Evidence map›Paper›PMID 16778077›Full record

ArticleGenes & development2006

Histone modification-dependent and -independent pathways for recruitment of checkpoint protein Crb2 to double-strand breaks.

Li-Lin Du, Toru M Nakamura, Paul Russell

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing 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

97 citing papers in PubMed, 145 citations in OpenAlex.

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  14. Basis for metabolite-dependent Cullin-RING ligase deneddylation by the COP9 signalosome.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Genes · 2020
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37 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

3 authors at 2 institutions in 1 country.

Li-Lin DuDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Toru M Nakamura
Paul Russell
Scripps Research Institute · USUniversity of Illinois Chicago · US

Funding

Studies of the DNA damage checkpointsR01CA077325 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI RUSSELL, PAUL · 1998 to 2017
$7.1M
NCI NIH HHS CA 77325NCI NIH HHS R01 CA077325
6 · The paper itself

Abstract

Cellular responses to DNA damage involve the relocalization of checkpoint proteins to DNA double-strand breaks (DSBs). The fission yeast checkpoint mediator protein Crb2, a homolog of mammalian 53BP1, forms ionizing radiation-induced nuclear foci (IRIF). The IRIF formation by Crb2 requires histone H2A C-terminal phosphorylation and H4-K20 methylation. However, the relevance of Crb2 relocalization is uncertain, because neither histone modification is required for a checkpoint response. Here we show that these histone modifications cooperate in the same Crb2 recruitment pathway, which also requires the Tudor and BRCT motifs in Crb2. In the absence of these histone modifications, an alternative recruitment pathway is sufficient for checkpoint activation and accumulation of Crb2 at a persistent DSB generated by HO endonuclease. This parallel pathway requires a cyclin-dependent kinase phosphorylation site in Crb2 that mediates an association with another BRCT protein Cut5 (the TopBP1 homolog), which also accumulates at HO-induced DSBs. We propose that such dual recruitment mechanisms may be a common feature of DNA damage checkpoint mediators.

Indexed as

DNA DamageCell Cycle ProteinsDeoxyribonucleases, Type II Site-SpecificDNADNA RepairHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesMethylationMutationNuclear ProteinsPhosphorylationProtein MethyltransferasesProtein TransportRadiation, IonizingSaccharomyces cerevisiae ProteinsCell Cycle ProteinsCrb2 protein, S pombeDeoxyribonucleases, Type II Site-SpecificDNAHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesNuclear ProteinsProtein MethyltransferasesSaccharomyces cerevisiae ProteinsSCEI protein, S cerevisiaeSchizosaccharomyces pombe Proteins

Identifiers

PMID16778077
PMCPMC1482479
OpenAlexW2140154770

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.