Evidence map›Paper›PMID 17240336›Full record

ArticleCurrent biology : CB2007

PtdIns(3,4,5)P(3)-dependent and -independent roles for PTEN in the control of cell migration.

Nick R Leslie, Xuesong Yang, C Peter Downes, Cornelis J Weijer

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

91 citing papers in PubMed, 217 citations in OpenAlex.

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  6. Voltage sensors.Molecular pharmacology · 2025
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  15. Redox Regulation of PTEN by Peroxiredoxins.Antioxidants (Basel, Switzerland) · 2021
    Review
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  17. Article
  18. Review
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  20. Article

31 more citing papers are in PubMed but not listed here.

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.

Nick R LeslieDivision of Molecular Physiology, University of Dundee, Dundee, DD1 5EH, Scotland, United Kingdom. n.r.leslie@dundee.ac.uk
Xuesong Yang
C Peter Downes
Cornelis J Weijer
University of Dundee · GB

Funding

Medical Research Council G9403619Wellcome Trust
6 · The paper itself

Abstract

backgroundPhosphatase and tensin homolog (PTEN) mediates many of its effects on proliferation, growth, survival, and migration through its PtdIns(3,4,5)P(3) lipid phosphatase activity, suppressing phosphoinositide 3-kinase (PI3K)-dependent signaling pathways. PTEN also possesses a protein phosphatase activity, the role of which is less well characterized.

resultsWe have investigated the role of PTEN in the control of cell migration of mesoderm cells ingressing through the primitive streak in the chick embryo. Overexpression of PTEN strongly inhibits the epithelial-to-mesenchymal transition (EMT) of mesoderm cells ingressing through the anterior and middle primitive streak, but it does not affect EMT of cells located in the posterior streak. The inhibitory activity on EMT is completely dependent on targeting PTEN through its C-terminal PDZ binding site, but can be achieved by a PTEN mutant (PTEN G129E) with only protein phosphatase activity. Expression either of PTEN lacking the PDZ binding site or of the PTEN C2 domain, or inhibition of PI3K through specific inhibitors, does not inhibit EMT, but results in a loss of both cell polarity and directional migration of mesoderm cells. The PTEN-related protein TPTE, which normally lacks any detectable lipid and protein phosphatase activity, can be reactivated through mutation, and only this reactivated mutant leads to nondirectional migration of these cells in vivo.

conclusionsPTEN modulates cell migration of mesoderm cells in the chick embryo through at least two distinct mechanisms: controlling EMT, which involves its protein phosphatase activity; and controlling the directional motility of mesoderm cells, through its lipid phosphatase activity.

Indexed as

AnimalsCell MovementChick EmbryoGastrulaMesodermPhosphatidylinositol PhosphatesProtein Structure, TertiaryPTEN PhosphohydrolasePhosphatidylinositol PhosphatesPTEN Phosphohydrolase

Identifiers

PMID17240336
PMCPMC1885949
OpenAlexW2098141125

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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 OpenQuestion graph.