Phosphorylation site specificities of glycogen synthase kinases: Determination by peptide mapping using high-performance liquid chromatography

Henning Juhl, Virender S. Sheorain, Charles M. Schworer, Mary Frances Jett, Thomas R. Soderling

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

A method is described which separates the various phosphorylation sites in glycogen synthase based on reverse phase high-performance liquid chromatography (HPLC) of tryptic 32P-peptides. Using this method we studied the phosphorylation site specificities of the kinases which act on glycogen synthase. The cAMP-dependent protein kinase phosphorylated sites 1a, 1b, and 2, whereas casein kinase II phosphorylated only site 5. Two calcium, calmodulin-dependent kinases, phosphorylase kinase and liver calmodulin-dependent synthase kinase, both phosphorylated site 2, and the latter enzyme also phosphorylated site 1b. A cAMP-independent kinase (kinase 4) purified from liver also specifically phosphorylated site 2. Synthase kinase 3 catalyzed the phosphorylation of only site 3. This HPLC method was also used to establish that all of these sites were subject to phosphorylation in vivo.

Original languageEnglish (US)
Pages (from-to)518-526
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume222
Issue number2
DOIs
StatePublished - Apr 15 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Fingerprint

Dive into the research topics of 'Phosphorylation site specificities of glycogen synthase kinases: Determination by peptide mapping using high-performance liquid chromatography'. Together they form a unique fingerprint.

Cite this