The P2X7/P2X4 interaction shapes the purinergic response in murine macrophages
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The ATP-gated P2X4 and P2X7 receptors are cation channels, co-expressed in excitable and non-excitable cells and play important roles in pain, bone development, cytokine release and cell death. Although these receptors interact the interacting domains are unknown and the functional consequences of this interaction remain unclear. Here we show by co-immunoprecipitation that P2X4 interacts with the C-terminus of P2X7 and by fluorescence resonance energy transfer experiments that this receptor-receptor interaction is driven by ATP. Furthermore, disrupting the ATP-driven interaction by knocking-out P2X4R provoked an attenuation of P2X7-induced cell death, dye uptake and IL-1β release in macrophages. Thus, P2X7 interacts with P2X4 via its C-terminus and disrupting the P2X7/P2X4 interaction hinders physiological responses in immune cells. © 2015 Elsevier Inc.All rights reserved.
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Cell death; FRET; IL-1β; P2X4; P2X7; Patch clamp interleukin 1beta; purinergic P2X4 receptor; purinergic P2X7 receptor; fluorescent dye; purinergic P2X4 receptor; purinergic P2X7 receptor; animal experiment; Article; carboxy terminal sequence; cell death; controlled study; cytokine release; fluorescence resonance energy transfer; human; human cell; immunoprecipitation; macrophage; mouse; nonhuman; patch clamp technique; priority journal; protein protein interaction; animal; C57BL mouse; HEK293 cell line; knockout mouse; macrophage; metabolism; Animals; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; HEK293 Cells; Humans; Macrophages; Mice; Mice, Inbred C57BL; Mice, Knockout; Receptors, Purinergic P2X4; Receptors, Purinergic P2X7
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