Evidence map›Paper›PMID 30988309›Full record

ArticleNature communications2019

Structural basis of specific H2A K13/K15 ubiquitination by RNF168.

Velten Horn, Michael Uckelmann, Heyi Zhang, Jelmer Eerland, Ivette Aarsman, Ulric B le Paige, Chen Davidovich, Titia K Sixma, Hugo van Ingen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Ubiquitin-induced RNF168 condensation promotes DNA double-strand break repair.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Emerging Roles of RNF168 in Tumor Progression.Molecules (Basel, Switzerland) · 2023
    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

9 authors at 3 institutions in 2 countries.

Velten HornDepartment of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, the Netherlands.
Michael UckelmannDivision of Biochemistry and Oncode Institute, Netherlands Cancer Institute, P.O. Box 90203, 1006 BE, Amsterdam, the Netherlands.
Heyi ZhangDepartment of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, the Netherlands.
Jelmer EerlandDepartment of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, the Netherlands.
Ivette AarsmanDivision of Biochemistry and Oncode Institute, Netherlands Cancer Institute, P.O. Box 90203, 1006 BE, Amsterdam, the Netherlands.
Ulric B le PaigeDepartment of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, the Netherlands.
Chen DavidovichDepartment of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Faculty of Medicine, Nursing and Health Sciences, Monash University, 23 Innovation Walk, Clayton, VIC, 3800, Australia.ORCID http://orcid.org/0000-0002-1085-6094
Titia K SixmaDivision of Biochemistry and Oncode Institute, Netherlands Cancer Institute, P.O. Box 90203, 1006 BE, Amsterdam, the Netherlands. t.sixma@nki.nl.
Hugo van IngenDepartment of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, the Netherlands. h.vaningen@uu.nl.
Leiden University · NLAustralian Regenerative Medicine Institute · AUThe Netherlands Cancer Institute · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination of chromatin by modification of histone H2A is a critical step in both regulation of DNA repair and regulation of cell fate. These very different outcomes depend on the selective modification of distinct lysine residues in H2A, each by a specific E3 ligase. While polycomb PRC1 complexes modify K119, resulting in gene silencing, the E3 ligase RNF168 modifies K13/15, which is a key event in the response to DNA double-strand breaks. The molecular origin of ubiquitination site specificity by these related E3 enzymes is one of the open questions in the field. Using a combination of NMR spectroscopy, crosslinking mass-spectrometry, mutagenesis and data-driven modelling, here we show that RNF168 binds the acidic patch on the nucleosome surface, directing the E2 to the target lysine. The structural model highlights the role of E3 and nucleosome in promoting ubiquitination and provides a basis for understanding and engineering of chromatin ubiquitination specificity.

Indexed as

Cell DifferentiationDNA RepairHistonesHumansModels, MolecularProtein DomainsUbiquitinationUbiquitin-Protein LigasesHistonesUbiquitin-Protein Ligases

Identifiers

PMID30988309
PMCPMC6465349
OpenAlexW2936398466

What OpenQuestion holds

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Registered trials

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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.