ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004
Identification of ectodomain regions contributing to gating, deactivation, and resensitization of purinergic P2X receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- 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
- Progress on functions of intracellular domainZhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024Review
- How Structural Biology Has Directly Impacted Our Understanding of P2X Receptor Function and Gating.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Purinergic signaling pathways in endocrine system.Autonomic neuroscience : basic & clinical · 2015Review
- Role of domain calcium in purinergic P2X2 receptor channel desensitization.American journal of physiology. Cell physiology · 2015Article
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Article
- Desensitization properties of P2X3 receptors shaping pain signaling.Frontiers in cellular neuroscience · 2013Review
- Molecular and functional properties of P2X receptors--recent progress and persisting challenges.Purinergic signalling · 2012Review
- The expression and role of hyperpolarization-activated and cyclic nucleotide-gated channels in endocrine anterior pituitary cells.Molecular endocrinology (Baltimore, Md.) · 2012Article
- The intracellular amino terminus plays a dominant role in desensitization of ATP-gated P2X receptor ion channels.The Journal of biological chemistry · 2011Article
- Activation and regulation of purinergic P2X receptor channels.Pharmacological reviews · 2011Review
- The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus.Molecular pharmacology · 2011Article
- Characterization of purinergic P2X4 receptor channels expressed in anterior pituitary cells.American journal of physiology. Endocrinology and metabolism · 2010Article
- Dinucleoside polyphosphates: strong endogenous agonists of the purinergic system.British journal of pharmacology · 2009Review
- Roles of ectodomain and transmembrane regions in ethanol and agonist action in purinergic P2X2 and P2X3 receptors.Neuropharmacology · 2008Article
- Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interaction with ivermectin.Pflugers Archiv : European journal of physiology · 2008Article
- Identification of an intersubunit cross-link between substituted cysteine residues located in the putative ATP binding site of the P2X1 receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
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Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
Abstract
The P2X receptors (P2XRs) are a family of ligand-gated channels activated by extracellular ATP through a sequence of conformational transitions between closed, open, and desensitized states. In this study, we examined the dependence of the activity of P2XRs on ectodomain structure and agonist potency. Experiments were done in human embryonic kidney 293 cells expressing rat P2X2aR, P2X2bR, and P2X3R, and chimeras having the V60-R180 or V60-F301 ectodomain sequences of P2X3R instead of the I66-H192 or I66-Y310 sequences of P2X2aR and P2X2bR. Chimeric P2X2a/V60-F301X3R and P2X2b/V60-F301X3R inherited the P2X3R ligand-selective profile, whereas the potency of agonists for P2X2a/V60-R180X3R was in between those observed at parental receptors. Furthermore, P2X2a/V60-F301X3R and P2X2a/V60-R180X3R desensitized in a P2X2aR-specific manner, and P2X2b/V60-F301X3R desensitized with rates comparable with those of P2X2bR. In striking contrast to parental receptors, the rates of decay in P2X2a/V60-F301X3R and P2X2b/V60-F301X3R currents after agonist withdrawal were 15- to 200-fold slower. For these chimeras, the decays in currents were not dependent on duration of stimuli and reflected both continuous desensitization and deactivation of receptors. Also, participation of deactivation in closure of channels inversely correlated with potency of agonists to activate receptors. The delay in deactivation was practically abolished in P2X2a/V60-R180X3R-expressing cells. However, the recovery from desensitization of P2X2a/V60-F301X3R and P2X2a/V60-R180X3R was similar and substantially delayed compared with that of parental receptors. These results indicate that both ectodomain halves participate in gating, but that the C and N halves influence the stability of open and desensitized conformation states, respectively, which in turn reflects on rates of receptor deactivation and resensitization.
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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.