Abstract
Glycogen synthase kinase-5 (casein kinase-II) phosphorylates glycogen synthase on a serine termed site 5. This residue is just C-terminal to the 3 serines phosphorylated by glycogen synthase kinase-3, which are critical for the hormonal regulation of glycogen synthase in vivo. Although phosphorylation of site 5 does not affect the catalytic activity, it is demonstrated that this modification is a prerequisite for phosphorylation by glycogen synthase kinase-3. Since site 5 is almost fully phosphorylated in vivo under all conditions, the role of glycogen synthase kinase-5 would appear to be a novel one in forming the recognition site for another protein kinase.
Original language | English |
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Pages (from-to) | 191-196 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 150 |
Issue number | 1 |
DOIs | |
Publication status | Published - 13 Dec 1982 |
Keywords
- Adrenalin
- Calmodulin
- Casein kinase
- Cyclic AMP
- Glycogen synthase
- Insulin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology