Substrate specificity of liver calmodulin-dependent glycogen synthase kinase

Charles M. Schworer, Thomas R. Soderling

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


A number of proteins were tested as potential substrates for purified rabbit liver calmodulin-dependent glycogen synthase kinase. It was found that liver phenylalanine hydroxylase and several brain proteins including tyrosine hydroxylase, microtubule-associated protein 2, and synapsin I were readily phosphorylated. Brain tubulin was very poorly phosphorylated. These results suggest that calmodulin-dependent glycogen synthase kinase may be a more general protein kinase involved in the regulation of several cellular Ca2+-dependent functions.

Original languageEnglish (US)
Pages (from-to)412-416
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Oct 31 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Substrate specificity of liver calmodulin-dependent glycogen synthase kinase'. Together they form a unique fingerprint.

Cite this