Phosphorylation of HMG-CoA reductase induced by mevalonate accelerates its rate of degradation in isolated rat hepatocytes.
Incubation of rat hepatocytes with 10 mM mevalonate produces a decrease in HMG-CoA reductase activity and in the rate of synthesis of both monomeric and dimeric HMG-CoA reductase, and an increase in the rate of degradation of the monomeric form without significant change in that of the dimeric form. Since mevalonate promotes a short-term phosphorylation of the monomeric form without affecting the dimeric form, it is suggested that the mechanism of degradation of reductase is controlled by its phosphorylation state.
D000818:Animals; D006207:Half-Life; D006903:Hydroxymethylglutaryl CoA Reductases / Q000378:metabolism*; D007163:Immunosorbent Techniques; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D046911:Macromolecular Substances; D008798:Mevalonic Acid / Q000494:pharmacology*; D010766:Phosphorylation; D051381:Rats
D046911:Macromolecular Substances; D006903:Hydroxymethylglutaryl CoA Reductases; D008798:Mevalonic Acid