ArticlePLoS biology2009
Direct observation of ATP-induced conformational changes in single P2X(4) receptors.
Article in PLoS biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 108 citations in OpenAlex.
- P2X4 receptors as the dynamic regulators of auditory sensory cell activity: a potential new mechanism for protecting hearing?Purinergic signalling · 2026Article
- Single-Molecule Techniques for Probing the Conformation, Dynamics and Interactions of Intrinsically Disordered Proteins.Biophysics reviews · 2025Article
- Review
- P2XScientific reports · 2022Article
- In vivo single-particle tracking of the aquaporin AtPIP2;1 in stomata reveals cell type-specific dynamics.Plant physiology · 2021Article
- Nucleotides-Induced Changes in the Mechanical Properties of Living Endothelial Cells and Astrocytes, Analyzed by Atomic Force Microscopy.International journal of molecular sciences · 2021Article
- Atomic Force Microscopy Reveals that the Drosophila Telomere-Capping Protein Verrocchio Is a Single-Stranded DNA-Binding Protein.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Resolving the Ionotropic P2X4 Receptor Mystery Points Towards a New Therapeutic Target for Cardiovascular Diseases.International journal of molecular sciences · 2020Review
- Advances in high-speed atomic force microscopy (HS-AFM) reveal dynamics of transmembrane channels and transporters.Current opinion in structural biology · 2019Review
- [Progress in the applications of high-speed atomic force microscopy in cell biology].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018Review
- Modulation of Pain and Itch by Spinal Glia.Neuroscience bulletin · 2018Review
- P2X4: A fast and sensitive purinergic receptor.Biomedical journal · 2017Review
- 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
- Intersubunit physical couplings fostered by the left flipper domain facilitate channel opening of P2X4 receptors.The Journal of biological chemistry · 2017Article
- P2X4 Receptor Function in the Nervous System and Current Breakthroughs in Pharmacology.Frontiers in pharmacology · 2017Review
- Insights into the channel gating of P2X receptors from structures, dynamics and small molecules.Acta pharmacologica Sinica · 2016Review
- Channel function reconstitution and re-animation: a single-channel strategy in the postcrystal age.The Journal of physiology · 2015Review
- Stable isotope imaging of biological samples with high resolution secondary ion mass spectrometry and complementary techniques.Methods (San Diego, Calif.) · 2014Article
- Multiparametric high-resolution imaging of native proteins by force-distance curve-based AFM.Nature protocols · 2014Article
- Filming biomolecular processes by high-speed atomic force microscopy.Chemical reviews · 2014Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ATP-gated P2X(4) receptor is a cation channel, which is important in various pathophysiological events. The architecture of the P2X(4) receptor in the activated state and how to change its structure in response to ATP binding are not fully understood. Here, we analyze the architecture and ATP-induced structural changes in P2X(4) receptors using fast-scanning atomic force microscopy (AFM). AFM images of the membrane-dissociated and membrane-inserted forms of P2X(4) receptors and a functional analysis revealed that P2X(4) receptors have an upward orientation on mica but lean to one side. Time-lapse imaging of the ATP-induced structural changes in P2X(4) receptors revealed two different forms of activated structures under 0 Ca(2+) conditions, namely a trimer structure and a pore dilation-like tripartite structure. A dye uptake measurement demonstrated that ATP-activated P2X(4) receptors display pore dilation in the absence of Ca(2+). With Ca(2+), the P2X(4) receptors exhibited only a disengaged trimer and no dye uptake was observed. Thus our data provide a new insight into ATP-induced structural changes in P2X(4) receptors that correlate with pore dynamics.
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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.