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FEBS Lett. 1988 Jul 4;234(1):189-94.

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

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1
Department of Biochemistry, University of Dundee, Scotland.

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.

PMID:
2839360
DOI:
10.1016/0014-5793(88)81331-0
[Indexed for MEDLINE]
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