Evidence map›Paper›PMID 18480059›Full record

ArticleThe Journal of biological chemistry2008

Catalytic function of the PR-Set7 histone H4 lysine 20 monomethyltransferase is essential for mitotic entry and genomic stability.

Sabrina I Houston, Kirk J McManus, Melissa M Adams, Jennifer K Sims, Phillip B Carpenter, Michael J Hendzel, Judd C Rice

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 3% 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

94 citing papers in PubMed, 1 synthesis or guideline pooled it, 157 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  8. Article
  9. Adaptive exchange sustains cullin-RING ubiquitin ligase networks and proper licensing of DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  11. Article
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  15. ReducedCancers · 2021
    Article
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  20. Review

34 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 3 institutions in 2 countries.

Sabrina I HoustonDepartment of Biochemistry and Molecular Biology, University of Southern California Keck School of Medicine, Los Angeles, California 90033, USA.
Kirk J McManus
Melissa M Adams
Jennifer K Sims
Phillip B Carpenter
Michael J Hendzel
Judd C Rice
University of Southern California · USThe University of Texas Health Science Center at Houston · USUniversity of Alberta · CA

Funding

Molecular mechanisms of gene silencing by H4 methylationR01GM075094 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI RICE, JUDD C · 2007 to 2011
$1.5M
Role of 53BP1 During the DNA Damage ResponseR56GM065812 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI CARPENTER, PHILLIP B · 2007 to 2007
$273k
NIGMS NIH HHS GM075094NIGMS NIH HHS R01 GM075094NIGMS NIH HHS R56 GM065812
6 · The paper itself

Abstract

Histone-modifying enzymes play a critical role in modulating chromatin dynamics. In this report we demonstrate that one of these enzymes, PR-Set7, and its corresponding histone modification, the monomethylation of histone H4 lysine 20 (H4K20), display a distinct cell cycle profile in mammalian cells: low at G1, increased during late S phase and G2, and maximal from prometaphase to anaphase. The lack of PR-Set7 and monomethylated H4K20 resulted in a number of aberrant phenotypes in several different mammalian cell types. These include the inability of cells to progress past G2, global chromosome condensation failure, aberrant centrosome amplification, and substantial DNA damage. By employing a catalytically dead dominant negative PR-Set7 mutant, we discovered that its mono-methyltransferase activity was required to prevent these phenotypes. Importantly, we demonstrate that all of the aberrant phenotypes associated with the loss of PR-Set7 enzymatic function occur independently of p53. Collectively, our findings demonstrate that PR-Set7 enzymatic activity is essential for mammalian cell cycle progression and for the maintenance of genomic stability, most likely by monomethylating histone H4K20. Our results predict that alterations of this pathway could result in gross chromosomal aberrations and aneuploidy.

Indexed as

Chromatin Assembly and DisassemblyGenomic InstabilityInterphaseAneuploidyAnimalsCentrosomeChromosomes, HumanDNA DamageHeLa CellsHistone-Lysine N-MethyltransferaseHistonesHumansMiceTumor Suppressor Protein p53Histone-Lysine N-MethyltransferaseHistonesKMT5A protein, humanKMT5a protein, mouseTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID18480059
PMCPMC2443654
OpenAlexW2019386365

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.