Apr 25, 1976

Evidence for the coordinate control of activity of liver glycogen synthase and phosphorylase by a single protein phosphatase

The Journal of Biological Chemistry
S D KillileaW J Whelan

Abstract

Homogeneous rabbit liver phosphorylase phosphatase (Brandt, H., Capulong, Z. L., and Lee, E. Y. C. (1975) J. Biol. Chem. 250, 8038-8044) also dephosphorylates glycogen synthase b. During purification, phosphorylase phosphatase and glycogen synthase phosphatase co-purified with a constant ratio of activities. The two activities co-migrated on disc gel electrophoresis. Both substrates competed with each other for the phosphatase, and both phosphatase activities were inhibited by lysine ethyl ester. It is concluded that liver phosphorylase phosphatase and glycogen synthase phosphatase have a common identity and that coordinate regulation of the phosphatase-catalyzed activation of glycogen synthase and inactivation of phosphorylase occurs in vivo. This provides a parallel and opposing mechanism to that mediated by adenosine 3':5'-monophosphate-dependent protein kinase, which coordinately inactivates glycogen synthase and, via phosphorylase kinase, activates phosphorylase. Maximal glycogen synthase phosphatase activity was observed near neutrality. Mg2+ and glucose-6-P activated the glycogen synthase phosphatase reaction and this activation was pH-dependent. The Km for glycogen synthase b was 0.12 muM.

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Mentioned in this Paper

Phosphorylase Phosphatase
Phosphoric Monoester Hydrolases
Adenosine
MUC7 gene
Lysine
Phosphorylase Kinase
Electrophoresis, Disc
Phosphoric Monoester Hydrolase Activity
Protein KINASE
Urine Lysine Measurement

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