Control of glycogen synthase by hierarchal protein phosphorylation

Research output: Contribution to journalReview article

182 Scopus citations

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 phenome non.

Original languageEnglish (US)
Pages (from-to)2961-2968
Number of pages8
JournalFASEB Journal
Volume4
Issue number12
StatePublished - Dec 4 1990

Keywords

  • Glycogen metabolism
  • Isozyme
  • Mutagenesis
  • Phosphoprotein
  • Phosphorylation site
  • Protein kinase
  • Synthetic peptides

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

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