Evidence map›Paper›PMID 24200966›Full record

ArticleCell cycle (Georgetown, Tex.)2014

DDB2 association with PCNA is required for its degradation after UV-induced DNA damage.

Ornella Cazzalini, Paola Perucca, Roberto Mocchi, Sabrina Sommatis, Ennio Prosperi, Lucia Anna Stivala

Expression of concernOpen access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It carries an expression of concern. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Revisiting the Function of p21International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Emerging Roles of DDB2 in Cancer.International journal of molecular sciences · 2019
    Review
  12. Human CRL4Oncotarget · 2017
    Article
  13. Decision for cell fate: deubiquitinating enzymes in cell cycle checkpoint.Cellular and molecular life sciences : CMLS · 2016
    Review
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Ornella CazzaliniDipartimento di Medicina Molecolare; Unità di Immunologia e Patologia Generale; Università di Pavia; Pavia, Italy.
Paola PeruccaDipartimento di Medicina Molecolare; Unità di Immunologia e Patologia Generale; Università di Pavia; Pavia, Italy.
Roberto MocchiDipartimento di Medicina Molecolare; Unità di Immunologia e Patologia Generale; Università di Pavia; Pavia, Italy.
Sabrina SommatisDipartimento di Medicina Molecolare; Unità di Immunologia e Patologia Generale; Università di Pavia; Pavia, Italy.
Ennio ProsperiIstituto di Genetica Molecolare (IGM) del CNR; Pavia, Italy.
Lucia Anna StivalaDipartimento di Medicina Molecolare; Unità di Immunologia e Patologia Generale; Università di Pavia; Pavia, Italy.
University of Pavia · ITIstituto di Genetica Molecolare · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DDB2 is a protein playing an essential role in the lesion recognition step of the global genome sub-pathway of nucleotide excision repair (GG-NER) process. Among the proteins involved in the DNA damage response, p21(CDKN1A) (p21) has been reported to participate in NER, but also to be removed by proteolytic degradation, thanks to its association with PCNA. DDB2 is involved in the CUL4-DDB1 complex mediating p21 degradation; however, the direct interaction between DDB2, p21 and PCNA has been never investigated. Here, we show that DDB2 co-localizes with PCNA and p21 at local UV-induced DNA-damage sites, and these proteins co-immunoprecipitate in the same complex. In addition, we provide evidence that p21 is not able to bind directly DDB2, but, to this end, the presence of PCNA is required. Direct physical association of recombinant DDB2 protein with PCNA is mediated by a conserved PIP-box present in the N-terminal region of DDB2. Mutation of the PIP-box resulted in the loss of protein interaction. Interestingly, the same mutation, or depletion of PCNA by RNA interference, greatly impaired DDB2 degradation induced by UV irradiation. These results indicate that DDB2 is a PCNA-binding protein, and that this association is required for DDB2 proteolytic degradation.

Indexed as

DNA DamageAmino Acid SequenceCyclin-Dependent Kinase Inhibitor p21DNA-Binding ProteinsHeLa CellsHumansMolecular Sequence DataMutationProliferating Cell Nuclear AntigenProtein BindingProteolysisRecombinant ProteinsUltraviolet RaysCDKN1A protein, humanCyclin-Dependent Kinase Inhibitor p21DDB2 protein, humanDNA-Binding ProteinsProliferating Cell Nuclear AntigenRecombinant ProteinsDDB2Nucleotide Excision Repairp21CDKN1APCNAUV damage

Identifiers

PMID24200966
PMCPMC3906241
OpenAlexW2041766735

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.