Ca2+, calmodulin-dependent phosphorylation of glycogen synthase by a brain protein kinase

Takafumi Iwasa, Kohji Fukunaga, Hideyuki Yamamoto, Etsuro Tanaka, Eishichi Miyamoto

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

A Ca2+, calmodulin-dependent protein kinase from brain with a Mr of 640 000 is capable of phosphorylating glycogen synthase from skeletal muscle. The reaction was inhibited by the addition of 1 mM EGTA and 50 μM trifluoperazine, but not by protein kinase inhibitor and heparin. The amount of phosphate incorporated into glycogen synthase was 1.4 mol/mol subunit. The phosphorylation sites of glycogen synthase were cyanogen bromide-treated peptides CB-1 and CB-2 and only the seryl residue was phosphorylated.

Original languageEnglish
Pages (from-to)28-32
Number of pages5
JournalFEBS Letters
Volume161
Issue number1
DOIs
Publication statusPublished - 1983 Sep 5
Externally publishedYes

Keywords

  • Brain
  • Ca
  • Calmodulin-dependent protein kinase
  • Glycogen synthase
  • Protein phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Ca<sup>2+</sup>, calmodulin-dependent phosphorylation of glycogen synthase by a brain protein kinase'. Together they form a unique fingerprint.

Cite this