Evidence map›Paper›PMID 22413754›Full record

ArticleThe Biochemical journal2012

Functional analysis of the protein phosphatase activity of PTEN.

Xiaoqun Catherine Zhang, Antonella Piccini, Michael P Myers, Linda Van Aelst, Nicholas K Tonks

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. To Study the Role of PTEN, EGFR and HER2 in Early Glottic Squamous Cell Carcinoma.Indian journal of otolaryngology and head and neck surgery : official publication of the Association of Otolaryngologists of India · 2023
    Article
  9. Article
  10. The orchestrated signaling by PI3Kα and PTEN at the membrane interface.Computational and structural biotechnology journal · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Redox Regulation of PTEN by Peroxiredoxins.Antioxidants (Basel, Switzerland) · 2021
    Review
  15. Article
  16. Toward Systems Pathology for PTEN Diagnostics.Cold Spring Harbor perspectives in medicine · 2020
    Review
  17. Article
  18. The Role of PTEN in Neurodevelopment.Molecular neuropsychiatry · 2020
    Review
  19. Article
  20. Review

3 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

5 authors at 1 institution in 1 country.

Xiaoqun Catherine ZhangCold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.
Antonella Piccini
Michael P Myers
Linda Van Aelst
Nicholas K Tonks
Cold Spring Harbor Laboratory · US

Funding

Single-Cell Biology Shared ResourceP30CA045508 · NCI · COLD SPRING HARBOR LABORATORY · PI John Edward Moses · 1987 to 2026
$118.9M
PROTEIN TYROSINE DEPHOSPHORYLATION &SIGNAL TRANSDUCTIONR01CA053840 · NCI · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 1991 to 2025
$11.8M
Receptor PTPs, Cell Contract and Signal TransductionR01GM055989 · NIGMS · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 1997 to 2018
$6.7M
Protein Tyrosine Dephosphorylation &signal TransductionR37CA053840 · NCI · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 2001 to 2008
$5.2M
DOCK7 Signaling in Neuronal DevelopmentR01MH082808 · NIMH · COLD SPRING HARBOR LABORATORY · PI VAN AELST, LINDA · 2008 to 2017
$4.7M
Role of Dok-1 in oncogenic tyrosine kinase signalingR01CA135053 · NCI · COLD SPRING HARBOR LABORATORY · PI VAN AELST, LINDA · 2009 to 2013
$1.8M
NCI NIH HHS CA45508NCI NIH HHS CA53840NCI NIH HHS P30 CA045508NCI NIH HHS R01 CA053840NCI NIH HHS R01 CA135053NCI NIH HHS R37 CA053840NIGMS NIH HHS R01 GM055989NIMH NIH HHS MH082808NIMH NIH HHS R01 MH082808
6 · The paper itself

Abstract

In vitro, the tumour suppressor PTEN (phosphatase and tensin homologue deleted on chromosome 10) displays intrinsic phosphatase activity towards both protein and lipid substrates. In vivo, the lipid phosphatase activity of PTEN, through which it dephosphorylates the 3 position in the inositol sugar of phosphatidylinositol derivatives, is important for its tumour suppressor function; however, the significance of its protein phosphatase activity remains unclear. Using two-photon laser-scanning microscopy and biolistic gene delivery of GFP (green fluorescent protein)-tagged constructs into organotypic hippocampal slice cultures, we have developed an assay of PTEN function in living tissue. Using this bioassay, we have demonstrated that overexpression of wild-type PTEN led to a decrease in spine density in neurons. Furthermore, it was the protein phosphatase activity, but not the lipid phosphatase activity, of PTEN that was essential for this effect. The ability of PTEN to decrease neuronal spine density depended upon the phosphorylation status of serine and threonine residues in its C-terminal segment and the integrity of the C-terminal PDZ-binding motif. The present study reveals a new aspect of the function of this important tumour suppressor and suggest that, in addition to dephosphorylating the 3 position in phosphatidylinositol phospholipids, the critical protein substrate of PTEN may be PTEN itself.

Indexed as

Amino Acid SequenceAnimalsAnimals, NewbornDendritic SpinesEnzyme ActivationHippocampusMolecular Sequence DataOrgan Culture TechniquesPhosphoprotein PhosphatasesPTEN PhosphohydrolaseRatsPhosphoprotein PhosphatasesPTEN PhosphohydrolasePten protein, rat

Identifiers

PMID22413754
PMCPMC3365644
OpenAlexW2087415885

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.