Evidence map›Paper›PMID 42472659›Full record

ArticleCancer science2026

Evidence That the Protein Phosphatase Activity of PTEN Contributes to Embryonic Development and Tumor Suppression.

Priyanka Tibarewal, Laura Spinelli, Nisha Kriplani, Helen Wise, Nadege Poncet, Giulia Marzano, Karen E Anderson, Katarzyna M Grzes, Zofia Varyova, Mahreen Adil and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cancer science, 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. 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

17 authors.

Priyanka TibarewalInstitute of Biological Chemistry, Biophysics and Bioengineering, Heriot Watt University, Edinburgh, UK.
Laura SpinelliInstitute of Biological Chemistry, Biophysics and Bioengineering, Heriot Watt University, Edinburgh, UK.
Nisha KriplaniInstitute of Biological Chemistry, Biophysics and Bioengineering, Heriot Watt University, Edinburgh, UK.
Helen WiseInstitute of Biological Chemistry, Biophysics and Bioengineering, Heriot Watt University, Edinburgh, UK.
Nadege PoncetDivision of Cell Signalling and Immunology, Faculty of Life Sciences, University of Dundee, Dundee, UK.
Giulia MarzanoInstitute of Biological Chemistry, Biophysics and Bioengineering, Heriot Watt University, Edinburgh, UK.
Karen E AndersonInositide Laboratory, Babraham Institute, Cambridge, UK.ORCID https://orcid.org/0000-0002-7394-6660
Katarzyna M GrzesDivision of Cell Signalling and Immunology, Faculty of Life Sciences, University of Dundee, Dundee, UK.
Zofia VaryovaCancer Institute, University College London, London, UK.
Mahreen AdilCancer Institute, University College London, London, UK.
C Peter DownesDivision of Cell Signalling and Immunology, Faculty of Life Sciences, University of Dundee, Dundee, UK.
Phillip T HawkinsInositide Laboratory, Babraham Institute, Cambridge, UK.
Len R StephensInositide Laboratory, Babraham Institute, Cambridge, UK.
Kate G StoreyDivision of Molecular, Cell and Developmental Biology, Faculty of Life Sciences, University of Dundee, Dundee, UK.
Doreen A CantrellDivision of Cell Signalling and Immunology, Faculty of Life Sciences, University of Dundee, Dundee, UK.
Bart VanhaesebroeckCancer Institute, University College London, London, UK.
Nicholas R LeslieInstitute of Biological Chemistry, Biophysics and Bioengineering, Heriot Watt University, Edinburgh, UK.ORCID https://orcid.org/0000-0001-5131-0541

Funding

Medical Research Council G0801865
6 · The paper itself

Abstract

PTEN (phosphatase and tensin homolog deleted on chromosome ten) is a tumor suppressor, the function of which is impaired in many diverse cancers. It has phosphoinositide lipid phosphatase activity by which it suppresses activation of the oncogenic PI3K signaling network but in vitro also displays activity against protein substrates and is able to auto-dephosphorylate its Thr366 residue. Here we generate germline knock-in mice expressing PTEN-Y138L, a mutant enzyme which selectively lacks protein phosphatase activity and retains lipid phosphatase activity. Homozygous Pten

Indexed as

AKTmicephosphatasePI3KPTEN

Identifiers

PMID42472659
PMCPMC13394760

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.