Phosphorylation of glycogen synthase and of the beta subunit of eukaryotic initiation factor two by a common protein kinase.

Abstract A protein kinase from rabbit reticulocytes, able to phosphorylate the beta subunit of eukaryotic initiation factor 2 (eIF-2), has been demonstrated to phosphorylate also glycogen synthase. A glycogen synthase kinase (PC0.7) from rabbit skeletal muscle has been shown to phosphorylate the beta subunit of eIF-2. Comparison of highly purified preparations of the two protein kinases has indicated several similarities of properties. 1) Both enzymes were associated with two major polypeptide species, alpha (Mr = 43,000) and beta (Mr = 25,000), and exhibited apparent native molecular weights of 176,000-180,000 by gel filtration and 130,000-140,000 by sucrose density gradient sedimentation. 2) Both enzymes phosphorylated glycogen synthase, eIF-2 beta, phosvitin, and casein and were effective in utilizing GTP and ATP as phosphoryl donors. 3) Both enzymes displayed the same chromatographic behavior on phosvitin-Sepharose, phosphocellulose, and DEAE-cellulose. 4) Both enzymes underwent an autophosphorylation of the beta polypeptide when incubated with ATP and Mg2+. On the basis of these and other properties, we propose that the two protein kinases, if not identical, are very similar enzymes.