Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism.
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.
Garton
A J
AJ
Department of Biochemistry and Genetics, Medical School, University of Newcastle Upon Tyne, England.
Campbell
D G
DG
Carling
D
D
Hardie
D G
DG
Colbran
R J
RJ
Yeaman
S J
SJ
D000818:Animals; D001665:Binding Sites; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D008066:Lipolysis; D010748:Phosphopeptides / Q000302:isolation & purification; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism* / Q000494:pharmacology; D002787:Sterol Esterase / Q000378:metabolism*
D010748:Phosphopeptides; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002265:Carboxylic Ester Hydrolases; D002787:Sterol Esterase