ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004
Gain and loss of channel function by alanine substitutions in the transmembrane segments of the rat ATP-gated P2X2 receptor.
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 29 papers.
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Who cites it
29 citing papers in PubMed.
- Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.Science advances · 2026Article
- Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.bioRxiv : the preprint server for biology · 2025Article
- Differential Effects of Hearing Loss Mutations in Homomeric P2X2 and Heteromeric P2X2/3 Receptors.Cells · 2025Article
- Whole-exome sequencing reveals a comprehensive germline mutation landscape and identifies twelve novel predisposition genes in Chinese prostate cancer patients.PLoS genetics · 2022Article
- Article
- Photo-switchable tweezers illuminate pore-opening motions of an ATP-gated P2X ion channel.eLife · 2016Article
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Regulation of ATP-gated P2X channels: from redox signaling to interactions with other proteins.Antioxidants & redox signaling · 2014Review
- Article
- Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating.Frontiers in cellular neuroscience · 2014Article
- Optical control of an ion channel gate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Functional identification of close proximity amino acid side chains within the transmembrane-spanning helixes of the P2X2 receptor.PloS one · 2013Article
- Multiple roles of the extracellular vestibule amino acid residues in the function of the rat P2X4 receptor.PloS one · 2013Article
- Prenatal expression of purinergic receptor P2X3 in human dorsal root ganglion.Purinergic signalling · 2012Article
- Activation and regulation of purinergic P2X receptor channels.Pharmacological reviews · 2011Review
- Allosteric modulation of ATP-gated P2X receptor channels.Reviews in the neurosciences · 2011Review
- Structural insights into the function of P2X4: an ATP-gated cation channel of neuroendocrine cells.Cellular and molecular neurobiology · 2010Review
- Pore-opening mechanism in trimeric P2X receptor channels.Nature communications · 2010Article
- Functional and structural identification of amino acid residues of the P2X2 receptor channel critical for the voltage- and [ATP]-dependent gating.The Journal of physiology · 2009Article
- Polar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectification.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
ATP opens ionotropic P2X channels through a process that is poorly understood. We made an array of mutant rat P2X2 channels containing unique alanine substitutions in the transmembrane segments with the goal of identifying possible secondary structure and mapping gating domains in the pore. Alteration of channel function was measured as a change in ATP potency, 2'-3'-O-(4-benzoylbenzoyl)ATP (BzATP) efficacy, and deactivation kinetics. Four mutants (V45A, Y47A, V51A, and D349A) failed to respond to ATP. Seven (H33A, Q37A, I40A, L41A, Y43A, F44A, and I50A) of 22 mutations in the first transmembrane segment (TM1) produced channels with altered potencies, and two mutants (Y43A and F44A) were active in the absence of agonist. The pattern of hits was consistent with a helical secondary structure. In contrast, nine (I328A, P329A, N333A, L338A, T339A, S340A, G342A, G344A, and S345A) of 24 mutations in the second transmembrane segment (TM2) resulted in a change in potency, but no regular pattern of impact was apparent. Many of the same mutations that altered ATP potency also changed the relative efficacy of the partial agonist BzATP. Together, these data suggest that both TM1 and TM2 participate in the conformational changes that occur during receptor activation and help to define domains involved in conformational switching within or near the pore.
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