ArticleEuropean biophysics journal : EBJ2009
Inter-subunit disulfide cross-linking in homomeric and heteromeric P2X receptors.
Article in European biophysics journal : EBJ, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 32 citations in OpenAlex.
- Molecular determinants for agonist recognition and discrimination in P2X2 receptors.The Journal of general physiology · 2019Article
- Conformational changes during human P2X7 receptor activation examined by structural modelling and cysteine-based cross-linking studies.Purinergic signalling · 2017Article
- P2X receptors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Review
- Inter-subunit disulfide locking of the human P2X3 receptor elucidates ectodomain movements associated with channel gating.Purinergic signalling · 2016Article
- Article
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Conformational flexibility of the agonist binding jaw of the human P2X3 receptor is a prerequisite for channel opening.British journal of pharmacology · 2014Article
- Ectodomain movements of an ATP-gated ion channel (P2X2 receptor) probed by disulfide locking.The Journal of biological chemistry · 2014Article
- Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013Review
- Functional identification of close proximity amino acid side chains within the transmembrane-spanning helixes of the P2X2 receptor.PloS one · 2013Article
- Insights into the Molecular Mechanisms Underlying Mammalian P2X7 Receptor Functions and Contributions in Diseases, Revealed by Structural Modeling and Single Nucleotide Polymorphisms.Frontiers in pharmacology · 2013Article
- Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Gating mechanism of a P2X4 receptor developed from normal mode analysis and molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Pharmacochemistry of the platelet purinergic receptors.Purinergic signalling · 2011Article
- Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gating.The Journal of biological chemistry · 2011Article
- Structural interpretation of P2X receptor mutagenesis studies on drug action.British journal of pharmacology · 2010Review
- A putative extracellular salt bridge at the subunit interface contributes to the ion channel function of the ATP-gated P2X2 receptor.The Journal of biological chemistry · 2010Article
- New structure enlivens interest in P2X receptors.Trends in pharmacological sciences · 2010Review
- Differential regulation of P2X7 receptor activation by extracellular nicotinamide adenine dinucleotide and ecto-ADP-ribosyltransferases in murine macrophages and T cells.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Contribution of the region Glu181 to Val200 of the extracellular loop of the human P2X1 receptor to agonist binding and gating revealed using cysteine scanning mutagenesis.Journal of neurochemistry · 2009Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P2X receptors are ATP-gated cation channels and assembled as homotrimers or heterotrimers from seven cloned subunits. Each subunit contains two transmembrane domains connected by a large extracellular loop. We have previously shown that replacement of two conserved residues, K68 and F291, by cysteine residues leads to disulfide cross-linking between neighbouring P2X(1) subunits. Since mutation of these residues results in a reduced ATP potency and cysteine cross-linking is prevented in the presence of ATP, we suggested an inter-subunit ATP binding site. To investigate whether the proximity of these residues is preserved in other P2X subtypes, we tested for spontaneous cystine formation between the corresponding P2X(2 )(K69C, F289C), P2X(3 )(K63C, F280C), and P2X(4 )(K67C, F294C) mutants upon pairwise expression in Xenopus laevis oocytes. Non-reducing SDS-PAGE analysis of the purified receptors revealed a specific dimer formation between P2X(2)K69C and P2X(2)F289C mutants. Likewise, co-expression of P2X(1)K68C and P2X(2)F289C, but not P2X(1)F291C and P2X(2)K69C, mutants resulted in dimer formation between the respective subunits. Cross-linked P2X(1/2) heteromers showed strongly reduced or absent function that was selectively recovered upon treatment with DTT. Cross-linking was less efficient between P2X(3) or P2X(4) mutants but could be enhanced by the short cysteine-reactive cross-linker MTS-2-MTS. These results show that the spatial proximity and/or orientation of residues analogous to positions K68 and F291 in P2X(1) are preserved in P2X(2) receptors and at one of two possible interfaces in heteromeric P2X(1/2) receptors but appears to be redundant for P2X(3) and P2X(4) receptor function.
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