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• W1480157153 abstract "The P2X receptor family consists of seven subunit types - P2X1-P2X7. All but P2X6 are able to assemble as homotrimers. In addition, various subunit permutations have been reported to form heterotrimers. Evidence for heterotrimer formation includes co-localization, co-immunoprecipitation and the generation of receptors with novel functional properties; however, direct structural evidence for heteromer formation, such as chemical cross-linking and single-molecule imaging, is available in only a few cases. Here we examined the nature of the interaction between two pairs of subunits - P2X2 and P2X4, and P2X4 and P2X7.We used several experimental approaches, including in situ proximity ligation, co-immunoprecipitation, co-isolation on affinity beads, chemical cross-linking and atomic force microscopy (AFM) imaging.Both pairs of subunits co-localize upon co-transfection, interact intimately within cells, and can be co-immunoprecipitated and co-isolated from cell extracts. Despite this, chemical cross-linking failed to show evidence for heteromer formation. AFM imaging of isolated receptors showed that all three subunits had the propensity to form receptor dimers. This self-association is likely to account for the observed close interaction between the subunit pairs, in the absence of true heteromer formation.We conclude that both pairs of receptors interact in the form of distinct homomers. We urge caution in the interpretation of biochemical evidence indicating heteromer formation in other cases." @default.
• W1480157153 created "2016-06-24" @default.
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• W1480157153 date "2011-06-08" @default.
• W1480157153 modified "2023-09-26" @default.
• W1480157153 title "P2X4 receptors interact with both P2X2 and P2X7 receptors in the form of homotrimers" @default.
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• W1480157153 doi "https://doi.org/10.1111/j.1476-5381.2011.01303.x" @default.
• W1480157153 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3130952" @default.
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