Publications by authors named "Lucy E Robinson"
P2X7 receptors are nonselective cation channels gated by high extracellular ATP, but with sustained activation, receptor sensitization occurs, whereby the intrinsic pore dilates, making the cell permeable to large organic cations, which eventually leads to cell death. P2X7 receptors associate with cholesterol-rich lipid rafts, but it is unclear how this affects the properties of the receptor channel. Here we show that pore-forming properties of human and rodent P2X7 receptors are sensitive to perturbations of cholesterol levels.
View Article and Find Full Text PDFThe functional expression of P2X receptors at the plasma membrane is dependent on their trafficking along secretory and endocytic pathways. There are seven P2X receptor subunits, and these differ in their subcellular distributions because they have very different trafficking properties. Some are retained within the endoplasmic reticulum (ER), while others are predominantly at the cell surface or within endosomes and lysosomes.
View Article and Find Full Text PDFArticle Synopsis
- P2X7 receptors are ATP-gated cation channels that work with other proteins to trigger various cell-specific responses, but their role in cell death and sensitivity to NAD is not well understood.
- The P2X7k variant of the receptor, found in T lymphocytes, enhances sensitivity to NAD due to structural differences, improving its stability and function compared to the more common P2X7a variant.
- The interaction between P2X7 receptors and pannexin-1 is complex, with P2X7k showing independent activity in ethidium uptake, while signaling occurs downstream of caspase activation rather than direct interaction between the receptors.