Evidence map›Paper›PMID 41626692›Full record

ArticleNucleic acids research2026

Functional characterisation of tumour suppressor PDCD4 reveals previously undisclosed role in the control of cell adhesion.

Veronica Dezi, Robert F Harvey, Tom Smith, Cameron H Cole, Mariavittoria Pizzinga, Mark Stoneley, Gavin D Garland, Emilie Horvilleur, Lajos Kalmar, Ritwick Sawarkar and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

12 authors.

Veronica DeziMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Robert F HarveyMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Tom SmithMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Cameron H ColeMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Mariavittoria PizzingaMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Mark StoneleyMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Gavin D GarlandMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Emilie HorvilleurMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Lajos KalmarMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Ritwick SawarkarMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.
Kathryn S LilleyDepartment of Biochemistry, University of Cambridge, Gleeson Building, Tennis Court Rd, Cambridge CB2 1QRUK.
Anne E WillisMRC Toxicology Unit, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QRUK.ORCID 0000-0002-1470-8531

Funding

Cancer Research UK Technology G108392Medical Research Council core program funding MC_UU_00025/10Medical Research Council core program funding MC_UU_00025/7Medical Research Council core program funding MC_UU_00025/8MRC Core award Medical Research Council MC_UU_00025/10Wellcome Trust 110071/Z/15/ZWellcome Trust 110170/Z/15/Z
6 · The paper itself

Abstract

PDCD4 is a multifunctional RNA-binding protein that has tumour suppressor function. To more fully understand how dysregulation of this protein contributes to carcinogenesis, we have carried out a comprehensive analysis of the role of PDCD4 in RNA metabolism in untransformed epithelial cells. We show that PDCD4 predominantly localises in the nucleus, where it interacts with proteins involved in a range of different RNA metabolic processes. We find that PDCD4 knockdown is associated with significant changes in either the expression or splicing of a number of transcripts, although it appears to have an indirect role in splicing. We identified the RNA targets of PDCD4 using iCLIP and observed an enrichment in binding to transcripts encoding cell adhesion and structural proteins. Consistent with these data, we show that PDCD4 acts as a general regulator of cell adhesion, which in a tumour setting would increase the metastatic potential of cells, and demonstrate that the nuclear localisation of PDCD4 is crucial in this process. Overall, the information obtained in untransformed cells provides a new perspective for the role of PDCD4 as a tumour suppressor.

Indexed as

Apoptosis Regulatory ProteinsCell AdhesionRNA-Binding ProteinsTumor Suppressor ProteinsAnimalsCell LineCell NucleusHumansRNARNA SplicingApoptosis Regulatory ProteinsPDCD4 protein, humanRNARNA-Binding ProteinsTumor Suppressor Proteins

Identifiers

PMID41626692
PMCPMC12862386

What Socratic holds

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Registered trials

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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 Socratic graph.