Evidence map›Paper›PMID 25268038›Full record

ArticleThe Biochemical journal2014

DNA polymerase η is regulated by poly(rC)-binding protein 1 via mRNA stability.

Cong Ren, Seong-Jun Cho, Yong-Sam Jung, Xinbin Chen

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

9 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. PCBP1 depletion promotes tumorigenesis through attenuation of p27Journal of experimental & clinical cancer research : CR · 2018
    Article
  7. Review
  8. Review
  9. 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 at 1 institution in 1 country.

Cong Ren*Comparative Oncology Laboratory, Schools of Medicine and Veterinary Medicine, University of California at Davis, Davis, CA 95616, U.S.A.
Seong-Jun Cho*Comparative Oncology Laboratory, Schools of Medicine and Veterinary Medicine, University of California at Davis, Davis, CA 95616, U.S.A.
Yong-Sam Jung*Comparative Oncology Laboratory, Schools of Medicine and Veterinary Medicine, University of California at Davis, Davis, CA 95616, U.S.A.
Xinbin Chen*Comparative Oncology Laboratory, Schools of Medicine and Veterinary Medicine, University of California at Davis, Davis, CA 95616, U.S.A.
University of California, Davis · US

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
MECHANISM OF P73 DEPENDENT TUMOR SUPPRESSIONR01CA081237 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XINBIN · 1999 to 2022
$6.8M
Mechanism of p53-Mediated Tumor SuppressionR01CA076069 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XINBIN · 2002 to 2017
$4.5M
The role of DNA polymerase eta in DNA damage response and p53 activationR01CA123227 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XINBIN · 2010 to 2014
$1.4M
MECHANISM OF P53 DEPENDENT APOPTOSISR29CA076069 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHEN, XINBIN · 1998 to 2002
$276k
NCI NIH HHS CA076069NCI NIH HHS CA081237NCI NIH HHS CA123227NCI NIH HHS P30 CA093373NCI NIH HHS R01 CA076069NCI NIH HHS R01 CA081237NCI NIH HHS R01 CA123227NCI NIH HHS R29 CA076069
6 · The paper itself

Abstract

POLH (DNA polymerase η), a target of p53 tumour suppressor, plays a key role in TLS (translesion DNA synthesis). Loss of POLH is responsible for the human cancer-prone syndrome XPV (xeroderma pigmentosum variant). Owing to its critical role in DNA repair and genome stability, POLH expression and activity are regulated by multiple pathways. In the present study, we found that the levels of both POLH transcript and protein were decreased upon knockdown of the transcript encoding PCBP1 [poly(rC)-binding protein 1]. We also found that the half-life of POLH mRNA was markedly decreased upon knockdown of PCBP1. Moreover, we found that PCBP1 directly bound to the POLH 3'-UTR and the PCBP1-binding site in POLH mRNA is an atypical AU-rich element. Finally, we showed that the AU-rich element in POLH 3'-UTR was responsive to PCBP1 and sufficient for PCBP1 to regulate POLH expression. Taken together, we uncovered a novel mechanism by which POLH expression is controlled by PCBP1 via mRNA stability.

Indexed as

3' Untranslated RegionsCell Line, TumorDNA-Binding ProteinsDNA-Directed DNA PolymeraseGene Expression Regulation, NeoplasticGene Knockdown TechniquesHCT116 CellsHEK293 CellsHeterogeneous-Nuclear RibonucleoproteinsHumansMCF-7 CellsProtein BindingRNA-Binding ProteinsRNA, MessengerRNA StabilityY-Family DNA Polymerases3' Untranslated RegionsDNA-Binding ProteinsDNA-Directed DNA PolymeraseHeterogeneous-Nuclear RibonucleoproteinsPCBP1 protein, humanRad30 proteinRNA-Binding ProteinsRNA, MessengerY-Family DNA Polymerases

Identifiers

PMID25268038
PMCPMC4562393
OpenAlexW2328022485

What OpenQuestion holds

Textmetadata
LicenceTDM
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.