Evidence map›Paper›PMID 20378545›Full record

ArticleThe Journal of biological chemistry2010

C-terminal calmodulin-binding motif differentially controls human and rat P2X7 receptor current facilitation.

Sébastien Roger, Ludovic Gillet, Alberto Baroja-Mazo, Annmarie Surprenant, Pablo Pelegrin

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 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Silencing P2YCell communication and signaling : CCS · 2025
    Article
  6. Article
  7. Article
  8. Untangling Macropore Formation and Current Facilitation in P2X7.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Article
  11. Review
  12. Ruscogenin Ameliorated Sjögren's Syndrome by Inhibiting NLRP3 Inflammasome Activation.Evidence-based complementary and alternative medicine : eCAM · 2022
    Article
  13. Article
  14. Using Symmetrical Organic Cation Solutions to Study P2X7 Ion Permeation.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  15. P2X4 Receptors Mediate CaInternational journal of molecular sciences · 2021
    Article
  16. Review
  17. P2X7 receptor: a critical regulator and potential target for breast cancer.Journal of molecular medicine (Berlin, Germany) · 2021
    Review
  18. Review
  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

5 authors at 4 institutions in 3 countries.

Sébastien RogerInserm U921, Université François Rabelais de Tours, 10 Boulevard Tonnellé, 37032 Tours, France. sebastien.roger@univ-tours.fr
Ludovic Gillet
Alberto Baroja-Mazo
Annmarie Surprenant
Pablo Pelegrin
Hospital Universitario Virgen de la Arrixaca · ESInserm · FRUniversité de Tours · FRUniversity of Manchester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P2X(7) receptors (P2X(7)R) are ATP-gated calcium-permeable cationic channels structurally unique among the P2X family by their much longer intracellular C-terminal tail. P2X(7)Rs show several unusual biophysical properties, in particular marked facilitation of currents and leftward shift in agonist affinity in response to repeated or prolonged agonist applications. We previously found the facilitation at rat P2X(7)R resulted from a Ca(2+)-calmodulin-dependent process and a distinct calcium-independent process. However, P2X(7)Rs show striking species differences; thus, this study compared the properties of ATP-evoked facilitation of currents in HEK293 cells transiently expressing the human or rat P2X(7)R as well as rat/human, human/rat chimeric, and mutated P2X(7)Rs. Facilitation at the human P2X(7)R was 5-fold slower than at the rat P2X(7)R. Facilitation did not resulting from an increase of receptor addressing the plasma membrane. We found the human P2X(7)R shows only calcium-independent facilitation with no evidence for calmodulin-dependent processes, nor does it contain the novel 1-5-16 calmodulin binding domain present in the C terminus of rat P2X(7)R. Replacement of three critical residues of this binding domain from the rat into the human P2X(7)R (T541I, C552S, and G559V) reconstituted the Ca(2+)-calmodulin-dependent facilitation, leaving the calcium-independent facilitation unaltered. The leftward shift in the ATP concentration-response curve with repeated agonist applications appears to be a property of the calcium-independent facilitation process because it was not altered in any of the chimeric or mutated P2X(7)Rs. The absence of Ca(2+)-dependent facilitation at the human P2X(7)R may represent a protective adaptation of the innate immune response in which P2X(7)R plays significant roles.

Indexed as

Amino Acid MotifsAniline CompoundsAnimalsCalciumCalmodulinCell MembraneCytosolElectrophysiologyHumansPoint MutationProtein BindingProtein Structure, TertiaryRatsReceptors, Purinergic P2Receptors, Purinergic P2X7XanthenesAniline CompoundsCalciumCalmodulinFluo 4P2RX7 protein, humanP2rx7 protein, ratReceptors, Purinergic P2Receptors, Purinergic P2X7Xanthenes

Identifiers

PMID20378545
PMCPMC2878516
OpenAlexW2052353444

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.