Phosphorylation of the basal site of hormone-sensitive lipase by glycogen synthase kinase-4.
In rat adipocytes hormone-sensitive lipase is phosphorylated at two sites termed 'regulatory' and 'basal', in the former case by cyclic AMP-dependent protein kinase causing an activation of the lipase [(1984) Proc. Natl. Acad. Sci. USA 81, 3317-3321]. Here, the basal phosphorylation site was found to be phosphorylated by glycogen synthase kinase-4 without any effects on lipase activity, or on the extent of its activation subsequent to phosphorylation of the regulatory site. Glycogen synthase kinase-3, casein kinase-I, and casein kinase-II did not phosphorylate the lipase. Phosphorylase kinase phosphorylated it to a very low extent at a third phosphorylation site not phosphorylated in the fat cell.
D000273:Adipose Tissue / Q000201:enzymology; D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D038341:Glycogen Synthase Kinases; D006728:Hormones / Q000494:pharmacology; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D010764:Phosphorylase Kinase / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits; D002787:Sterol Esterase / Q000378:metabolism*
D006728:Hormones; D011494:Protein Kinases; D010764:Phosphorylase Kinase; D038341:Glycogen Synthase Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002787:Sterol Esterase