Evidence map›Paper›PMID 25211206›Full record

ArticlePLoS computational biology2014

PTEN hopping on the cell membrane is regulated via a positively-charged C2 domain.

Masato Yasui, Satomi Matsuoka, Masahiro Ueda

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Spontaneous signal generation by an excitable system for cell migration.Frontiers in cell and developmental biology · 2024
    Review
  5. Article
  6. When PIPFrontiers in cell and developmental biology · 2022
    Review
  7. Structural Mechanisms of PTEN Regulation.Cold Spring Harbor perspectives in medicine · 2020
    Review
  8. Single-molecule imaging of PI(4,5)PCommunications biology · 2020
    Article
  9. Article
  10. Monitoring single-cell bioluminescence ofPlant biotechnology (Tokyo, Japan) · 2019
    Article
  11. Review
  12. Collective cell migration ofCommunications biology · 2019
    Article
  13. Article
  14. OverexpressingOncotarget · 2018
    Article
  15. Article
  16. Review
  17. Article
  18. Strange kinetics of bulk-mediated diffusion on lipid bilayers.Physical chemistry chemical physics : PCCP · 2016
    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

3 authors at 2 institutions in 1 country.

Masato YasuiLaboratories for Nanobiology, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan; Laboratory for Cell Signaling Dynamics, QBiC (Quantitative Biology Center), RIKEN, Suita, Osaka, Japan; Laboratory of Single Molecule Biology, Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka, Japan.
Satomi MatsuokaLaboratory for Cell Signaling Dynamics, QBiC (Quantitative Biology Center), RIKEN, Suita, Osaka, Japan.
Masahiro UedaLaboratories for Nanobiology, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan; Laboratory for Cell Signaling Dynamics, QBiC (Quantitative Biology Center), RIKEN, Suita, Osaka, Japan; Laboratory of Single Molecule Biology, Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka, Japan.
RIKEN Center for Biosystems Dynamics Research · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PTEN, a tumor suppressor that is frequently mutated in a wide spectrum of cancers, exerts PI(3,4,5)P3 phosphatase activities that are regulated by its dynamic shuttling between the membrane and cytoplasm. Direct observation of PTEN in the interfacial environment can offer quantitative information about the shuttling dynamics, but remains elusive. Here we show that positively charged residues located in the cα2 helix of the C2 domain are necessary for the membrane localization of PTEN via stable electrostatic interactions in Dictyostelium discoideum. Single-molecule imaging analyses revealed that PTEN molecules moved distances much larger than expected had they been caused by lateral diffusion, a phenomenon we call "hopping." Our novel single-particle tracking analysis method found that the cα2 helix aids in regulating the hopping and stable-binding states. The dynamically established membrane localization of PTEN was revealed to be essential for developmental processes and clarified a fundamental regulation mechanism of the protein quantity and activity on the plasma membrane.

Indexed as

Cell MembraneDictyosteliumHumansProtein Structure, TertiaryPTEN PhosphohydrolaseStatic ElectricityPTEN Phosphohydrolase

Identifiers

PMID25211206
PMCPMC4161299
OpenAlexW2014528848

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.