Amino acid sequence at the site on rabbit skeletal muscle glycogen synthase phosphorylated by the endogenous glycogen synthase kinase‐2 activity

@article{Rylatt1979AminoAS,
  title={Amino acid sequence at the site on rabbit skeletal muscle glycogen synthase phosphorylated by the endogenous glycogen synthase kinase‐2 activity},
  author={Dennis B. Rylatt and Philip Cohen},
  journal={FEBS Letters},
  year={1979},
  volume={98}
}
Purified preparations of glycogen synthase (EC 2.4.1.11) have been shown to be contaminated with two types of protein kinase that phosphorylate the enzyme. One of these kinases was cyclic AMPdependent protein kinase (EC 2.7.1.37), while the other was an activity termed glycogen synthase kinase-2. The latter enzyme could be distinguished from cyclic AMP-dependent protein kinase in a number of ways. Its activity was unaffected by cyclic AMP or by the specific protein inhibitor of cyclic AMP… 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
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 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
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
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
Phosphorylation of glycogen synthase by cyclic AMP-independent glycogen synthases kinase-1 (GSK-1) comparative study with cyclic AMP-dependent protein kinase and phosphorylase kinase.
TLDR
It is reported that GSK-1 is able to phosphorylate at least four sites and that three of those sites are different from two of the three sites phosphorylated by cAMPdPK. Expand
Glycogen synthase kinase-3 from rabbit skeletal muscle.
TLDR
This chapter discusses glycogen synthase kinase-3 from rabbit skeletal muscle, which has a second activity that is not shared by any other protein kinase—namely, the ability to activate an enzyme termed the MgATP-dependent protein phosphatase. Expand
Glycogen Synthase from Rabbit Skeletal Muscle
TLDR
The results show that cyclic-AMP-dependent protein kinase, glycogen synthase kinase 3 and glycogen synthesis kinase 5 act as glycogen synthesase kinases in vivo. Expand
The calmodulin-dependent glycogen synthase kinase from rabbit skeletal muscle. Purification, subunit structure and substrate specificity.
TLDR
Glycogen synth enzyme kinase-4 is an enzyme that resembles the calmodulin-dependent glycogen synthase kinase in phosphorylating glycogens synthase (at site-2), but not glycogenosphorylase, that has lost its ability to be regulated by Ca2+-calmodulin. Expand
Amino-terminal sequence analysis of rat heart and muscle glycogen synthase: homology to the rabbit enzyme and the implications for hormonal control.
TLDR
Glycogen synthase was purified from rat heart and muscle and electroblotted from sodium dodecyl sulfate polyacrylamide gels to polyvinylidene difluoride, and the NH2-terminal amino acid sequence was determined, and two potentially important differences were observed. Expand
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References

SHOWING 1-10 OF 15 REFERENCES
Amino acid sequences at the two sites on glycogen synthetase phosphorylated by cyclic AMP‐dependent protein kinase and their dephosphorylation by protein phosphatase‐III
TLDR
Results indicated that the addition of both protein kinases resulted in the incorporation of almost two molecules of phosphate per subunit and the conversion of glycogen synthetase to a form, termed bl,2, which was almost completely inactive in the absence of glucosed-phosphate. 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
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
Effect of proteases on the structure and activity of rabbit skeletal muscle glycogen synthetase
TLDR
In the course of this work the amino acid sequence of the NH2 -terminal portion of the synthetase was determined and found to be slightly different from that reported, and it was noted that low levels of either trypsin or subtilisin cause some modification of theNH2 - terminal region of the Synthetase. Expand
The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver.
Synthetic peptides, representing part of the phosphorylatable site of rat liver pyruvate kinase, were phosphorylated by (32P)ATP and the catalytic subunit of cyclic AMP-stimulated protein kinase. TheExpand
Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.
TLDR
Findings support the idea that multiple basic residues, in particular arginine, on the NH,-terminal side of the phosphorylated serine act as important substrate specificity determinants for the protein kinase. Expand
The substrate specificity of cyclic AMP‐dependent protein kinase: Amino acid sequences at the phosphorylation sites of herring protamine (clupeine)
TLDR
In support of this hypothesis, a number of proteins that are likely to be physiological substrates for the enzyme have been identified and it has become apparent that the presence of two adjacent basic amino acids may be critical for specific substrate recognition in vivo. Expand
Structural studies on rabbit muscle glycogen synthase. I. Subunit composition.
Essentially glycogen-free, fully converted rabbit muscle glycogen synthase I and D forms were purified to a specific activity of 30 approximately 35 units/mg, higher than that previously reported.Expand
The purification and properties of rabbit skeletal muscle glycogen synthase.
Glycogen synthase a was purified over 500-fold by a procedure which involved solubilisation of the enzyme from a protein-glycogen complex by the action of endogenous phosphorylase and debranchingExpand
Amino‐terminal sequence of rabbit muscle phosphorylase
TLDR
The present communication describes both the nature of the amino-terminal blocking group and the amino acid sequence from the amino terminus through the phosphorylation site in rabbit muscle phosphorylase b and the corresponding sequence in dogfish phosphoryLase. Expand
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