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 |
|---|---|
| Pages (from-to) | 261-264 |
| Number of pages | 4 |
| Journal | BioFactors |
| Volume | 1 |
| Issue number | 3 |
| State | Published - Jan 1 1988 |
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ASJC Scopus subject areas
- Biochemistry
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The occurrence of serine phosphate in glycogenin : A possible regulatory site. / Lomako, J.; Whelan, William J.
In: BioFactors, Vol. 1, No. 3, 01.01.1988, p. 261-264.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The occurrence of serine phosphate in glycogenin
T2 - A possible regulatory site
AU - Lomako, J.
AU - Whelan, William J.
PY - 1988/1/1
Y1 - 1988/1/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0023798570&partnerID=8YFLogxK
M3 - Article
C2 - 3151442
AN - SCOPUS:0023798570
VL - 1
SP - 261
EP - 264
JO - BioFactors
JF - BioFactors
SN - 0951-6433
IS - 3
ER -