Evidence map›Paper›PMID 11564859›Full record

ArticleMolecular and cellular biology2001

The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells.

A Nag, T Bondar, S Shiv, P Raychaudhuri

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

87 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Emerging Roles of DDB2 in Cancer.International journal of molecular sciences · 2019
    Review
  6. Article
  7. Review
  8. The emerging role for Cullin 4 family of E3 ligases in tumorigenesis.Biochimica et biophysica acta. Reviews on cancer · 2019
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Orchestral maneuvers at the damaged sites in nucleotide excision repair.Cellular and molecular life sciences : CMLS · 2015
    Review

27 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

A NagDepartment of Biochemistry and Molecular Biology (M/C 536), University of Illinois at Chicago, Chicago, Illinois 60612, USA.
T Bondar
S Shiv
P Raychaudhuri
University of Illinois Chicago · US

Funding

Role of DDB in Checkpoint Control and CarcinogenesisR01CA077637 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI RAYCHAUDHURI, PRADIP · 1999 to 2014
$3.6M
ROLE OF CULLIN 4A IN TUMOR DEVELOPMENT.R01CA088863 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI RAYCHAUDHURI, PRADIP · 2001 to 2005
$1.2M
NCI NIH HHS CA77637NCI NIH HHS CA88863NCI NIH HHS R01 CA077637NCI NIH HHS R01 CA088863
6 · The paper itself

Abstract

The damaged-DNA binding protein DDB consists of two subunits, DDB1 (127 kDa) and DDB2 (48 kDa). Mutations in the DDB2 subunit have been detected in patients suffering from the repair deficiency disease xeroderma pigmentosum (group E). In addition, recent studies suggested a role for DDB2 in global genomic repair. DDB2 also exhibits transcriptional activity. We showed that expression of DDB1 and DDB2 stimulated the activity of the cell cycle regulatory transcription factor E2F1. Here we show that DDB2 is a cell cycle-regulated protein. It is present at a low level in growth-arrested primary fibroblasts, and after release the level peaks at the G(1)/S boundary. The cell cycle regulation of DDB2 involves posttranscriptional mechanisms. Moreover, we find that an inhibitor of 26S proteasome increases the level of DDB2, suggesting that it is regulated by the ubiquitin-proteasome pathway. Our previous study indicated that the cullin family protein Cul-4A associates with the DDB2 subunit. Because cullins are involved in the ubiquitin-proteasome pathway, we investigated the role of Cul-4A in regulating DDB2. Here we show that DDB2 is a specific target of Cul-4A. Coexpression of Cul-4A, but not Cul-1 or other highly related cullins, increases the ubiquitination and the decay rate of DDB2. A naturally occurring mutant of DDB2 (2RO), which does not bind Cul-4A, is not affected by coexpression of Cul-4A. Studies presented here identify a specific function of the Cul-4A gene, which is amplified and overexpressed in breast cancers.

Indexed as

Cell Cycle ProteinsCullin ProteinsProteasome Endopeptidase ComplexAnimalsBlotting, WesternCell CycleCell LineCell NucleusCycloheximideDNADNA-Binding ProteinsDNA, ComplementaryDNA RepairE2F1 Transcription FactorE2F Transcription FactorsFibroblastsATP dependent 26S proteaseCell Cycle ProteinsCUL4A protein, humanCullin ProteinsCycloheximideDDB1 protein, humanDDB2 protein, humanDNADNA-Binding ProteinsDNA, ComplementaryE2F1 protein, humanE2F1 Transcription FactorE2F Transcription FactorsNeoplasm ProteinsPeptide HydrolasesProteasome Endopeptidase ComplexProtein Synthesis InhibitorsRibonucleasesTranscription FactorsUbiquitins

Identifiers

PMID11564859
PMCPMC99852
OpenAlexW2136470788

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.