Evidence map›Paper›PMID 10585883›Full record

ArticleThe Biochemical journal1999

The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo.

A Gray, J Van Der Kaay, C P Downes

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing 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

83 citing papers in PubMed, 194 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Phafins Are More Than Phosphoinositide-Binding Proteins.International journal of molecular sciences · 2023
    Review
  9. PI3Kα Translocation Mediates Nuclear PtdIns(3,4,5)PMolecular & cellular proteomics : MCP · 2023
    Article
  10. An update on genetically encoded lipid biosensors.Molecular biology of the cell · 2022
    Article
  11. GLUT4 On the move.The Biochemical journal · 2022
    Article
  12. Class I PI3K Biology.Current topics in microbiology and immunology · 2022
    Article
  13. Article
  14. Review
  15. Review
  16. Quantification of Genetically Encoded Lipid Biosensors.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  17. Article
  18. Review
  19. Article
  20. Genetically encoded lipid biosensors.Molecular biology of the cell · 2018
    Article

23 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

3 authors at 1 institution in 1 country.

A GrayDepartment of Biochemistry, University of Dundee, Dundee DD1 5EH, Scotland, U.K. agray@bad.dundee.ac.uk
J Van Der Kaay
C P Downes
University of Dundee · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have tested the binding specificities of the pleckstrin homology (PH) domains of protein kinase B (PKB) and GRP1 (general receptor for phosphoinositides-1), expressed as green fluorescent protein (GFP) fusion proteins [PH(PKB)GFP and PH(GRP1)GFP respectively] in HEK 293 cells and Swiss 3T3 cells, using confocal microscopy. Stimulation of HEK 293 cells with insulin caused a small, but sustained, increase in PtdIns(3,4,5)P(3) levels, detected using a radioligand displacement assay, which was mirrored by the translocation of PH(PKB)GFP and PH(GRP1)GFP from the cytosol to the plasma membrane of live, transfected cells. Similar results were obtained using Swiss 3T3 cells stimulated with platelet-derived growth factor (PDGF) and expressing either PH(PKB)GFP or PH(GRP1)GFP. Biochemical analyses confirmed the accumulation of both PtdIns(3,4,5)P(3) and PtdIns(3,4)P(2) in response to PDGF, but only the latter was present at increased levels in Swiss 3T3 cells 30 min after an oxidative stress (1 mM H(2)O(2)). Concomitantly, only PH(PKB)GFP, and not PH(GRP1)GFP, was localized at plasma membranes after 30 min of treatment with H(2)O(2). The fusion proteins appear accurately to report the spatial and temporal distribution of PtdIns(3,4,5)P(3) and PtdIns(3,4)P(2) in intact cells. These results establish the lipid selectivity of these PH domains in vivo, and further emphasize the overlapping, but distinct, second messenger roles of PtdIns(3,4,5)P(3) and PtdIns(3,4)P(2).

Indexed as

Protein Serine-Threonine KinasesAndrostadienesAnimalsCell LineCell MembraneFluorescent DyesGreen Fluorescent ProteinsHumansHydrogen PeroxideInsulinLipidsLuminescent ProteinsMiceMicroscopy, ConfocalPhosphatidylinositol PhosphatesPlatelet-Derived Growth FactorAndrostadienesFluorescent DyesGreen Fluorescent ProteinsHydrogen PeroxideInsulinLipidsLuminescent Proteinsphosphatidylinositol 3,4,5-triphosphatephosphatidylinositol 3,4-diphosphatePhosphatidylinositol Phosphatesphosphatidylinositol receptorsPlatelet-Derived Growth FactorProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsWortmannin

Identifiers

PMID10585883
PMCPMC1220718
OpenAlexW2150597600

What OpenQuestion holds

Textmetadata
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.