Evidence map›Paper›PMID 27284163›Full record

ArticleGenes & development2016

The CENP-T/-W complex is a binding partner of the histone chaperone FACT.

Lisa Prendergast, Sebastian Müller, Yiwei Liu, Hongda Huang, Florent Dingli, Damarys Loew, Isabelle Vassias, Dinshaw J Patel, Kevin F Sullivan, Geneviève Almouzni

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2016. 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
–field-weighted citation impact
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, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. The dynamics of centromere assembly and disassembly during quiescence.bioRxiv : the preprint server for biology · 2025
    Article
  4. A brief historical perspective on cell cycle control of CENP-A assembly and inheritance.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Kinetochore Architecture Employs Diverse Linker Strategies Across Evolution.Frontiers in cell and developmental biology · 2022
    Review
  16. InvestigatingFrontiers in genetics · 2022
    Article
  17. Article
  18. Review
  19. Article
  20. Epigenetic regulation of centromere function.Cellular and molecular life sciences : CMLS · 2020
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 3 countries.

Lisa PrendergastUMR3664, Centre National de la Recherche Scientifique, Institut Curie, PSL (Paris Sciences et Lettres) Research University, F-75005 Paris, France; UMR3664, Centre National de la Recherche Scientifique, University Pierre and Marie Curie Paris 06, Sorbonne Universités, F-75005 Paris, France;
Sebastian MüllerUMR3664, Centre National de la Recherche Scientifique, Institut Curie, PSL (Paris Sciences et Lettres) Research University, F-75005 Paris, France; UMR3664, Centre National de la Recherche Scientifique, University Pierre and Marie Curie Paris 06, Sorbonne Universités, F-75005 Paris, France;
Yiwei LiuStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA;
Hongda HuangStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA;
Florent DingliUMR3664, Centre National de la Recherche Scientifique, Institut Curie, PSL (Paris Sciences et Lettres) Research University, F-75005 Paris, France; Laboratoire de Spectrométrie de Masse Protéomique, Institut Curie, PSL (Paris Sciences et Lettres) Research University Centre de Recherche, Paris 75005, France;
Damarys LoewUMR3664, Centre National de la Recherche Scientifique, Institut Curie, PSL (Paris Sciences et Lettres) Research University, F-75005 Paris, France; Laboratoire de Spectrométrie de Masse Protéomique, Institut Curie, PSL (Paris Sciences et Lettres) Research University Centre de Recherche, Paris 75005, France;
Isabelle VassiasUMR3664, Centre National de la Recherche Scientifique, Institut Curie, PSL (Paris Sciences et Lettres) Research University, F-75005 Paris, France; UMR3664, Centre National de la Recherche Scientifique, University Pierre and Marie Curie Paris 06, Sorbonne Universités, F-75005 Paris, France;
Dinshaw J PatelStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA;
Kevin F SullivanCentre for Chromosome Biology, School of Natural Sciences, National University of Ireland, Galway, Ireland.
Geneviève AlmouzniUMR3664, Centre National de la Recherche Scientifique, Institut Curie, PSL (Paris Sciences et Lettres) Research University, F-75005 Paris, France; UMR3664, Centre National de la Recherche Scientifique, University Pierre and Marie Curie Paris 06, Sorbonne Universités, F-75005 Paris, France;
Université Paris Sciences et Lettres · FRMemorial Sloan Kettering Cancer Center · USOllscoil na Gaillimhe – University of Galway · IE

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
NCI NIH HHS P30 CA008748
6 · The paper itself

Abstract

The CENP-T/-W histone fold complex, as an integral part of the inner kinetochore, is essential for building a proper kinetochore at the centromere in order to direct chromosome segregation during mitosis. Notably, CENP-T/-W is not inherited at centromeres, and new deposition is absolutely required at each cell cycle for kinetochore function. However, the mechanisms underlying this new deposition of CENP-T/-W at centromeres are unclear. Here, we found that CENP-T deposition at centromeres is uncoupled from DNA synthesis. We identified Spt16 and SSRP1, subunits of the H2A-H2B histone chaperone facilitates chromatin transcription (FACT), as CENP-W binding partners through a proteomic screen. We found that the C-terminal region of Spt16 binds specifically to the histone fold region of CENP-T/-W. Furthermore, depletion of Spt16 impairs CENP-T and CENP-W deposition at endogenous centromeres, and site-directed targeting of Spt16 alone is sufficient to ensure local de novo CENP-T accumulation. We propose a model in which the FACT chaperone stabilizes the soluble CENP-T/-W complex in the cell and promotes dynamics of exchange, enabling CENP-T/-W deposition at centromeres.

Indexed as

AnimalsCell Cycle ProteinsCell LineCentromereChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHeLa CellsHigh Mobility Group ProteinsHistone ChaperonesHumansKinetochoresProtein BindingProtein DomainsProtein FoldingProteomicsRecombinant ProteinsCell Cycle ProteinsCENPT protein, humanCENPW protein, humanChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHigh Mobility Group ProteinsHistone ChaperonesRecombinant ProteinsSSRP1 protein, humanSUPT16H protein, humanTranscriptional Elongation FactorsTranscription FactorsCENPcentromerehistone chaperonemitosis

Identifiers

PMID27284163
PMCPMC4911930
OpenAlexW2412224982

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.