Association of a receptor and G-protein-regulated phospholipase C with the cytoskeleton.

摘要: Abstract Approximately 98% of turkey erythrocyte phospholipase C (PLC) is cytosolic and released by hypotonic lysis the cells extensive washing resultant ghosts. Well washed ghosts retain a fraction tightly associated PLC, which activated P2y-purinergic receptor G-protein present in ghost membranes. The particulate PLC sufficient to couple all available purinergic receptor-regulated G-protein. In contrast ghosts, plasma membrane preparations contain no detectable PLC. To investigate subcellular location ghost-associated cytoskeletons were prepared Triton X-100 extraction was quantitatively recovered cytoskeleton preparations. Cytoskeleton-associated solubilized sodium cholate extraction, partially purified, shown reconstitute with PLC-free an agonist guanine nucleotide-dependent fashion, indicating that cytoskeleton-associated G-protein-regulated. Dissociation actin-binding protein DNase 1 resulted dose-dependent inhibition nucleotide-stimulated responses caused release from or These data demonstrate specific association G-protein-regulated component detergent-insoluble indicate integrity actin important for localization effective coupling relevant