Evidence map›Paper›PMID 27248858›Full record

ArticleCell cycle (Georgetown, Tex.)2016

Excess free histone H3 localizes to centrosomes for proteasome-mediated degradation during mitosis in metazoans.

Candice L Wike, Hillary K Graves, Arpit Wason, Reva Hawkins, Jay Gopalakrishnan, Jill Schumacher, Jessica K Tyler

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Review
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.

Candice L Wikea Department of Epigenetics and Molecular Carcinogenesis , University of Texas MD Anderson Cancer Center , Houston , TX , USA.
Hillary K Gravesa Department of Epigenetics and Molecular Carcinogenesis , University of Texas MD Anderson Cancer Center , Houston , TX , USA.
Arpit Wasonb Institute for Biochemistry and Center for Molecular Medicine, University of Cologne , Cologne , Germany.
Reva Hawkinsa Department of Epigenetics and Molecular Carcinogenesis , University of Texas MD Anderson Cancer Center , Houston , TX , USA.
Jay Gopalakrishnanb Institute for Biochemistry and Center for Molecular Medicine, University of Cologne , Cologne , Germany.
Jill Schumacherc Department of Genetics , University of Texas MD Anderson Cancer Center , Houston , TX , USA.
Jessica K Tylera Department of Epigenetics and Molecular Carcinogenesis , University of Texas MD Anderson Cancer Center , Houston , TX , USA.
The University of Texas MD Anderson Cancer Center · USUniversity of Cologne · DECornell University · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Scott Kopetz · 1985 to 2026
$290.8M
Chromatin's Role in Repair of Radiation-induced Damage.R01CA095641 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI TYLER, JESSICA K · 2002 to 2023
$5.2M
Chromatin Assembly, Structure and FunctionR01GM064475 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI TYLER, JESSICA K · 2002 to 2019
$4.4M
NCI NIH HHS P30 CA016672NCI NIH HHS R01 CA095641NIGMS NIH HHS R01 GM064475
6 · The paper itself

Abstract

The cell tightly controls histone protein levels in order to achieve proper packaging of the genome into chromatin, while avoiding the deleterious consequences of excess free histones. Our accompanying study has shown that a histone modification that loosens the intrinsic structure of the nucleosome, phosphorylation of histone H3 on threonine 118 (H3 T118ph), exists on centromeres and chromosome arms during mitosis. Here, we show that H3 T118ph localizes to centrosomes in humans, flies, and worms during all stages of mitosis. H3 abundance at the centrosome increased upon proteasome inhibition, suggesting that excess free histone H3 localizes to centrosomes for degradation during mitosis. In agreement, we find ubiquitinated H3 specifically during mitosis and within purified centrosomes. These results suggest that targeting of histone H3 to the centrosome for proteasome-mediated degradation is a novel pathway for controlling histone supply, specifically during mitosis.

Indexed as

MitosisProteolysisAnimalsCell Cycle ProteinsCentrosomeHeLa CellsHistonesHumansModels, BiologicalMutationPolo-Like Kinase 1Proteasome InhibitorsProtein Serine-Threonine KinasesProto-Oncogene ProteinsUbiquitinUbiquitinationCell Cycle ProteinsHistonesPolo-Like Kinase 1Proteasome InhibitorsProtein Serine-Threonine KinasesProto-Oncogene ProteinsUbiquitincentrosomedegradationhistone phosphorylationproteasome

Identifiers

PMID27248858
PMCPMC4993543
OpenAlexW2412258143

What OpenQuestion holds

Textmetadata
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.