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}
}
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.
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.
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.
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.
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.
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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.
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. The
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.
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 debranching
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