Phosphorylation of Bovine Hormone-Sensitive Lipase by the AMP-activated Protein Kinase. A Possible Antilipolytic Mechanism

Eur J Biochem. 1989 Jan 15;179(1):249-54. doi: 10.1111/j.1432-1033.1989.tb14548.x.

Abstract

Hormone-sensitive lipase is phosphorylated at a single site (site 2) in vitro by the AMP-activated protein kinase, without any direct effect on the activity of the enzyme. The amino acid sequence around this site has been determined. Ca2+/calmodulin-dependent protein kinase II also phosphorylates hormone-sensitive lipase predominantly at this site, whilst cyclic-GMP-dependent protein kinase phosphorylates exclusively the regulatory site (site 1) which is also phosphorylated by cyclic-AMP-dependent protein kinase. Phosphorylation of site 2 has been found to inhibit subsequent phosphorylation and activation of hormone-sensitive lipase by the cyclic-AMP-dependent and cyclic-GMP-dependent protein kinases, indicating that site-2 phosphorylation may have an antilipolytic role in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Carboxylic Ester Hydrolases / metabolism*
  • Cattle
  • Chromatography, High Pressure Liquid
  • Lipolysis*
  • Phosphopeptides / isolation & purification
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Protein Kinases / pharmacology
  • Sterol Esterase / metabolism*

Substances

  • Phosphopeptides
  • Protein Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Carboxylic Ester Hydrolases
  • Sterol Esterase