Evidence map›Paper›PMID 19805145›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

E3 ubiquitin ligase COP1 regulates the stability and functions of MTA1.

Da-Qiang Li, Kazufumi Ohshiro, Sirigiri Divijendra Natha Reddy, Suresh B Pakala, Mong-Hong Lee, Yanping Zhang, Suresh K Rayala, Rakesh Kumar

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. IntegratingFrontiers in immunology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. A COP1-GATA2 axis suppresses AR signaling and prostate cancer.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. EGF Relays Signals to COP1 and Facilitates FOXO4 Degradation to Promote Tumorigenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. E3 ubiquitin ligase RFWD2 controls lung branching through protein-level regulation of ETV transcription factors.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. 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

8 authors.

Da-Qiang LiDepartment of Biochemistry and Molecular Biology and Institute of Coregulator Biology, The George Washington University Medical Center, Washington, DC 20037, USA.
Kazufumi Ohshiro
Sirigiri Divijendra Natha Reddy
Suresh B Pakala
Mong-Hong Lee
Yanping Zhang
Suresh K Rayala
Rakesh Kumar

Funding

Regulation of MDM2 by the ribosomal protein L11R01CA100302 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YANPING · 2003 to 2013
$3.2M
Role of Metastatic Tumor Antigen-1 in Mammary GlandR01CA098823 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI KUMAR, RAKESH · 2003 to 2013
$3.1M
Regulation of cyclin-dependent kinase inhibitor p27 in cancerR01CA089266 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI LEE, MONG-HONG · 2002 to 2013
$2.8M
In vivo function of Mdm2 E3 ubiquitin ligaseR01CA127770 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YANPING · 2008 to 2013
$1.5M
NCI NIH HHS CA98823NCI NIH HHS R01 CA089266NCI NIH HHS R01 CA098823NCI NIH HHS R01 CA100302NCI NIH HHS R01 CA127770
6 · The paper itself

Abstract

Metastasis-associated protein 1 (MTA1), a component of the nucleosome remodeling and histone deacetylation (NuRD) complex, is widely upregulated in human cancers. However, the mechanism for regulating its protein stability remains unknown. Here we report that MTA1 is an ubiquitinated protein and targeted by the RING-finger E3 ubiquitin-protein ligase constitutive photomorphogenesis protein 1 (COP1) for degradation via the ubiquitin-proteasome pathway. Induced expression of wild-type COP1 but not its RING motif mutants promotes the ubiquitination and degradation of MTA1, indicating that the ligase activity is required for the COP1-mediated proteolysis of MTA1. Conversely, depletion of endogenous COP1 resulted in a marked decrease in MTA1 ubiquitination, accompanied by a pronounced accumulation of MTA1 protein. MTA1, in turn, destabilizes COP1 by promoting its autoubiquitination, thus creating a tight feedback loop that regulates both MTA1 and COP1 protein stability. Accordingly, disruption of the COP1-mediated proteolysis by ionizing radiation leads to MTA1 stabilization, accompanied by an increased coregulatory function of MTA1 on its target. Furthermore, we discovered that MTA1 is required for optimum DNA double-strand break repair after ionizing radiation. These findings provide novel insights into the regulation of MTA1 protein and reveal a novel function of MTA1 in DNA damage response.

Indexed as

AnimalsCell LineDNA DamageDNA RepairEnzyme StabilityFibroblastsHistone DeacetylasesHumansMiceNuclear ProteinsRadiation, IonizingRepressor ProteinsTrans-ActivatorsTranscription FactorsUbiquitinUbiquitin-Protein LigasesCOP1 protein, humanCOP1 protein, mouseHistone DeacetylasesMTA1 protein, humanMta1 protein, mouseNuclear ProteinsRepressor ProteinsTrans-ActivatorsTranscription FactorsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID19805145
PMCPMC2762678

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.