ArticleBritish journal of pharmacology2011
P2X4 receptors interact with both P2X2 and P2X7 receptors in the form of homotrimers.
Article in British journal of pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 66 citations in OpenAlex.
- Single-cell architecture of purinergic signaling in human cord blood hematopoietic stem and progenitor cells.Leukemia · 2026Article
- Genetic Deletion of Adenosine AGlia · 2026Article
- P2X7 Signaling in Neuroinflammation: Glial Crosstalk, Redox Integration, and Therapeutic Targeting.Journal of molecular neuroscience : MN · 2026Review
- P2X4 receptors on myeloid cells mediate tissue injury in a model of trauma and hemorrhagic shock in male mice.Purinergic signalling · 2026Article
- P2X4 receptors on myeloid cells mediate tissue injury in a murine model of trauma and hemorrhagic shock.Research square · 2025Article
- Different localization of P2X4 and P2X7 receptors in native mouse lung - lack of evidence for a direct P2X4-P2X7 receptor interaction.Frontiers in immunology · 2024Article
- Migraine signaling pathways: purine metabolites that regulate migraine and predispose migraineurs to headache.Molecular and cellular biochemistry · 2023Review
- Altered purinergic receptor expression in the frontal cortex in schizophrenia.Schizophrenia (Heidelberg, Germany) · 2022Article
- ATP-gated P2X7 receptor as a potential target for prostate cancer.Human cell · 2022Review
- Blocking P2X purinoceptor 4 signalling alleviates cigarette smoke induced pulmonary inflammation.Respiratory research · 2022Article
- Structure-activity features of purines and their receptors: implications in cell physiopathology.Molecular biomedicine · 2022Review
- P2X7 receptor: a critical regulator and potential target for breast cancer.Journal of molecular medicine (Berlin, Germany) · 2021Review
- Structural and Functional Features of the P2X4 Receptor: An Immunological Perspective.Frontiers in immunology · 2021Review
- Role of microglia and P2X4 receptors in chronic pain.Pain reports · 2021Review
- Crosstalk Between ATP-PFrontiers in cellular neuroscience · 2021Article
- Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor.International journal of molecular sciences · 2020Review
- Extracellular ATP as an Inter-Kingdom Signaling Molecule: Release Mechanisms by Bacteria and Its Implication on the Host.International journal of molecular sciences · 2020Review
- P2 Receptors as Therapeutic Targets in the Salivary Gland: From Physiology to Dysfunction.Frontiers in pharmacology · 2020Review
- Extracellular Nucleotides and P2 Receptors in Renal Function.Physiological reviews · 2020Review
- Function of P2X4 Receptors Is Directly Modulated by a 1:1 Stoichiometric Interaction With 5-HTFrontiers in cellular neuroscience · 2020Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
background and purposeThe P2X receptor family consists of seven subunit types - P2X1-P2X7. All but P2X6 are able to assemble as homotrimers. In addition, various subunit permutations have been reported to form heterotrimers. Evidence for heterotrimer formation includes co-localization, co-immunoprecipitation and the generation of receptors with novel functional properties; however, direct structural evidence for heteromer formation, such as chemical cross-linking and single-molecule imaging, is available in only a few cases. Here we examined the nature of the interaction between two pairs of subunits - P2X2 and P2X4, and P2X4 and P2X7. EXPERIMENTAL APPROACH: We used several experimental approaches, including in situ proximity ligation, co-immunoprecipitation, co-isolation on affinity beads, chemical cross-linking and atomic force microscopy (AFM) imaging. KEY
resultsBoth pairs of subunits co-localize upon co-transfection, interact intimately within cells, and can be co-immunoprecipitated and co-isolated from cell extracts. Despite this, chemical cross-linking failed to show evidence for heteromer formation. AFM imaging of isolated receptors showed that all three subunits had the propensity to form receptor dimers. This self-association is likely to account for the observed close interaction between the subunit pairs, in the absence of true heteromer formation. CONCLUSIONS AND IMPLICATIONS: We conclude that both pairs of receptors interact in the form of distinct homomers. We urge caution in the interpretation of biochemical evidence indicating heteromer formation in other cases.
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Registered trials
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.