Evidence map›Paper›PMID 20826779›Full record

ArticleThe Journal of biological chemistry2010

Heterogeneity of phosphatidic acid levels and distribution at the plasma membrane in living cells as visualized by a Föster resonance energy transfer (FRET) biosensor.

Teruko Nishioka, Michael A Frohman, Michiyuki Matsuda, Etsuko Kiyokawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Phosphatidic acid signaling and function in nuclei.Progress in lipid research · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Guidelines for the Use of Protein Domains in Acidic Phospholipid Imaging.Methods in molecular biology (Clifton, N.J.) · 2016
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Cellular and physiological roles for phospholipase D1 in cancer.The Journal of biological chemistry · 2014
    Review
  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

4 authors at 2 institutions in 2 countries.

Teruko NishiokaLaboratory of Bioimaging and Cell Signaling, Graduate School of Biostudies, Kyoto University, Yoshida Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Michael A Frohman
Michiyuki Matsuda
Etsuko Kiyokawa
Kyoto University · JPStony Brook University · US

Funding

Lipid-signaling pathways regulating mitochondrial morphology, energetics, and movR01GM084251 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI FROHMAN, MICHAEL A. · 2009 to 2017
$2.6M
NIGMS NIH HHS GM0171520NIGMS NIH HHS GM084251NIGMS NIH HHS R01 GM084251
6 · The paper itself

Abstract

Phosphatidic acid (PA) is one of the major phospholipids in the plasma membrane. Although it has been reported that PA plays key roles in cell survival and morphology, it remains unknown when and where PA is produced in the living cell. Based on the principle of Förster resonance energy transfer (FRET), we generated PA biosensor, and named Pii (phosphatidic acid indicator). In these biosensors, the lipid-binding domain of DOCK2 is sandwiched with the cyan fluorescent protein and yellow fluorescent protein and is tagged with the plasma membrane-targeting sequence of K-Ras. The addition of synthetic PA, or the activation of phospholipase D or diacylglycerol kinase at the plasma membrane, changed the level of FRET in Pii-expressing cells, demonstrating the response of Pii to PA. The biosensor also detected divergent PA content among various cell lines as well as within one cell line. Interestingly, the growth factor-induced increment in PA content correlated negatively with the basal PA content before stimulation, suggesting the presence of an upper threshold in the PA concentration at the plasma membrane. The biosensor also revealed uneven PA distribution within the cell, i.e. the basal level and growth factor-induced accumulation of PA was higher at the cell-free edges than at the cell-cell contact region. An insufficient increase in PA may account for ineffective Ras activation at areas of cell-cell contact. In conclusion, the PA biosensor Pii is a versatile tool for examining heterogeneity in the content and distribution of PA in single cells as well as among different cells.

Indexed as

AnimalsBinding SitesBiosensing TechniquesCell LineCell MembraneChlorocebus aethiopsCOS CellsDiacylglycerol KinaseEpidermal Growth FactorFluorescence Resonance Energy TransferGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsHeLa CellsHumansIntercellular JunctionsLuminescent ProteinsDiacylglycerol KinaseDOCK2 protein, humanEpidermal Growth FactorGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsLuminescent ProteinsPhosphatidic AcidsPhospholipase D

Identifiers

PMID20826779
PMCPMC2975220
OpenAlexW2012100512

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.