Abstract
Glycogenin is the covalently bound protein found in muscle glycogen that it thought to be the primer for glycogen synthesis. We now report that glycogenin contains a phosphoserine residue. From a less than stoichiometric amount of phosphate in glycogenin as isolated, the content may be increased to one molecular proportion, using the catalytic subunit of cAMP-dependent protein kinase. The phosphoserine residue is present within a hitherto-undescribed amino acid sequence. In particular, the serine is not flanked by arginine, previously thought to be an essential adjunct for a serine residue to act as substrate for this kinase. We suggest that the serine phosphate may represent a means of regulating the ability of glycogenin to prime glycogen synthesis.
Original language | English (US) |
---|---|
Pages (from-to) | 261-264 |
Number of pages | 4 |
Journal | BioFactors |
Volume | 1 |
Issue number | 3 |
State | Published - 1988 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Clinical Biochemistry