Evidence map›Paper›PMID 30367048›Full record

ArticleNature communications2018

Mutual inhibition between PTEN and PIP3 generates bistability for polarity in motile cells.

Satomi Matsuoka, Masahiro Ueda

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.6field-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

44 citing papers in PubMed, 109 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Signaling and actin waves at a glance.Journal of cell science · 2025
    Review
  7. Article
  8. Spatiotemporal distribution of PTEN before directed cell migration in monolayers.In vitro cellular & developmental biology. Animal · 2024
    Article
  9. Article
  10. Article
  11. Nonlinear dynamics in phosphoinositide metabolism.Current opinion in cell biology · 2024
    Review
  12. Article
  13. Article
  14. Review
  15. Spontaneous signal generation by an excitable system for cell migration.Frontiers in cell and developmental biology · 2024
    Review
  16. Article
  17. Reactive Oxygen Species andAntioxidants (Basel, Switzerland) · 2023
    Review
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Satomi MatsuokaLaboratory for Cell Signaling Dynamics, RIKEN QBiC, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan. s.matsuoka@riken.jp.ORCID http://orcid.org/0000-0002-4552-4460
Masahiro UedaLaboratory for Cell Signaling Dynamics, RIKEN QBiC, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan.ORCID http://orcid.org/0000-0002-9354-3404
RIKEN Center for Biosystems Dynamics Research · JP

Funding

Japan Agency for Medical Research and Development (AMED) JP17gm0910001Japan Society for the Promotion of Science (JSPS) JP25871120
6 · The paper itself

Abstract

Phosphatidylinositol 3,4,5-trisphosphate (PIP3) and PIP3 phosphatase (PTEN) are enriched mutually exclusively on the anterior and posterior membranes of eukaryotic motile cells. However, the mechanism that causes this spatial separation between the two molecules is unknown. Here we develop a method to manipulate PIP3 levels in living cells and used it to show PIP3 suppresses the membrane localization of PTEN. Single-molecule measurements of membrane-association and -dissociation kinetics and of lateral diffusion reveal that PIP3 suppresses the PTEN binding site required for stable PTEN membrane binding. Mutual inhibition between PIP3 and PTEN provides a mechanistic basis for bistability that creates a PIP3-enriched/PTEN-excluded state and a PTEN-enriched/PIP3-excluded state underlying the strict spatial separation between PIP3 and PTEN. The PTEN binding site also mediates the suppression of PTEN membrane localization in chemotactic signaling. These results illustrate that the PIP3-PTEN bistable system underlies a cell's decision-making for directional movement irrespective of the environment.

Indexed as

Binding SitesCell CompartmentationCell MembraneCell MovementCell PolarityChemotaxisCyclic AMPDictyosteliumKineticsModels, BiologicalMutationPhosphatidylinositol PhosphatesProtein BindingProtozoan ProteinsPTEN PhosphohydrolaseSignal TransductionCyclic AMPphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol PhosphatesProtozoan ProteinsPTEN Phosphohydrolase

Identifiers

PMID30367048
PMCPMC6203803
OpenAlexW2896622321

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.