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

TY - JOUR

T1 - Phosphorylation of the glycogen-binding subunit of protein phosphatase-1G in response to adrenalin

AU - MacKintosh, Carol

AU - Campbell, David G.

AU - Hiraga, Akira

AU - Cohen, Philip

PY - 1988

Y1 - 1988

N2 - 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

AB - 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

U2 - 10.1016/0014-5793(88)81331-0

DO - 10.1016/0014-5793(88)81331-0

M3 - Article

SN - 0014-5793

VL - 234

SP - 189

EP - 194

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -