Substrate specificity of liver calmodulin-dependent glycogen synthase kinase

Charles M. Schworer, Thomas Soderling

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

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
Volume116
Issue number2
DOIs
StatePublished - Oct 31 1983
Externally publishedYes

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Glycogen Synthase Kinases
Calmodulin
Substrate Specificity
Liver
Brain
Synapsins
Phenylalanine Hydroxylase
Microtubule-Associated Proteins
Tyrosine 3-Monooxygenase
Substrates
Tubulin
Protein Kinases
Proteins
Rabbits

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Substrate specificity of liver calmodulin-dependent glycogen synthase kinase. / Schworer, Charles M.; Soderling, Thomas.

In: Biochemical and Biophysical Research Communications, Vol. 116, No. 2, 31.10.1983, p. 412-416.

Research output: Contribution to journalArticle

Schworer, Charles M. ; Soderling, Thomas. / Substrate specificity of liver calmodulin-dependent glycogen synthase kinase. In: Biochemical and Biophysical Research Communications. 1983 ; Vol. 116, No. 2. pp. 412-416.
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