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PMID: 2168324 Published · ppublish English Journal Article

Control of glycogen synthase by hierarchal protein phosphorylation.

Roach PJ

Abstract

Protein phosphorylation is one of the most common mechanisms for controlling protein function. We now know that most phosphoproteins contain multiple phosphorylation sites and that these sites are often located in clusters. From the study of the enzyme glycogen synthase, one mechanism for the formation of phosphorylation clusters has been discovered that involves the concerted action of two or more protein kinases. One protein kinase, the primary kinase, introduces a phosphate group that is a requirement for the action of another, secondary, protein kinase. Thus the multiple phosphorylation occurs in a hierarchal fashion. This mechanism, which is critical for the phosphorylation of glycogen synthase, is likely to be a much more widespread phenomenon.

MeSH Terms
Animals Calcium-Calmodulin-Dependent Protein Kinases Chemical Phenomena Chemistry Glycogen Synthase/biosynthesis,metabolism Humans Liver/enzymology Muscles/enzymology Phosphorylation Protein Kinases/metabolism Rabbits Rats
Chemicals
Glycogen Synthase Protein Kinases Calcium-Calmodulin-Dependent Protein Kinases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Roach P J
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46223.
Article Info
Journal
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
Abbr.
FASEB J
ISSN
0892-6638
Published
1990-09-00
Pages
2961-8
Language
English
Region
United States
NLM ID
8804484
Subset
IM
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