ArticleThe Journal of biological chemistry2015
Contribution of the Juxtatransmembrane Intracellular Regions to the Time Course and Permeation of ATP-gated P2X7 Receptor Ion Channels.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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.
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.
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Who cites it
26 citing papers in PubMed, 33 citations in OpenAlex.
- P2X7 Receptor in Rare Diseases: Shared Molecular Mechanisms and Therapeutic Implications.Journal of inflammation research · 2026Review
- Genetic Variations in the P2X7 Receptor: Opportunities and Challenges for Drug Development.International journal of molecular sciences · 2025Review
- Human P2X4 receptor gating is modulated by a stable cytoplasmic cap and a unique allosteric pocket.Science advances · 2025Article
- Subtype-Specific Ligand Binding and Activation Gating in Homomeric and Heteromeric P2X Receptors.Biomolecules · 2024Article
- The Purinergic P2X7 Receptor as a Target for Adjunctive Treatment for Drug-Refractory Epilepsy.International journal of molecular sciences · 2024Review
- Untangling Macropore Formation and Current Facilitation in P2X7.International journal of molecular sciences · 2023Review
- Article
- ATP-gated P2X7 receptor as a potential target for prostate cancer.Human cell · 2022Review
- The long β2,3-sheets encoded by redundant sequences play an integral role in the channel function of P2X7 receptors.The Journal of biological chemistry · 2022Article
- How Structural Biology Has Directly Impacted Our Understanding of P2X Receptor Function and Gating.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Molecular Pharmacology of P2X Receptors: Exploring Druggable Domains Revealed by Structural Biology.Frontiers in pharmacology · 2022Review
- Structural basis for the functional properties of the P2X7 receptor for extracellular ATP.Purinergic signalling · 2021Review
- Role of Conserved Residues and F322 in the Extracellular Vestibule of the Rat P2X7 Receptor in Its Expression, Function and Dye Uptake Ability.International journal of molecular sciences · 2020Article
- Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor.International journal of molecular sciences · 2020Review
- Full-Length P2XCell · 2019Article
- CaThe Journal of biological chemistry · 2019Article
- Alternative splicing of P2RX7 pre-messenger RNA in health and diseases: Myth or reality?Biomedical journal · 2019Review
- Organization of ATP-gated P2X1 receptor intracellular termini in apo and desensitized states.The Journal of general physiology · 2019Article
- P2X7 Interactions and Signaling - Making Head or Tail of It.Frontiers in molecular neuroscience · 2019Review
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
P2X7 receptors are ATP-gated ion channels that contribute to inflammation and cell death. They have the novel property of showing marked facilitation to repeated applications of agonist, and the intrinsic channel pore dilates to allow the passage of fluorescent dyes. A 60-s application of ATP to hP2X7 receptors expressed in Xenopus oocytes gave rise to a current that had a biphasic time course with initial and secondary slowly developing components. A second application of ATP evoked a response with a more rapid time to peak. This facilitation was reversed to initial levels following a 10-min agonist-free interval. A chimeric approach showed that replacement of the pre-TM1 amino-terminal region with the corresponding P2X2 receptor section (P2X7-2Nβ) gave responses that quickly reached a steady state and did not show facilitation. Subsequent point mutations of variant residues identified Asn-16 and Ser-23 as important contributors to the time course/facilitation. The P2X7 receptor is unique in having an intracellular carboxyl-terminal cysteine-rich region (Ccys). Deletion of this region removed the secondary slowly developing current, and, when expressed in HEK293 cells, ethidium bromide uptake was only ∼5% that of WT levels, indicating reduced large pore formation. Dye uptake was also reduced for the P2X7-2Nβ chimera. Surprisingly, combination of the chimera and the Ccys deletion (P2X7-2NβdelCcys) restored the current rise time and ethidium uptake to WT levels. These findings suggest that there is a coevolved interaction between the juxtatransmembrane amino and carboxyl termini in the regulation of P2X7 receptor gating.
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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.