ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2012
P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 72 citations in OpenAlex.
- 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
- Enlightening activation gating in P2X receptors.Purinergic signalling · 2022Review
- Dihydropyridines Potentiate ATP-Induced Currents Mediated by the Full-Length Human P2X5 Receptor.Molecules (Basel, Switzerland) · 2022Article
- Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor.International journal of molecular sciences · 2020Review
- Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors.The Journal of biological chemistry · 2019Article
- P2Y2 purinergic receptor modulates virus yield, calcium homeostasis, and cell motility in human cytomegalovirus-infected cells.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Re-evaluation of neuronal P2X7 expression using novel mouse models and a P2X7-specific nanobody.eLife · 2018Article
- New Insights Into Permeation of Large Cations Through ATP-Gated P2X Receptors.Frontiers in molecular neuroscience · 2018Article
- On the permeation of large organic cations through the pore of ATP-gated P2X receptors.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The purinergic receptor P2X5 regulates inflammasome activity and hyper-multinucleation of murine osteoclasts.Scientific reports · 2017Article
- Review
- Modulation of Central Synapses by Astrocyte-Released ATP and Postsynaptic P2X Receptors.Neural plasticity · 2017Review
- Comparative study of the P2X gene family in animals and plants.Purinergic signalling · 2016Article
- Modeling Interactions among Individual P2 Receptors to Explain Complex Response Patterns over a Wide Range of ATP Concentrations.Frontiers in physiology · 2016Article
- ATP-induced P2X Receptor-Dependent Large Pore Formation: How Much Do We Know?Frontiers in pharmacology · 2016Article
- Purinergic signaling pathways in endocrine system.Autonomic neuroscience : basic & clinical · 2015Review
- Allosteric regulation of the P2X4 receptor channel pore dilation.Pflugers Archiv : European journal of physiology · 2015Article
- Structural and molecular modeling features of P2X receptors.International journal of molecular sciences · 2014Review
- Principles and properties of ion flow in P2X receptors.Frontiers in cellular neuroscience · 2014Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Ligand-gated ion channels are prototypic oligomeric membrane proteins whose stoichiometry determines their functional properties and subcellular localization. Deciphering the quaternary structure of such protein complexes is an arduous task and usually requires the combination of multiple approaches. ATP-gated P2X receptors are formed by the association of three subunits, but the quaternary arrangement of the seven P2X subunits at the plasma membrane remains poorly characterized. By combining bioluminescence resonance energy transfer, bifunctional fluorescence complementation and protein biochemistry, we developed an experimental approach that allows precise determination of rat P2X receptor quaternary assembly. We found that P2X5 subunits associate with P2X1, P2X2, and P2X4 subunits. We demonstrate that P2X5 and P2X2 subunits interact to form as yet uncharacterized heteromeric receptors with alternate stoichiometries, both present at the plasma membrane. P2X2/5 receptors display functional properties such as pore dilatation, membrane blebbing, and phosphatidylserine exposure that were previously thought to be characteristic hallmarks of the P2X7 receptor. In mouse, P2X2 and P2X5 subunits colocalize and physically interact in specific neuronal populations suggesting that other P2X receptors might contribute to cellular responses typically attributed to P2X7 receptor.
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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.