Evidence map›Paper›PMID 18420701›Full record

ArticleThe Journal of physiology2008

Monitoring changes in membrane phosphatidylinositol 4,5-bisphosphate in living cells using a domain from the transcription factor tubby.

Kathryn V Quinn, Philippe Behe, Andrew Tinker

Abstract read
In one paragraph

Article in The Journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
–field-weighted citation impact
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

69 citing papers in PubMed.

  1. PIP4K attenuates PIP5K lipid kinase activity by disrupting membrane-mediated dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  19. An update on genetically encoded lipid biosensors.Molecular biology of the cell · 2022
    Article
  20. Article

9 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.

Kathryn V QuinnBHF Laboratories and Department of Medicine, University College London, 5 University Street, London WC1E 6JJ, UK. a.tinker@ucl.ac.uk
Philippe Behe
Andrew Tinker

Funding

British Heart FoundationWellcome Trust
6 · The paper itself

Abstract

Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)) is a key component in signal transduction, being a precursor to other signalling molecules and itself associated with roles in signal transduction and cell biology. Tubby is a membrane bound transcription factor whose dysfunction results in obesity in mice. It contains a domain that selectively binds PtdIns(4,5)P(2). We have investigated the use of a fluorescently tagged version of this domain to monitor changes in PtdIns(4,5)P(2) concentration in living cells and compared it to the pleckstrin homology domain of PLCdelta1. Our results show that selected mutants of this domain report receptor-mediated changes in cellular PtdIns(4,5)P(2). In contrast to the pleckstrin homology domain of PLCdelta1 it does not have a significant affinity for inositol 1,4,5-trisphosphate (IP(3)). Using a selected mutant, we examine the regulation of ATP-sensitive K(+) channels via a G(q/11)-coupled receptor. These experiments reveal a correlation between reporter translocation and the onset of current inhibition whilst the recovery of current after agonist removal is delayed when compared to the reporter. Furthermore our studies reveal the importance of Ca(2+) in determining the overall activity of phospholipase C in living cells. This probe may be valuable in examining changes in PtdIns(4,5)P(2) distinct from those of IP(3) in intact cells in a variety of physiological settings.

Indexed as

Molecular Probe TechniquesAdaptor Proteins, Signal TransducingBiological AssayCell LineCell MembraneHumansKidneyMicroscopy, FluorescenceMonitoring, PhysiologicPhosphatidylinositol 4,5-DiphosphateProteinsProtein Structure, TertiaryTranscription FactorsAdaptor Proteins, Signal TransducingPhosphatidylinositol 4,5-DiphosphateProteinsTranscription FactorsTub protein, mouse

Identifiers

PMID18420701
PMCPMC2517197

What OpenQuestion holds

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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.