Substrate specificity of liver calmodulin-dependent glycogen synthase kinase.
A number of proteins were tested as potential substrates for purified rabbit liver calmodulin-dependent glycogen synthase kinase. It was found that liver phenylalanine hydroxylase and several brain proteins including tyrosine hydroxylase, microtubule-associated protein 2, and synapsin I were readily phosphorylated. Brain tubulin was very poorly phosphorylated. These results suggest that calmodulin-dependent glycogen synthase kinase may be a more general protein kinase involved in the regulation of several cellular Ca2+-dependent functions.
D000818:Animals; D001921:Brain / Q000201:enzymology; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002147:Calmodulin / Q000378:metabolism*; D038341:Glycogen Synthase Kinases; D008099:Liver / Q000201:enzymology*; D008869:Microtubule-Associated Proteins; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010651:Phenylalanine Hydroxylase / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D011817:Rabbits; D013379:Substrate Specificity; D016704:Synapsins; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism
D002147:Calmodulin; D008869:Microtubule-Associated Proteins; D009419:Nerve Tissue Proteins; D011506:Proteins; D016704:Synapsins; D010651:Phenylalanine Hydroxylase; D014446:Tyrosine 3-Monooxygenase; D011494:Protein Kinases; D038341:Glycogen Synthase Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases