Evidence map›Paper›PMID 24522885›Full record

ArticleOpen biology2014

A CENP-S/X complex assembles at the centromere in S and G2 phases of the human cell cycle.

Carsten Dornblut, Nadine Quinn, Shamci Monajambashi, Lisa Prendergast, Chelly van Vuuren, Sandra Münch, Wen Deng, Heinrich Leonhardt, M Cristina Cardoso, Christian Hoischen and 2 more

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Structure and function of the centromere and inner kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
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  7. Mobility of kinetochore proteins measured by FRAP analysis in living cells.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2022
    Article
  8. Article
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  11. Stepwise unfolding supports a subunit model for vertebrate kinetochores.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Review
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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

12 authors at 4 institutions in 2 countries.

Carsten DornblutMolecular Biology, FLI, Beutenbergstrasse 11, Jena 07745, Germany.
Nadine Quinn
Shamci Monajambashi
Lisa Prendergast
Chelly van Vuuren
Sandra Münch
Wen Deng
Heinrich Leonhardt
M Cristina Cardoso
Christian Hoischen
Stephan Diekmann
Kevin F Sullivan
Ollscoil na Gaillimhe – University of Galway · IECenter for Integrated Protein Science Munich · DELudwig-Maximilians-Universität München · DETechnical University of Darmstadt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The functional identity of centromeres arises from a set of specific nucleoprotein particle subunits of the centromeric chromatin fibre. These include CENP-A and histone H3 nucleosomes and a novel nucleosome-like complex of CENPs -T, -W, -S and -X. Fluorescence cross-correlation spectroscopy and Förster resonance energy transfer (FRET) revealed that human CENP-S and -X exist principally in complex in soluble form and retain proximity when assembled at centromeres. Conditional labelling experiments show that they both assemble de novo during S phase and G2, increasing approximately three- to fourfold in abundance at centromeres. Fluorescence recovery after photobleaching (FRAP) measurements documented steady-state exchange between soluble and assembled pools, with CENP-X exchanging approximately 10 times faster than CENP-S (t1/2 ∼ 10 min versus 120 min). CENP-S binding to sites of DNA damage was quite distinct, with a FRAP half-time of approximately 160 s. Fluorescent two-hybrid analysis identified CENP-T as a uniquely strong CENP-S binding protein and this association was confirmed by FRET, revealing a centromere-bound complex containing CENP-S, CENP-X and CENP-T in proximity to histone H3 but not CENP-A. We propose that deposition of the CENP-T/W/S/X particle reveals a kinetochore-specific chromatin assembly pathway that functions to switch centromeric chromatin to a mitosis-competent state after DNA replication. Centromeres shuttle between CENP-A-rich, replication-competent and H3-CENP-T/W/S/X-rich mitosis-competent compositions in the cell cycle.

Indexed as

Apoptosis Regulatory ProteinsBinding SitesCell Line, TumorCentromereChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsDNA DamageFluorescence Resonance Energy TransferG2 PhaseHeLa CellsHistonesHumansModels, MolecularNuclear ProteinsS PhaseApoptosis Regulatory ProteinsCENPS protein, humanCENPX protein, humanChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsHistonesNuclear ProteinsTumor Suppressor Proteinscentromereconstitutive centromere-associated networkkinetochoremitosis

Identifiers

PMID24522885
PMCPMC3938055
OpenAlexW2142024411

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.