1979
DOI: 10.1111/j.1432-1033.1979.tb04176.x
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Glycogen Synthase Kinase-2 and Phosphorylase Kinase Are the Same Enzyme

Abstract: Homogeneous preparations of phosphorylase kinase from rabbit skeletal muscle catalyse a calcium-dependent phosphorylation of glycogen synthase a isolated from the same tissue. The calcium-dependent glycogen synthase kinase activity copurifies with phosphorylase kinase throughout the standard procedure for the isolation of the latter enzyme. At the final step of the purification, gel filtration on Sepharose 4B, the elution profiles for glycogen synthase kinase and phosphorylase kinase activities are identical. … Show more

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Cited by 112 publications
(45 citation statements)
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“…GSK3B is a serine-threonine kinase [23,24] involved in the regulation of important intracellular signaling pathways, including cell cycle, gene expression and apoptosis [25][26][27] . In neurons, GSK3B is a major Tau kinase, critically involved in the maintenance of the stability of microtubules and, therefore, in the preservation of the structure and function of the neuronal cytoskeleton [28] .…”
Section: Glycogen Synthase Kinase and Taumentioning
confidence: 99%
“…GSK3B is a serine-threonine kinase [23,24] involved in the regulation of important intracellular signaling pathways, including cell cycle, gene expression and apoptosis [25][26][27] . In neurons, GSK3B is a major Tau kinase, critically involved in the maintenance of the stability of microtubules and, therefore, in the preservation of the structure and function of the neuronal cytoskeleton [28] .…”
Section: Glycogen Synthase Kinase and Taumentioning
confidence: 99%
“…1 1 . Gas-phase sequencer analysis of the S-ethylcysteinyl derivative produced from the phosphorylated form of the peptide C85 -C96 from adrenalin-treated animals. The figure shows reverse-phase chromatograms of Pth derivatives corresponding to residues C86-C9S (Edman cycles [2][3][4][5][6][7][8][9][10][11]. The cysteine at position 4 was identified by the appearance of a characteristic peak which is either a breakdown product or an adduct of this amino acid.…”
Section: The Peptide C98 -C124mentioning
confidence: 99%
“…1. In the N-terminal domain, residue N7 was phosphorylated in vitro by the calmodulin-dependent multiprotein kinase [3 -51, phosphorylase kinase [6,7], cyclic-AMP-dependent protein kinase [8] and glycogen synthase kinase-4 [9]. In the C-terminal domain, glycogen synthase kinase-3 phosphorylated three residues C30, C34 and C38, all contained within the same tryptic peptide [lo], while casein kinase-11 labelled residue C46 [9].…”
mentioning
confidence: 99%
“…CaM-kinase II catalyses the phosphorylation of muscle glycogen synthase primarily at site 2, with limited phosphorylation at site lb [16,17,90], resulting in partial inactivation of the enzyme [8,15,16]. Two other calcium-dependent protein kinases can also phosphorylate glycogen synthase in vitro, namely phosphorylase kinase (site 2) [91,92] and protein kinase C (sites 1 a and 2) [93]. More recent results indicate that the liver isoenzyme of glycogen synthase is similar to the skeletal muscle isoenzyme in terms of its phosphorylation, except for the apparent lack of sites 1 a and lb [94].…”
Section: Species Tissue and Subcellular Distributionmentioning
confidence: 99%