Multisite phosphorylation of the glycogen-binding subunit of protein phosphatase-1G by cyclic AMP-dependent protein kinase and glycogen synthase kinase-3.

Abstract:

:The glycogen-binding (G) subunit of protein phosphatase-1G is phosphorylated stoichiometrically by glycogen synthase kinase-3 (GSK3), and with a greater catalytic efficiency than glycogen synthase, but only after prior phosphorylation by cyclic AMP-dependent protein kinase (A-kinase) at site 1. The residues phosphorylated are the first two serines in the sequence AIFKPGFSPQPSRRGS-, while the C-terminal serine (site 1) is one of the two residues phosphorylated by A-kinase. These findings demonstrate that (i) the G subunit undergoes multisite phosphorylation in vitro; (ii) phosphorylation by GSK3 requires the presence of a C-terminal phosphoserine residue; (iii) GSK3 can synergise with protein kinases other than casein kinase-2.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Dent P,Campbell DG,Hubbard MJ,Cohen P

doi

10.1016/0014-5793(89)80433-8

subject

Has Abstract

pub_date

1989-05-08 00:00:00

pages

67-72

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(89)80433-8

journal_volume

248

pub_type

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