Evidence map›Paper›PMID 24416409›Full record

ArticlePloS one2014

The prolyl isomerase pin1 regulates mRNA levels of genes with short half-lives by targeting specific RNA binding proteins.

Nithya Krishnan, Mark A Titus, Roopa Thapar

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  9. Review
  10. Pinning Down the Transcription: A Role for Peptidyl-ProlylFrontiers in cell and developmental biology · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015
    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

3 authors at 3 institutions in 1 country.

Nithya KrishnanHauptman-Woodward Medical Research Institute, SUNY at Buffalo, New York, United States of America.
Mark A TitusDepartment of Genitourinary Medical Oncology, The University of Texas M.D. Anderson Cancer Center, Houston, Texas, United States of America.
Roopa ThaparHauptman-Woodward Medical Research Institute, SUNY at Buffalo, New York, United States of America ; Department of Structural Biology, SUNY at Buffalo, New York, United States of America ; Department of Biochemistry and Cell Biology, Rice University, Houston, Texas, United States of America.
Hauptman-Woodward Medical Research Institute · USThe University of Texas MD Anderson Cancer Center · USUniversity at Buffalo, State University of New York · US

Funding

Phosphorylation dependent recognition of a histone mRNA hairpin by SLBPR01GM076660 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MARZLUFF, WILLIAM F. · 2006 to 2009
$1.1M
NIGMS NIH HHS 1R01-GM076660NIGMS NIH HHS R01 GM076660
6 · The paper itself

Abstract

The peptidyl-prolyl isomerase Pin1 is over-expressed in several cancer tissues is a potential prognostic marker in prostate cancer, and Pin1 ablation can suppress tumorigenesis in breast and prostate cancers. Pin1 can co-operate with activated ErbB2 or Ras to enhance tumorigenesis. It does so by regulating the activity of proteins that are essential for gene expression and cell proliferation. Several targets of Pin1 such as c-Myc, the Androgen Receptor, Estrogen Receptor-alpha, Cyclin D1, Cyclin E, p53, RAF kinase and NCOA3 are deregulated in cancer. At the posttranscriptional level, emerging evidence indicates that Pin1 also regulates mRNA decay of histone mRNAs, GM-CSF, Pth, and TGFβ mRNAs by interacting with the histone mRNA specific protein SLBP, and the ARE-binding proteins AUF1 and KSRP, respectively. To understand how Pin1 may affect mRNA abundance on a genome-wide scale in mammalian cells, we used RNAi along with DNA microarrays to identify genes whose abundance is significantly altered in response to a Pin1 knockdown. Functional scoring of differentially expressed genes showed that Pin1 gene targets control cell adhesion, leukocyte migration, the phosphatidylinositol signaling system and DNA replication. Several mRNAs whose abundance was significantly altered by Pin1 knockdown contained AU-rich element (ARE) sequences in their 3' untranslated regions. We identified HuR and AUF1 as Pin1 interacting ARE-binding proteins in vivo. Pin1 was also found to stabilize all core histone mRNAs in this study, thereby validating our results from a previously published study. Statistical analysis suggests that Pin1 may target the decay of essential mRNAs that are inherently unstable and have short to medium half-lives. Thus, this study shows that an important biological role of Pin1 is to regulate mRNA abundance and stability by interacting with specific RNA-binding proteins that may play a role in cancer progression.

Indexed as

Genome, HumanCell AdhesionCell MovementCell ProliferationDNA ReplicationELAV ProteinsGene Expression ProfilingGene Expression RegulationGene Knockdown TechniquesHalf-LifeHEK293 CellsHeLa CellsHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0HistonesHumansELAV ProteinsHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0HistonesHNRNPD protein, humanNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphatidylinositolsPIN1 protein, humanRNA, MessengerRNA, Small Interfering

Identifiers

PMID24416409
PMCPMC3887067
OpenAlexW2117006449

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.