Evidence map›Paper›PMID 38242129›Full record

ArticleMolecular cell2024

Mechanisms of RNF168 nucleosome recognition and ubiquitylation.

Qi Hu, Debiao Zhao, Gaofeng Cui, Janarjan Bhandari, James R Thompson, Maria Victoria Botuyan, Georges Mer

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.6field-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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Precision Chemistry for Protein Lysine Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  2. A Chromatin Biology Assessment of AlphaFold3.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Ubiquitin System-Driven Proteostasis in DNA Damage Response.International journal of molecular sciences · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. 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

7 authors at 3 institutions in 1 country.

Qi HuDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA.
Debiao ZhaoDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA.
Gaofeng CuiDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA.
Janarjan BhandariThe Hormel Institute, University of Minnesota, Austin, MN, USA.
James R ThompsonThe Hormel Institute, University of Minnesota, Austin, MN, USA.
Maria Victoria BotuyanDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA. Electronic address: botuyan.maria@mayo.edu.
Georges MerDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA; Department of Cancer Biology, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA. Electronic address: mer.georges@mayo.edu.
Mayo Clinic · USHormel (United States) · USUniversity of Minnesota · US

Funding

Pacific Northwest Center for Cryo-EM - Screening supplementU24GM129547 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI EVANS, JAMES E, GOUAUX, JAMES E · 2018 to 2023
$54.8M
Structural Biology of Lysine Methylation in DNA Damage and Checkpoint SignalingR01CA132878 · NCI · MAYO CLINIC ROCHESTER · PI Georges Mer · 2008 to 2026
$4.5M
Structural biology of DNA damage response in chromatinR35GM136262 · NIGMS · MAYO CLINIC ROCHESTER · PI MER, GEORGES · 2020 to 2025
$4.2M
NCI NIH HHS R01 CA132878NIGMS NIH HHS R35 GM136262NIGMS NIH HHS U24 GM129547U.S. Department of Energy (DOE) DE-AC02-06CH11357
6 · The paper itself

Abstract

RNF168 plays a central role in the DNA damage response (DDR) by ubiquitylating histone H2A at K13 and K15. These modifications direct BRCA1-BARD1 and 53BP1 foci formation in chromatin, essential for cell-cycle-dependent DNA double-strand break (DSB) repair pathway selection. The mechanism by which RNF168 catalyzes the targeted accumulation of H2A ubiquitin conjugates to form repair foci around DSBs remains unclear. Here, using cryoelectron microscopy (cryo-EM), nuclear magnetic resonance (NMR) spectroscopy, and functional assays, we provide a molecular description of the reaction cycle and dynamics of RNF168 as it modifies the nucleosome and recognizes its ubiquitylation products. We demonstrate an interaction of a canonical ubiquitin-binding domain within full-length RNF168, which not only engages ubiquitin but also the nucleosome surface, clarifying how such site-specific ubiquitin recognition propels a signal amplification loop. Beyond offering mechanistic insights into a key DDR protein, our study aids in understanding site specificity in both generating and interpreting chromatin ubiquitylation.

Indexed as

NucleosomesUbiquitin-Protein LigasesChromatinCryoelectron MicroscopyDNA DamageDNA RepairHistonesTumor Suppressor p53-Binding Protein 1UbiquitinUbiquitinationChromatinHistonesNucleosomesTumor Suppressor p53-Binding Protein 1UbiquitinUbiquitin-Protein Ligases53BP1BRCA1-BARD1chromatincryo-EMDNA damage responseNMR spectroscopynucleosomeRNF168UbcH5cubiquitin ligaseX-ray crystallography

Identifiers

PMID38242129
PMCPMC10939898
OpenAlexW4391056105

What OpenQuestion holds

Textmetadata
LicenceTDM
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.