Evidence map›Paper›PMID 21035370›Full record

ArticleMolecular cell2010

Regulation of the histone H4 monomethylase PR-Set7 by CRL4(Cdt2)-mediated PCNA-dependent degradation during DNA damage.

Hisanobu Oda, Michael R Hübner, David B Beck, Michiel Vermeulen, Jerard Hurwitz, David L Spector, Danny Reinberg

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.

0numbers the graph read from it
0cells of the map it votes in
159citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

159 citing papers in PubMed, 248 citations in OpenAlex.

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  16. Epigenetics, DNA damage, and aging.The Journal of clinical investigation · 2022
    Review
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  18. Article
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  20. Article

99 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 5 institutions in 2 countries.

Hisanobu OdaDepartment of Biochemistry, New York University School of Medicine, 522 First Avenue, New York, NY 10016, USA.
Michael R Hübner
David B Beck
Michiel Vermeulen
Jerard Hurwitz
David L Spector
Danny Reinberg
Cold Spring Harbor Laboratory · USNew York University · USHoward Hughes Medical Institute · USMemorial Sloan Kettering Cancer Center · USUniversity Medical Center Utrecht · NL

Funding

Spatial Organization of Gene ExpressoinR01GM042694 · NIGMS · COLD SPRING HARBOR LABORATORY · PI SPECTOR, DAVID L · 1990 to 2018
$12.7M
Transcription Regulation by NC2R01GM064844 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI REINBERG, DANNY · 2002 to 2014
$3.3M
Howard Hughes Medical InstituteNIGMS NIH HHS GM42694NIGMS NIH HHS GM64844NIGMS NIH HHS R01 GM042694NIGMS NIH HHS R01 GM064844
6 · The paper itself

Abstract

The histone methyltransferase PR-Set7/Set8 is the sole enzyme that catalyzes monomethylation of histone H4 at K20 (H4K20me1). Previous reports document disparate evidence regarding PR-Set7 expression during the cell cycle, the biological relevance of PR-Set7 interaction with PCNA, and its role in the cell. We find that PR-Set7 is indeed undetectable during S phase and instead is detected during late G2, mitosis, and early G1. PR-Set7 is transiently recruited to laser-induced DNA damage sites through its interaction with PCNA, after which 53BP1 is recruited dependent on PR-Set7 catalytic activity. During the DNA damage response, PR-Set7 interaction with PCNA through a specialized "PIP degron" domain targets it for PCNA-coupled CRL4(Cdt2)-dependent proteolysis. PR-Set7 mutant in its "PIP degron" is now detectable during S phase, during which the mutant protein accumulates. Outside the chromatin context, Skp2 promotes PR-Set7 degradation as well. These findings demonstrate a stringent spatiotemporal control of PR-Set7 that is essential for preserving the genomic integrity of mammalian cells.

Indexed as

DNA DamageProtein Processing, Post-TranslationalAnimalsBiocatalysisCell Line, TumorCullin ProteinsDNA-Binding ProteinsEnzyme ActivationEnzyme StabilityHistone-Lysine N-MethyltransferaseHistonesHumansIntracellular Signaling Peptides and ProteinsMiceModels, BiologicalNuclear ProteinsCUL4A protein, humanCUL4B protein, humanCullin ProteinsDDB1 protein, humanDNA-Binding ProteinsDTL protein, humanHistone-Lysine N-MethyltransferaseHistonesIntracellular Signaling Peptides and ProteinsKMT5A protein, humanNuclear ProteinsProliferating Cell Nuclear AntigenProteasome Endopeptidase ComplexTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1UbiquitinUbiquitin-Protein Ligases

Identifiers

PMID21035370
PMCPMC2999913
OpenAlexW2071787911

What OpenQuestion holds

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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.