apta-SmithDivision of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK.
Juan Ramon Hernandez-FernaudProteomics Research Technology Platform, School of Life Sciences, University of Warwick, Coventry, UK.
Andrew James BowmanDivision of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK a.bowman.1@warwick.ac.uk.ORCID 0000-0002-5507-669X
University of Warwick · GB

Funding

Wellcome TrustWellcome Trust 105627/Z/14/ZWellcome Trust 208801/Z/17/Z
6 · The paper itself

Abstract

Newly synthesised histones are thought to dimerise in the cytosol and undergo nuclear import in complex with histone chaperones. Here, we provide evidence that human H3.1 and H4 are imported into the nucleus as monomers. Using a tether-and-release system to study the import dynamics of newly synthesised histones, we find that cytosolic H3.1 and H4 can be maintained as stable monomeric units. Cytosolically tethered histones are bound to importin-alpha proteins (predominantly IPO4), but not to histone-specific chaperones NASP, ASF1a, RbAp46 (RBBP7) or HAT1, which reside in the nucleus in interphase cells. Release of monomeric histones from their cytosolic tether results in rapid nuclear translocation, IPO4 dissociation and incorporation into chromatin at sites of replication. Quantitative analysis of histones bound to individual chaperones reveals an excess of H3 specifically associated with sNASP, suggesting that NASP maintains a soluble, monomeric pool of H3 within the nucleus and may act as a nuclear receptor for newly imported histone. In summary, we propose that histones H3 and H4 are rapidly imported as monomeric units, forming heterodimers in the nucleus rather than the cytosol.

Indexed as

Active Transport, Cell NucleusCell NucleusHeLa CellsHistonesHumansInterphaseMolecular ChaperonesHistonesMolecular Chaperoneschaperonechromatinhistonenuclear importnucleosome

Identifiers

PMID30177573
PMCPMC6166134
OpenAlexW2890022950

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.