Amino acid sequences at the two sites on glycogen synthetase phosphorylated by cyclic AMP‐dependent protein kinase and their dephosphorylation by protein phosphatase‐III

@article{Proud1977AminoAS,
  title={Amino acid sequences at the two sites on glycogen synthetase phosphorylated by cyclic AMP‐dependent protein kinase and their dephosphorylation by protein phosphatase‐III},
  author={Christopher G. Proud and Dennis B. Rylatt and Stephen J. Yeaman and Philip Cohen},
  journal={FEBS Letters},
  year={1977},
  volume={80}
}
It has been established that glycogen synthetase activity in skeletal muscle can be regulated by two distinct protein kinases. One of these is cyclic AMPdependent protein kinase, while the other is an enzyme termed glycogen synthetase kinase-2 [ 1,2] . The phosphorylation of glycogen synthetase a in vitro by either kinase in the presence of ATP-Mg was found to reach a plateau when about one molecule of phosphate had been incorporated per subunit, and the resulting enzyme species were more… Expand
Amino acid sequence at the site on rabbit skeletal muscle glycogen synthase phosphorylated by the endogenous glycogen synthase kinase‐2 activity
TLDR
The endogenous glycogen synthase kinase-2 activity, preferentially phosphorylates a serine residue distinct from either of the sites labelled by cyclic AMP-dependent protein kinase. Expand
Amino acid sequence of a region in rabbit skeletal muscle glycogen synthase phosphorylated by cyclic AMP‐dependent protein kinase
TLDR
This analysis has surprisingly demonstrated that sites-l a and 1 b are separated by only 13 amino acids in the primary structure of glycogen synthase, which comprises -770 residues. Expand
The substrate specificity and regulation of the protein phosphatases involved in the control of glycogen metabolism in mammalian skeletal muscle.
TLDR
Glycogen metabolism in mammalian skeletal muscle is controlled by protein phosphorylation and dephosphorylation reactions which involve three protein kinases and two protein phosphatases, and the possible physiological roles of inhibitor-1 and inhibitor-2 are discussed. Expand
A reinvestigation of the phosphorylation of rabbit skeletal-muscle glycogen synthase by cyclic-AMP-dependent protein kinase. Identification of the third site of phosphorylation as serine-7.
TLDR
Glycogen synthase preparations which were free of endogenous phosphorylase kinase were phosphorylated to different extents with cyclic-AMP-dependent protein kinase and the phosphopeptides obtained by tryptic digestion were analysed, concluding that site 2 is the only site at which overlapping substrate specificity occurs between these three glycogen synthases. Expand
Glycogen synthase kinase-2 and phosphorylase kinase are the same enzyme.
TLDR
Evidence is presented which demonstrates that glycogen synthase-2 is merely a modified form of phosphorylase kinase which has lost its ability to be regulated by calcium ions at pH 6.8, and the implications of these findings are considered. Expand
Isolation and characterization of cyclic AMP-independent glycogen synthase kinase from rat skeletal muscle.
TLDR
Glycogen synthase kinase was isolated from rat skeletal muscle and the phosphorylation and inactivation catalyzed by glycogen synthases was compared to that catalyzing by cyclic AMP-dependent protein kinase or phosphorylase kinases, which had different specificities for phosphorylated sites on glycogen synthease. Expand
Phosphorylation of glycogen synthase by phosphorylase kinase
TLDR
It is shown that the presence of phosphorylase inhibits the inactivation of glycogen synthase by phosphORYlase kinase and that the phosphorylation site in the trypsin-insensitive domain is preferentially phosphorylated by the CAMP-dependent protein kinase. Expand
The role of cyclic-AMP-dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle.
  • P. Cohen
  • Chemistry, Medicine
  • Current topics in cellular regulation
  • 1978
TLDR
The role of cyclic-AMP-dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle is discussed, which determines the time at which dephosphorylation of the β subunit and inactivation of the enzyme can become rapid through phosphorylations of the α subunit. Expand
Phosphorylation of rabbit skeletal muscle glycogen synthase 1 by the cAMP dependent protein kinase, the cAMP independent synthase kinase and the phosvitin kinase from human polymorphonuclear leukocytes
TLDR
It is suggested that within the first P1subunit phosphorylation in the trypsin insensitive region determine the affinity for the allosteric activator, glucose-6-phosphate, which is the major determinant in rabbit skeletal muscle glycogen synthase I. Expand
Glycogen synthase kinase‐2 from rabbit skeletal muscle is activated by the calcium‐dependent regulator protein
TLDR
It is demonstrated that the phosphorylation of ~lycogen synthases by endogenous glycogen synthase kinase-2 is markedly stimulated by the c~cium-dependent regulator protein (termed CDR) in the presence of Car, suggesting the possibility that this enzyme could represent a mechanism for the regulation of glycogen synthesis activity in response to nervous stimulation. Expand
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The hormonal control of glycogen metabolism: The amino acid sequence at the phosphorylation site of protein phosphatase inhibitor‐1
Glycogen metabolism in skeletal muscle is controlled by a regulatory network which involves three protein kinases and two protein phosphatases (fig.1 and ref. [l] for recent review). The conversionExpand
The phosphorylation of rabbit skeletal muscle glycogen synthase by glycogen synthase kinase-2 and adenosine-3':5'-monophosphate-dependent protein kinase.
TLDR
The results indicate that glycogen synthase can be regulated by two distinct phosphorylation-dephosphorylation cycles, and the implication of these findings for the regulation of glycogens synthase in vivo are discussed. Expand
Glycogen synthetase kinase 2 (GSK 2); The identification of a new protein kinase in skeletal muscle
TLDR
Theoretically, the elevation of synthetase I levels by insulin could be achieved in one of three different ways, and it is unlikely that the effect is explainable in terms of an inactivation of cyclic AMP dependent protein kinase resulting from a decreased availability of cyclIC AMP. Expand
CYCLIC AMP AND HISTONE PHOSPHORYLATION *
  • T. Langan
  • Chemistry, Medicine
  • Annals of the New York Academy of Sciences
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TLDR
The interpretation that the phosphoserine found in histone preparations represents, at least in part, phosphorylated histone was favored by the findings that tissues contain a rather specific protein kinase which catalyzes the phosphorylation of histones and also of the functionally homologous basic proteins of certain fish sperm, the protamines. Expand
Comparison of the substrate specificities of protein phosphatases involved in the regulation of glycogen metabolism in rabbit skeletal muscle.
TLDR
It is suggested that a single protein phosphatase (protein phosphatases-III) catalyses each of the dephosphorylation reactions that inhibit glycogenolysis or stimulate glycogen synthesis. Expand
Separation of two phosphorylase kinase phosphatases from rabbit skeletal muscle.
TLDR
The two phosphatases copurified through ethanol fractionation, DEAE-cellulose chromatography and ammonium sulphate precipitation, but were separated from each other by a gel filtration on Sephadex G-200. Expand
Specificity of a protein phosphatase inhibitor from rabbit skeletal muscle.
TLDR
The results suggest that theprotein phosphatase inhibitor may be a useful probe for differentiating different classes of protein phosphatases in mammalian cells. Expand
GLYCOGEN SYNTHETASE ACTIVITY IN SKELETAL MUSCLE. INTERCONVERSION OF TWO FORMS AND CONTROL OF GLYCOGEN SYNTHESIS.
  • W. Danforth
  • Biology, Medicine
  • The Journal of biological chemistry
  • 1965
TLDR
The present paper describes the interconversion of these two forms of glycogen synthetase in living muscle in response to physiological stimuli and shows that the two forms are regulated in such a way as to hasten glycogen synthesis when the tissue concentration of glucose-6-P is low, and to slow glycogenhesis when the tissues concentration is elevated. Expand
Purification and Characterization of a Protein Inhibitor of Adenosine 3',5'-Monophosphate-dependent Protein Kinases
TLDR
A kinetic analysis of the effect of the inhibitor on the phosphorylation of casein by skeletal muscle protein kinase indicates that it interacts noncompetitively with respect to ATP, the protein substrate, and adenosine 3',5'-monophosphate. Expand
The substrate specificity of adenosine 3':5'-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle.
TLDR
The amino acid sequences when compared with those at the phosphorylation sites of other physiological substrates suggest that the presence of two adjacent basic amino acids on the N-terminal side of the susceptible serine residue may be critical for specific substrate recognition in vivo. Expand
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