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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

MacKintosh C,Campbell DG,Hiraga A,Cohen P

doi

10.1016/0014-5793(88)81331-0

subject

Has Abstract

pub_date

1988-07-04 00:00:00

pages

189-94

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(88)81331-0

journal_volume

234

pub_type

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