Effect of phosphorylation by different protein kinases on the behaviour of glycogen synthase as a substrate for hepatic synthase phosphatases

Mathieu Bollen, Maria Plana, Emilio Itarte, Willy Stalmans

Research output: Contribution to journalArticleResearchpeer-review

3 Citations (Scopus)

Abstract

Glycogen synthase a from skeletal muscle was phosphorylated in vitro and then used as substrate for the two major synthase phosphatases from liver. Synthase phosphorylated by cAMP-dependent protein kinase (1.4-1.7 P/subunit) was preferentially activated by the cytosolic S-component; in contrast, progressive phosphorylation by casein kinase-1 (0.9-6.5 P/subunit) yielded substrates that were always better dephosphorylated and activated by the glycogen-bound G-component. We have previously isolated from dog liver several types of synthase b that differ by their need for the S- and/or G-component for prompt activation. After additional phosphorylation by a mixture of synthase kinases the activation of these enzyme preparations required the presence of both components. © 1986 Academic Press, Inc.
Original languageEnglish
Pages (from-to)1033-1039
JournalBiochemical and Biophysical Research Communications
Volume139
DOIs
Publication statusPublished - 30 Sep 1986

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