Direct demonstration that increased phosphorylation of 3-hydroxy-3-methylglutaryl-CoA reductase does not increase its rate of degradation in isolated rat hepatocytes
- 15 June 1992
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 284 (3) , 901-904
- https://doi.org/10.1042/bj2840901
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Calmodulin‐dependent multiprotein kinase and protein kinase C phosphorylate the same site on HMG‐CoA reductase as the AMP‐activated protein kinaseFEBS Letters, 1990
- Conditions that result in the mobilization and influx of Ca2+ into rat hepatocytes induce the rapid loss of 3-hydroxy-3-methylglutaryl-CoA reductase activity that is not reversed by phosphatase treatmentBiochemical Journal, 1990
- Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme.Journal of Biological Chemistry, 1988
- Regulation of hepatic HMG-CoA reductase in vivo by reversible phosphorylationBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1987
- Phosphorylation of HMG‐CoA reductase induced by mevalonate accelerates its rate of degradation in isolated rat hepatocytesFEBS Letters, 1986
- Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase synthesis by a non-sterol mevalonate-derived product in Mev-1 cells. Apparent translational control.Journal of Biological Chemistry, 1985
- Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzymeCell, 1985
- Phosphorylation of microsomal HMG CoA reductase increases susceptibility to proteolytic degradationBiochemical and Biophysical Research Communications, 1984
- Diurnal changes in the fraction of 3-hydroxy-3-methylglutaryl-CoA reductase in the active form in rat liver microsomal fractionsBiochemical Journal, 1984
- A cold-clamping technique for the rapid sampling of rat liver for studies on enzymes in separate cell fractions. Suitability for the study of enzymes regulated by reversible phosphorylation-dephosphorylationBiochemical Journal, 1984