Evidence map›Paper›PMID 30508113›Full record

ArticleNucleic acids research2019

The OTUD5-UBR5 complex regulates FACT-mediated transcription at damaged chromatin.

Angelo de Vivo, Anthony Sanchez, Jose Yegres, Jeonghyeon Kim, Sylvia Emly, Younghoon Kee

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

58 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Chromatin association promotes UBR5-mediated degradation of Rb.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. OTU deubiquitinases in disease: roles and targeting.Trends in molecular medicine · 2026
    Review
  7. Article
  8. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  9. Article
  10. AKT and DUBs: a bidirectional relationship.Cellular & molecular biology letters · 2025
    Review
  11. Nucleoporins cooperate with Polycomb silencers to promote transcriptional repression and repair at DNA double-strand breaks.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Beyond Chaperoning: The Multifaceted Role of FACT in Chromatin Transactions.International journal of molecular sciences · 2025
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. The GScience advances · 2024
    Article
  19. UBR-5 and UBE2D mediate timely exit from stem fate via destabilization of poly(A)-binding protein PABP-2 in cell state transition.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article
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

6 authors at 1 institution in 1 country.

Angelo de VivoDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, FL 33620, USA.
Anthony SanchezDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, FL 33620, USA.
Jose YegresDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, FL 33620, USA.
Jeonghyeon KimDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, FL 33620, USA.
Sylvia EmlyDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, FL 33620, USA.
Younghoon KeeDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, FL 33620, USA.
University of South Florida · US

Funding

The role of UBR5 in the PRC1-mediated transcriptional repression at damaged chromatinR01GM117062 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI WESTERHEIDE, SANDRA D. · 2017 to 2021
$1.5M
NIGMS NIH HHS R01 GM117062
6 · The paper itself

Abstract

Timely stalling and resumption of RNA polymerases at damaged chromatin are actively regulated processes. Prior work showed an importance of FACT histone chaperone in such process. Here we provide a new role of OTUD5 deubiquitinase in the FACT-dependent process. Through a DUB RNAi screen, we found OTUD5 as a specific stabilizer of the UBR5 E3 ligase. OTUD5 localizes to DNA double strand breaks (DSBs), interacts with UBR5 and represses the RNA Pol II elongation and RNA synthesis. OTUD5 co-localizes and interacts with the FACT component SPT16 and antagonizes the histone H2A deposition at DSB lesions. OTUD5 interacts with UBR5 and SPT16 independently through two distinct regions, and both interactions are necessary for arresting the Pol II elongation at lesions. These analyses suggested that the catalytic (through UBR5 stabilization) as well as scaffolding (through FACT binding) activities of OTUD5 are involved in the FACT-dependent transcription. We found that a cancer-associated missense mutation within the OTUD5 Ubiquitin Interacting Motif (UIM) abrogates the FACT association and the Pol II arrest, providing a possible link between the transcriptional regulation and tumor suppression. Our work establishes OTUD5 as a new regulator of the DNA damage response, and provides an insight into the FACT-dependent transcription at damaged chromatin.

Indexed as

DNA DamageTranscription, GeneticCell Cycle ProteinsCell LineChromatinDNA Breaks, Double-StrandedEndopeptidasesGene Expression RegulationGenomic InstabilityHistonesHumansMutationNeoplasmsProtein Interaction Domains and MotifsRNA Polymerase IITranscription Elongation, GeneticCell Cycle ProteinsChromatinEndopeptidasesHistonesOTUD5 protein, humanRNA Polymerase IISUPT16H protein, humanTranscription FactorsUbiquitin-Protein LigasesUBR5 protein, human

Identifiers

PMID30508113
PMCPMC6344881
OpenAlexW2903366123

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.