Evidence map›Paper›PMID 25723571›Full record

ArticlePloS one2015

MDM2-mediated degradation of p14ARF: a novel mechanism to control ARF levels in cancer cells.

Maria Vivo, Maria Matarese, Maria Sepe, Rosaria Di Martino, Luisa Festa, Viola Calabrò, Girolama La Mantia, Alessandra Pollice

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  13. BioMed research international · 2017
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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 at 1 institution in 1 country.

Maria VivoDipartimento di Biologia, Università di Napoli Federico II, Naples, Italy.
Maria MatareseDipartimento di Biologia, Università di Napoli Federico II, Naples, Italy; Istituto di Genetica e Biofisica (IGB)-Consiglio Nazionale delle Ricerche (CNR), Naples, Italy.
Maria SepeDipartimento di Biologia, Università di Napoli Federico II, Naples, Italy; Dipartimento di Medicina Molecolare e Biotecnologie Mediche- Università di Napoli Federico II, Naples, Italy.
Rosaria Di MartinoDipartimento di Biologia, Università di Napoli Federico II, Naples, Italy; Istituto di Biochimica delle Proteine (IBP)-Consiglio Nazionale delle Ricerche (CNR), Naples, Italy.
Luisa FestaDipartimento di Biologia, Università di Napoli Federico II, Naples, Italy; Diagnostica e Farmaceutica Molecolare- Consiglio Nazionale delle Ricerche (CNR), Naples, Italy.
Viola CalabròDipartimento di Biologia, Università di Napoli Federico II, Naples, Italy.
Girolama La MantiaDipartimento di Biologia, Università di Napoli Federico II, Naples, Italy.
Alessandra PolliceDipartimento di Biologia, Università di Napoli Federico II, Naples, Italy.
University of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We here show a new relationship between the human p14ARF oncosuppressor and the MDM2 oncoprotein. MDM2 overexpression in various cancer cell lines causes p14ARF reduction inducing its degradation through the proteasome. The effect does not require the ubiquitin ligase activity of MDM2 and preferentially occurs in the cytoplasm. Interestingly, treatment with inhibitors of the PKC (Protein Kinase C) pathway and use of p14ARF phosphorylation mutants indicate that ARF phosphorylation could play a role in MDM2 mediated ARF degradation reinforcing our previous observations that ARF phosphorylation influences its stability and biological activity. Our study uncovers a new potentially important mechanism through which ARF and MDM2 can counterbalance each other during the tumorigenic process.

Indexed as

Cell Line, TumorCell Transformation, NeoplasticCytoplasmEnzyme ActivationGene ExpressionGene SilencingHumansNeoplasmsProteasome Endopeptidase ComplexProtein BindingProtein Interaction Domains and MotifsProtein Kinase CProtein TransportProteolysisProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p14ARFProteasome Endopeptidase ComplexProtein Kinase CProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p14ARF

Identifiers

PMID25723571
PMCPMC4344200
OpenAlexW2039278293

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.