Evidence map›Paper›PMID 19767745›Full record

ArticleNature cell biology2009

MyosinV controls PTEN function and neuronal cell size.

Michiel T van Diepen, Maddy Parsons, C Peter Downes, Nicholas R Leslie, Robert Hindges, Britta J Eickholt

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

55 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
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  8. Review
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  11. Review
  12. Posttranslational Regulation and Conformational Plasticity of PTEN.Cold Spring Harbor perspectives in medicine · 2020
    Review
  13. Article
  14. An update on PTEN modulators - a patent review.Expert opinion on therapeutic patents · 2019
    Review
  15. Regulation and modulation of PTEN activity.Molecular biology reports · 2018
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Michiel T van DiepenMRC Centre for Developmental Neurobiology, New Hunt's House, King's College London, London SE1 1UL, UK.
Maddy Parsons
C Peter Downes
Nicholas R Leslie
Robert Hindges
Britta J Eickholt
King's College London · GBUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C514307/1Medical Research Council G0801865Medical Research Council G9403619
6 · The paper itself

Abstract

The tumour suppressor PTEN can inhibit cell proliferation and migration as well as control cell growth, in different cell types. PTEN functions predominately as a lipid phosphatase, converting PtdIns(3,4,5)P(3) to PtdIns(4,5)P(2), thereby antagonizing PI(3)K (phosphoinositide 3-kinase) and its established downstream effector pathways. However, much is unclear concerning the mechanisms that regulate PTEN movement to the cell membrane, which is necessary for its activity towards PtdIns(3,4,5)P(3) (Refs 3, 4, 5). Here we show a requirement for functional motor proteins in the control of PI3K signalling, involving a previously unknown association between PTEN and myosinV. FRET (Förster resonance energy transfer) measurements revealed that PTEN interacts directly with myosinV, which is dependent on PTEN phosphorylation mediated by CK2 and/or GSK3. Inactivation of myosinV-transport function in neurons increased cell size, which, in line with known attributes of PTEN-loss, required PI(3)K and mTor. Our data demonstrate a myosin-based transport mechanism that regulates PTEN function, providing new insights into the signalling networks regulating cell growth.

Indexed as

Cell SizeAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsAspartic AcidBinding SitesCells, CulturedGlycogen Synthase Kinase 3Green Fluorescent ProteinsHippocampusMiceModels, BiologicalMolecular Sequence DataMyosin Type VNeuronsAlanineAspartic AcidCKT2 protein, mouseGlycogen Synthase Kinase 3Green Fluorescent ProteinsMyosin Type VPhosphatidylinositol 3-KinasesPhosphoproteinsPTEN PhosphohydrolasePten protein, mouse

Identifiers

PMID19767745
PMCPMC2756284
OpenAlexW1988141599

What OpenQuestion holds

Textmetadata
LicenceTDM
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.