Evidence for a junctional feet-ryanodine receptor complex from sarcoplasmic reticulum.
Heavy sarcoplasmic reticulum vesicles, labelled with the Ca2+ release channel probe [3H]ryanodine, were solubilized in detergent, then centrifuged through sucrose gradients. A single peak of ryanodine binding activity was observed with an apparent sedimentation coefficient of 30S. Electron microscopy of the peak fraction showed disk structures of 25-28 nm diameter and 10 nm thickness. Proteins specifically enriched in the peak fraction were the Mr 160,000 and 260,000 and junctional feet proteins (Mr 320,000 and 300,000). This suggests that the feet proteins and ryanodine receptor may be specifically associated into a large oligomeric complex comprising subunits of Mr 160,000-320,000.
D000470:Alkaloids / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000502:physiology; D007425:Intracellular Membranes / Q000378:metabolism / Q000648:ultrastructure; D007473:Ion Channels / Q000378:metabolism*; D008854:Microscopy, Electron; D011817:Rabbits; D011950:Receptors, Cholinergic / Q000378:metabolism*; D012433:Ryanodine / Q000378:metabolism*; D019837:Ryanodine Receptor Calcium Release Channel; D012519:Sarcoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure
D000470:Alkaloids; D007473:Ion Channels; D011950:Receptors, Cholinergic; D019837:Ryanodine Receptor Calcium Release Channel; D012433:Ryanodine; D002118:Calcium