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 Lettjournal_title
FEBS lettersauthors
MacKintosh C,Campbell DG,Hiraga A,Cohen Pdoi
10.1016/0014-5793(88)81331-0subject
Has Abstractpub_date
1988-07-04 00:00:00pages
189-94issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(88)81331-0journal_volume
234pub_type
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