Phosphoserine as a recognition determinant for glycogen synthase kinase-3: phosphorylation of a synthetic peptide based on the G-component of protein phosphatase-1.

@article{Fiol1988PhosphoserineAA,
  title={Phosphoserine as a recognition determinant for glycogen synthase kinase-3: phosphorylation of a synthetic peptide based on the G-component of protein phosphatase-1.},
  author={C. Fiol and J. H. Haseman and Y. Wang and P. Roach and R. Roeske and M. Kowalczuk and A. Depaoli-Roach},
  journal={Archives of biochemistry and biophysics},
  year={1988},
  volume={267 2},
  pages={
          797-802
        }
}
Prior phosphorylation of its substrate has been shown to be important for substrate recognition by the protein kinase glycogen synthase kinase-3 (GSK-3). Phosphorylation of glycogen synthase by GSK-3 is known to be enhanced by the previous action of casein kinase II and the sequence -SXXXS(P)- was proposed as the minimal recognition determinant for GSK-3. The glycogen binding subunit of type 1 phosphoprotein phosphatase has been shown to be phosphorylated by cyclic AMP-dependent protein kinase… Expand
GSK-3: tricks of the trade for a multi-tasking kinase
The structure, role, and regulation of type 1 protein phosphatases.
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