Evidence map›Paper›PMID 19304656›Full record

ArticleThe Journal of biological chemistry2009

Analysis of assembly and trafficking of native P2X4 and P2X7 receptor complexes in rodent immune cells.

Miyyada Boumechache, Marianela Masin, J Michael Edwardson, Dariusz C Górecki, Ruth Murrell-Lagnado

Abstract 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 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

  1. Glial cells in neuropathic pain.Physiological reviews · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. The P2X7 Hypothesis of Central Post-Stroke Pain.International journal of molecular sciences · 2024
    Article
  9. Article
  10. Review
  11. Animal Models for the Investigation of P2X7 Receptors.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. P2X7 receptor: a critical regulator and potential target for breast cancer.Journal of molecular medicine (Berlin, Germany) · 2021
    Review
  20. P2XFrontiers in cellular neuroscience · 2021
    Review

15 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

5 authors.

Miyyada BoumechacheDepartment of Pharmacology, University of Cambridge, Cambridge CB2 1PD.
Marianela MasinDepartment of Pharmacology, University of Cambridge, Cambridge CB2 1PD.
J Michael EdwardsonDepartment of Pharmacology, University of Cambridge, Cambridge CB2 1PD.
Dariusz C GóreckiSchool of Pharmacy and Biomedical Sciences, University of Portsmouth, Portsmouth PO1 2DT, United Kingdom.
Ruth Murrell-LagnadoDepartment of Pharmacology, University of Cambridge, Cambridge CB2 1PD. Electronic address: rdm1003@cam.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/F001320/1
6 · The paper itself

Abstract

P2X4 and P2X7 are the predominant P2X receptor subtypes expressed in immune cells. Having previously shown a structural and functional interaction between the two recombinant receptors, our aims here were to identify the preferred assembly pathway of the endogenous receptors in macrophage-like cells and to investigate the trafficking of these receptors between the plasma membrane and intracellular sites. We exploited the difference in size between the two subunits, and we used a combination of cross-linkers and blue native-PAGE analysis to investigate the subunit composition of complexes present in primary cultures of rat microglia and macrophages from wild type and P2X7(-/-) mice. Our results indicate that the preferred assembly pathway for both receptors is the formation of homotrimers. Homotrimers of P2X7 were able to co-immunoprecipitate with P2X4, suggesting that an interaction occurs between rather than within receptor complexes. In both macrophages and microglia, P2X7 receptors were predominantly at the cell surface, whereas P2X4 receptors were predominantly intracellular. There were clear cell type-dependent differences in the extent to which P2X4 receptors trafficked to and from the surface; trafficking was much more dynamic in microglia than in the macrophages, and further activation of cultured microglia with relatively short (3-h) incubations with lipopolysaccharide caused an approximately 4-fold increase in the fraction of receptors at the surface with only a 1.2-fold increase in total expression. The redistribution of intracellular receptors is thus an efficient means of enhancing the functional expression of P2X4 at the plasma membrane of microglia.

Indexed as

AnimalsCell MembraneCells, CulturedCytoplasmGene Expression RegulationLipopolysaccharidesMacrophagesMiceMicrogliaProtein TransportRatsReceptors, Purinergic P2Receptors, Purinergic P2X4Receptors, Purinergic P2X7Time FactorsLipopolysaccharidesP2rx4 protein, mouseP2rx4 protein, ratP2rx7 protein, mouseP2rx7 protein, ratReceptors, Purinergic P2Receptors, Purinergic P2X4Receptors, Purinergic P2X7

Identifiers

PMID19304656
PMCPMC2679444

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.