Discovery - University of Dundee - Online Publications

Library & Learning Centre

Phosphorylation of the glycogen-binding subunit of protein phosphatase-1G in response to adrenalin

Phosphorylation of the glycogen-binding subunit of protein phosphatase-1G in response to adrenalin

Research output: Contribution to journalArticle

View graph of relations

Info

Original languageEnglish
Pages189-194
Number of pages6
JournalFEBS Letters
Journal publication date1988
Journal number1
Volume234
DOIs
StatePublished

Abstract

The glycogen-binding (G) subunit of protein phosphatase-1 is phosphorylated in vivo. In rabbits injected with propranolol the serine residue termed site-1 was phosphorylated in 56% of the molecules isolated, and phosphorylation increased to 82% after administration of adrenalin. It is concluded that the G-subunit is a physiological substrate for cyclic AMP-dependent protein kinase. The G-subunit remained largely bound to glycogen even after injection of adrenalin, whereas half of the protein phosphatase-1 activity associated with glycogen was released into the cytosol. The results indicate that adrenalin induces dissociation of the catalytic subunit from the G-subunit in vivo

Documents

Library & Learning Centre

Contact | Accessibility | Policy