Evidence map›Paper›PMID 19833731›Full record

ArticleThe Journal of biological chemistry2009

Functional characterization of intracellular Dictyostelium discoideum P2X receptors.

Melanie J Ludlow, Latha Durai, Steven J Ennion

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Intracellular expression of purinoceptors.Purinergic signalling · 2015
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. The trafficking and targeting of P2X receptors.Frontiers in cellular neuroscience · 2013
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. A mechanism of intracellular P2X receptor activation.The Journal of biological chemistry · 2012
    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 1 institution in 1 country.

Melanie J LudlowDepartment of Cell Physiology and Pharmacology, University of Leicester, Leicester LE1 9HN, United Kingdom.
Latha Durai
Steven J Ennion
University of Leicester · GB

Funding

Biotechnology and Biological Sciences Research Council C19146Wellcome TrustWellcome Trust WT081601MA
6 · The paper itself

Abstract

Indicative of cell surface P2X ion channel activation, extracellular ATP evokes a rapid and transient calcium influx in the model eukaryote Dictyostelium discoideum. Five P2X-like proteins (dP2XA-E) are present in this organism. However, their roles in purinergic signaling are unclear, because dP2XA proved to have an intracellular localization on the contractile vacuole where it is thought to be required for osmoregulation. To determine functional properties of the remaining four dP2X-like proteins and to assess their cellular roles, we recorded membrane currents from expressed cloned receptors and generated a quintuple knock-out Dictyostelium strain devoid of dP2X receptors. ATP evoked inward currents at dP2XB and dP2XE receptors but not at dP2XC or dP2XD. beta,gamma-Imido-ATP was more potent than ATP at dP2XB but a weak partial agonist at dP2XE. Currents in dP2XB and dP2XE were strongly inhibited by Na(+) but insensitive to copper and the P2 receptor antagonists pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid and suramin. Unusual for P2X channels, dP2XA and dP2XB were also Cl(-)-permeable. The extracellular purinergic response to ATP persisted in p2xA/B/C/D/E quintuple knock-out Dictyostelium demonstrating that dP2X channels are not responsible. dP2XB, -C, -D, and -E were found to be intracellularly localized to the contractile vacuole with the ligand binding domain facing the lumen. However, quintuple p2xA/B/C/D/E null cells were still capable of regulating cell volume in water demonstrating that, contrary to previous findings, dP2X receptors are not required for osmoregulation. Responses to the calmodulin antagonist calmidazolium, however, were reduced in p2xA/B/C/D/E null cells suggesting that dP2X receptors play a role in intracellular calcium signaling.

Indexed as

AnimalsCalciumCalcium SignalingCopperDictyosteliumOocytesPatch-Clamp TechniquesProtein IsoformsPurinesPyridoxal PhosphateReceptors, Purinergic P2Receptors, Purinergic P2XRecombinant Fusion ProteinsSuraminWater-Electrolyte BalanceXenopus laevisCalciumCopperProtein IsoformsPurinesPyridoxal Phosphatepyridoxal phosphate-6-azophenyl-2',4'-disulfonic acidReceptors, Purinergic P2Receptors, Purinergic P2XRecombinant Fusion ProteinsSuramin

Identifiers

PMID19833731
PMCPMC2787382
OpenAlexW2018401991

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.