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Phosphorylation of HMG‐CoA reductase induced by mevalonate accelerates its rate of degradation in isolated rat hepatocytes
Author(s) -
Marrero Pedro F.,
Haro Diego,
Hegardt Fausto G.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80323-4
Subject(s) - reductase , hmg coa reductase , phosphorylation , hydroxymethylglutaryl coa reductase , chemistry , degradation (telecommunications) , biochemistry , monomer , enzyme , incubation , telecommunications , organic chemistry , computer science , polymer
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.