ArticleThe Journal of biological chemistry2008
Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA damage.
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 34 papers.
What it found
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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.
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Who cites it
34 citing papers in PubMed, 63 citations in OpenAlex.
- CRB2 Activates an Epigenetic Axis to Promote Ferroptosis in Head and Neck Squamous Cell Carcinoma.Cancer research · 2026Article
- New perspectives on epigenetic modifications and PARP inhibitor resistance in HR-deficient cancers.Cancer drug resistance (Alhambra, Calif.) · 2023Article
- CHD7 and 53BP1 regulate distinct pathways for the re-ligation of DNA double-strand breaks.Nature communications · 2020Article
- Population-Based Analysis of DNA Damage and Epigenetic Effects of 1,3-Butadiene in the Mouse.Chemical research in toxicology · 2019Article
- The tale of histone modifications and its role in multiple sclerosis.Human genomics · 2018Review
- The inhibition of checkpoint activation by telomeres does not involve exclusion of dimethylation of histone H4 lysine 20 (H4K20me2).F1000Research · 2018Article
- A cell cycle-independent mode of the Rad9-Dpb11 interaction is induced by DNA damage.Scientific reports · 2017Article
- Select human cancer mutants of NRMT1 alter its catalytic activity and decrease N-terminal trimethylation.Protein science : a publication of the Protein Society · 2017Article
- Replication-Coupled Dilution of H4K20me2 Guides 53BP1 to Pre-replicative Chromatin.Cell reports · 2017Article
- Functional Roles of Acetylated Histone Marks at Mouse Meiotic Recombination Hot Spots.Molecular and cellular biology · 2017Article
- CRL4(Wdr70) regulates H2B monoubiquitination and facilitates Exo1-dependent resection.Nature communications · 2016Article
- Histone H4 Lysine 20 (H4K20) Methylation, Expanding the Signaling Potential of the Proteome One Methyl Moiety at a Time.Molecular & cellular proteomics : MCP · 2016Review
- Distribution of histone H4 modifications as revealed by a panel of specific monoclonal antibodies.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2015Article
- Constitutive heterochromatin formation and transcription in mammals.Epigenetics & chromatin · 2015Review
- Non-histone protein methylation as a regulator of cellular signalling and function.Nature reviews. Molecular cell biology · 2015Review
- The functional diversity of protein lysine methylation.Molecular systems biology · 2014Review
- Role of 53BP1 in the regulation of DNA double-strand break repair pathway choice.Radiation research · 2014Review
- Article
- The 53BP1 homolog in C. elegans influences DNA repair and promotes apoptosis in response to ionizing radiation.PloS one · 2013Article
- The role of DNA methylation and histone modifications in transcriptional regulation in humans.Sub-cellular biochemistry · 2013Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Histone lysine methylation is an important chromatin modification that can be catalyzed to a mono-, di-, or tri-methyl state. An ongoing challenge is to decipher how these different methyllysine histone marks can mediate distinct aspects of chromatin function. The fission yeast checkpoint protein Crb2 is rapidly targeted to sites of DNA damage after genomic insult, and this recruitment requires methylation of histone H4 lysine 20 (H4K20). Here we show that the tandem tudor domains of Crb2 preferentially bind the di-methylated H4K20 residue. Loss of this interaction by disrupting either the tudor-binding motif or the H4K20 methylating enzyme Set9/Kmt5 ablates Crb2 localization to double-strand breaks and impairs checkpoint function. Further we show that dimethylation, but not tri-methylation, of H4K20 is required for Crb2 localization, checkpoint function, and cell survival after DNA damage. These results argue that the di-methyl H4K20 modification serves as a binding target that directs Crb2 to sites of genomic lesions and defines an important genome integrity pathway mediated by a specific methyl-lysine histone mark.
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Registered trials
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.