Evidence map›Paper›PMID 24979766›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

RNF144A, an E3 ubiquitin ligase for DNA-PKcs, promotes apoptosis during DNA damage.

Shiuh-Rong Ho, Christina S Mahanic, Yu-Ju Lee, Weei-Chin Lin

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Secrets of DNA-PKcs beyond DNA repair.NPJ precision oncology · 2024
    Review
  11. Article
  12. Article
  13. The TP53-activated E3 ligase RNF144B is a tumour suppressor that prevents genomic instability.Journal of experimental & clinical cancer research : CR · 2024
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. 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

4 authors.

Shiuh-Rong HoSection of Hematology/Oncology, Department of Medicine.
Christina S MahanicSection of Hematology/Oncology, Department of Medicine,Integrative Molecular and Biomedical Sciences Graduate Program.
Yu-Ju LeeSection of Hematology/Oncology, Department of Medicine,Interdepartmental Program in Translational Biology and Molecular Medicine.
Weei-Chin LinSection of Hematology/Oncology, Department of Medicine,Integrative Molecular and Biomedical Sciences Graduate Program,Interdepartmental Program in Translational Biology and Molecular Medicine,Department of Molecular and Cellular Biology, andDan L. Duncan Cancer Center, Baylor College of Medicine, Houston, TX 77030 weeichil@bcm.edu.

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI DAVID R ROWLEY · 2007 to 2026
$73.9M
Hematology Training ProgramT32DK060445 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI GOODELL, MARGARET A. · 2002 to 2023
$8.3M
The ATM/E2F1 Pathway in DNA Damage and Growth ControlR01CA100857 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI LIN, WEEI-CHIN · 2004 to 2019
$4.8M
Therapeutic Targeting of Oncogenic Stress in Cancer TreatmentR01CA138641 · NCI · BAYLOR COLLEGE OF MEDICINE · PI LIN, WEEI-CHIN · 2010 to 2014
$1.5M
Howard Hughes Medical InstituteNCI NIH HHS 3 P30CA125123-03SNCI NIH HHS P30 CA125123NCI NIH HHS R01 CA100857NCI NIH HHS R01CA100857NCI NIH HHS R01 CA138641NCI NIH HHS R01CA138641NIDDK NIH HHS T32 DK060445NIDDK NIH HHS T32DK60445
6 · The paper itself

Abstract

Several ring between ring fingers (RBR) -domain proteins, such as Parkin and Parc, have been shown to be E3 ligases involved in important biological processes. Here, we identify a poorly characterized RBR protein, Ring Finger protein 144A (RNF144A), as the first, to our knowledge, mammalian E3 ubiquitin ligase for DNA-PKcs. We show that DNA damage induces RNF144A expression in a p53-dependent manner. RNF144A is mainly localized in the cytoplasmic vesicles and plasma membrane and interacts with cytoplasmic DNA-dependent protein kinase, catalytic subunit (DNA-PKcs). DNA-PKcs plays a critical role in the nonhomologous end-joining DNA repair pathway and provides prosurvival signaling during DNA damage. We show that RNF144A induces ubiquitination of DNA-PKcs in vitro and in vivo and promotes its degradation. Depletion of RNF144A leads to an increased level of DNA-PKcs and resistance to DNA damaging agents, which is reversed by a DNA-PK inhibitor. Taken together, our data suggest that RNF144A may be involved in p53-mediated apoptosis through down-regulation of DNA-PKcs when cells suffer from persistent or severe DNA damage insults.

Indexed as

ApoptosisBlotting, WesternCarrier ProteinsCatalytic DomainColony-Forming Units AssayDNA-Activated Protein KinaseDNA DamageDNA PrimersFluorescent Antibody TechniqueGene Expression Regulation, EnzymologicHEK293 CellsHumansImmunoprecipitationReal-Time Polymerase Chain ReactionReverse Transcriptase Polymerase Chain ReactionUbiquitin-Protein LigasesCarrier ProteinsDNA-Activated Protein KinaseDNA PrimersRNF144A protein, humanUbiquitin-Protein LigasesDDRendosometransmembrane domain

Identifiers

PMID24979766
PMCPMC4084471

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.